Belongs to the FPP/GGPP synthase family.
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, using ferredoxin I (PetF) as the reducing agent.
Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Belongs to the complex I 30 kDa subunit family.
NDH-1 can be composed of about 15 different subunits; different subcomplexes with different compositions have been identified which probably have different functions.
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Belongs to the cytochrome c family. PsbV subfamily.
Binds 1 heme c group covalently per monomer.
Present at very low levels (at protein level) (PubMed:12881497).
Probable low-potential cytochrome c, can partially replace cytochrome c-550 (PsbV) function.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
Part of the ABC transporter complex (TC 3.A.1.6.1) involved in sulfate/thiosulfate import.
Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (CysA), two transmembrane proteins (CysT and CysW) and a solute-binding protein (CysP).
Belongs to the bacterial sugar transferase family.
Belongs to the SAICAR synthetase family.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Belongs to the methyltransferase superfamily. RsmI family.
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family. DTD3 subfamily.
Binds 2 divalent metal cations per subunit.
Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr).
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
In the C-terminal section; belongs to the transposase 35 family.
In the N-terminal section; belongs to the transposase 2 family.
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center.
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Monomer. Binds directly to the core enzyme of the DNA-dependent RNA polymerase and to nascent RNA.
Participates in both transcription termination and antitermination.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Binds oxidized quinones via the N-terminal PsR domain, allowing it to sense redox changes and possibly mediate clock input.
Homodimer (Probable) (PubMed:28302851). The KaiABC complex composition changes during the circadian cycle to control KaiC phosphorylation. Complexes KaiC(6), KaiA(2-4):KaiC(6), KaiB(6):KaiC(6) and KaiC(6):KaiB(6):KaiA(12) are among the most important forms, many form cooperatively (PubMed:28302851). Binds to KaiB and KaiC, the N-terminus (pseudoreceiver domain PsR) is not required for either interaction. 1 KaiB binds to one subunit of the KaiA homodimer. KaiA and CikA bind to the same region of the KaiB(fs) form and therefore compete (PubMed:24112939, PubMed:28302851).
Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII domain during the subjective day yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB during the subjective night to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding on KaiB that sequesters KaiA from KaiC's CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex resulting in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator (By similarity). Formation of the KaiB:KaiC complex is promoted by KaiA, helping switch KaiC from its autophosphorylation to autodephosphatase function (PubMed:24112939).
The KaiA C-terminal domain mediates homodimerization and formation of a stable complex with KaiB and KaiC. The N-terminal pseudoreceiver domain (PsR, residues 1-146 in these experiments) is not necessary for most KaiA functions, while the linker region (residues 147-179) between the 2 domains is probably required at least for KaiA:KaiB interaction (PubMed:24112939, PubMed:28302851). Undergoes large conformational changes in the KaiABC complex which inactivates the second KaiA monomer, preventing it from activating the KaiC CII domain (PubMed:28302851). The PsR domain binds oxidized quinones (By similarity).
Belongs to the anhydro-N-acetylmuramic acid kinase family.
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
NDH-1 shuttles electrons from NAD(P)H, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the CobB/CobQ family. CobQ subfamily.
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Homotetramer. Forms heterodimers with either ThiH or ThiS.
A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product.
Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily.
Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
CpcE and CpcF associate to form a lyase.
Required for the chromophorylation of the CpcA gene product.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Belongs to the glycosyltransferase 10 family.
Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
The beta-hairpin motif is involved in DNA binding.
Homodimer which binds Holliday junction (HJ) DNA. The HJ becomes 2-fold symmetrical on binding to RuvC with unstacked arms; it has a different conformation from HJ DNA in complex with RuvA. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Belongs to the complex I NdhO subunit family.
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration (By similarity).
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Also functions in a two-component CikA/RpaA output pathway from the circadian clock, negatively regulating kaiBC expression independently of labA and of sasA. One of three clock output pathways. Dephosphorylates phospho-RpaA, enhanced by KaiB and KaiC, has only modest kinase activity on RpaA.
Functions in an input pathway to the Kai circadian clock. Senses oxidized quinones via its C-terminal pseudo-receiver domain, providing a link between cell metabolism and the clock. Affects the ratio of phosphorylated to unphosphorylated KaiC, binds quinones via its pseudo-receptor domain. Quinone-binding destabilizes the protein rapidly. Autophosphorylates, does not transfer the phosphate to its pseudo-receiver (PsR) domain. May play a role in cell division.
Homodimer. Part of the circadian clock (KaiA, KaiB, KaiC, CikA, RpaA, SasA), the composition of which varies during the circadian cycle. KaiA and CikA compete for binding to KaiB(fs) (By similarity). The PsR domain binds the KaiB:KaiC CI complex but poorly to either protein alone. KaiA and CikA bind to the same region of the KaiB(fs) form and therefore compete (PubMed:28302851).
In the N-terminal section; belongs to the phytochrome family.
The N-terminal domain is followed by a GAF (phytochrome-like) domain that lacks the conserved Cys residue for ligand binding, a histidine kinase domain and a C-terminal response regulator domain without the conserved Asp residue that is phosphorylated (pseudo-receiver domain, PsR).
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA (By similarity).
Homodimer. Interacts with FtsZ (By similarity).
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Belongs to the ribulose-phosphate 3-epimerase family.
Binds 1 divalent metal cation per subunit.
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal subunits or 70S ribosomes.
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Belongs to the phycobilisome linker protein family.
Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Belongs to the SurE nucleotidase family.
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Binds 1 pyridoxal phosphate per subunit.
May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
Belongs to the polyribonucleotide nucleotidyltransferase family.
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family.
Ca(+)/H(+) antiporter that extrudes calcium in exchange for external protons.
Lacks conserved residue(s) required for the propagation of feature annotation.
Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits.
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Homohexamer. The oligomerization is ATP-dependent.
Belongs to the LeuD family. LeuD type 1 subfamily.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the RuBisCO small chain family.
Heterohexadecamer of 8 large and 8 small subunits.
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
RuBisCO folding and assembly commences when the nascent large subunit folds with the help of chaperonin GroEL-GroES. Both RbcX and Raf1 help folded RbcL release from the chaperonin and dimerize (Probable). Dimeric Raf1 binds to RbcL(2) leading to an RbcL8-Raf1(8) complex. RbcS displaces Raf1, resulting in holoenzyme formation (By similarity).
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Belongs to the IPP isomerase type 2 family.
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.
According to (Ref.2, PubMed:22665786, PubMed:23413188, PubMed:25006873) there are no direct protein ligands to pheophytin D2, whereas (PubMed:14764885, PubMed:16355230, PubMed:19219048, PubMed:20558739, PubMed:21367867, PubMed:25043005) show 1 or 2 direct ligands.
Belongs to the reaction center PufL/M/PsbA/D family.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. Part of a photosystem II (PSII) assembly intermediate complex PSII-I; crystallized from a strain deleted of psbJ, it forms monomeric PSII before addition of the oxygen evolving complex. PSII-I includes 3 assembly factors not found in mature PSII (Psb27, Psb28 and Psb34) (PubMed:33846594).
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution (PubMed:19219048, PubMed:21367867). PSII binds additional chlorophylls, carotenoids and specific lipids.
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Heterotetramer of two alpha and two beta chains.
Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
Belongs to the disproportionating enzyme family.
Binds 2 Mg(2+) ions per subunit, one in each domain. Mg(2+) is required for hexamerization and phosphatase activity.
Central component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. Clock output pathways impact the RpaA transcriptional regulator. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. KaiB and KaiC together enhance the phospho-RpaA dephosphatase activity of CikA.
Has a weak, temperature-independent ATPase activity (about 14 molecules of ATP per day) that defines the circadian period (PubMed:28302851, PubMed:34618577). ATPase activity is mostly contributed by the CI domain; the CII domain augments the activity. The addition of KaiA increases activity. ATPase is inhibited during the KaiC phosphorylating phase and activated during the KaiC dephosphorylating phase (PubMed:35507871).
Homohexamer resembling 2 stacked donuts rings with a central pore nearly blocked on one side; hexamerization is dependent on ATP-binding. Binds 2 ATP per monomer, at the subunit interface on each ring (PubMed:12622725, PubMed:28302851, PubMed:35507871). The KaiABC complex composition changes during the circadian cycle to control KaiC phosphorylation. Complexes KaiC(6), KaiA(2-4):KaiC(6), KaiB(6):KaiC(6) and KaiC(6):KaiB(6):KaiA(12) are among the most important forms, many form cooperatively (PubMed:28302851, PubMed:34618577, PubMed:35507871). Interacts with SasA, probably as 1 SasA trimer:1 KaiC homohexamer, has highest affinity for unphosphorylated SasA (PubMed:22512339). The CI domain binds to KaiB and SasA; as they have a similar fold they compete for the same site on CI (PubMed:24112939, PubMed:28302851, PubMed:34618577). KaiB assumes a thioredoxin-like form called KaiB(fs) when bound to KaiC (PubMed:26113641, PubMed:28302851).
In the homohexamer the 2 domains (called CI and CII) self-associate to each form a 'donut' layer (PubMed:35507871, PubMed:26113641). The KaiC CI domain mediates interaction with KaiB, CikA and SasA (PubMed:22512339, PubMed:24112939, PubMed:28302851). ATP hydrolysis by the CI domain causes a conformational change that allows KaiB binding (PubMed:28302851). The 2 domains communicate to control ATPase activity (PubMed:35507871).
In the homohexamer the 2 domains (called CI and CII) self-associate to each form a 'donut' layer; the compactness and local conformation of the domains varies over the cell cycle and impacts function. CII has the autokinase and autophosphatase activities, both CI and CII have (weak) ATPase activity; CI has the clock pacemaker role.
Phosphorylated on serine and threonine residues by autocatalysis. Has a 4 step phosphorylation cycle; the autokinase acts first on Thr-432, then Ser-431. When Ser-431 is modified KaiC switches to an autophosphatase mode, acting first on phospho-Thr-432 then phospho-Ser-431.
Phosphorylated on serine/threonine residues by autocatalysis. Both phosphorylated and unphosphorylated forms exist. Both autophosphorylates and autodephosphorylates. Phosphorylated form correlates with clock speed.
Stimulates SasA autophosphorylation. Fully phosphorylated KaiC (tested with phosphomimetic Asp-431-432-Asp) is the best stimulant, requires the ATPase activity of the CII domain. Unphosphorylated SasA associates with KaiC and its autophosphorylation activity is enhanced. Phospho-SasA is released and associates with RpaA, transferring its phosphate group (PubMed:22512339). Formation of the KaiA:KaiB complex is promoted by KaiC, helping switch KaiC from its autophosphorylation to autodephosphatase function (PubMed:24112939, PubMed:28302851).
The interaction with KaiA enhances its phosphorylation status, while the interaction with KaiB decreases it.
Belongs to the queuine tRNA-ribosyltransferase family.
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the Mg-chelatase subunit H family.
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
Belongs to the RNA polymerase beta chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Belongs to the glycosyltransferase 28 family. MurG subfamily.
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Belongs to the universal ribosomal protein uS2 family.
Association with the cytoplasmic side of the thylakoid membrane proposed in PubMed:9599805 is at odds with the subcellular location of orthologs in Synechocystis PCC 6803 and the presence of a signal peptide in this protein.
Belongs to the bacterial solute-binding protein 1 family.
By iron limitation and to a smaller extent by manganese limitation.
May also be part of a periplasmic ABC transporter complex involved in iron import.
Plays an important role in protecting the acceptor side of photosystem II (PSII) against oxidative damage, especially under iron-limiting growth conditions.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
A metamorphic protein which reversibly switches between an inactive tetrameric fold and a rare, thioredoxin-like monomeric fold (KaiB(fs)). KaiB(fs) binds phospho-KaiC, KaiA and CikA. KaiA and CikA compete for binding to KaiB(fs), and KaiB(fs) and SasA compete for binding to KaiC, thus the clock oscillator and output signal pathway are tightly coupled.
Has 2 forms, fold switches to a thioredoxin-like fold (KaiB(fs)) when bound to KaiC, KaiA or CikA (PubMed:26113641, PubMed:28302851). The KaiB(fs) form binds faster to KaiC than its alternate form, so less fully phosphorylated KaiC forms; the KaiB(fs) form activates signaling through CikA and inhibits signaling through SasA (PubMed:26113641) (Probable). The C-terminal region may confer species specificity; C-terminal hybrids do not all rescue deletions in S.elongatus PCC 7942 (PubMed:16227211).
Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria (PubMed:24112939, PubMed:16227211, PubMed:28302851). Its composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to KaiC yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA (PubMed:28302851). KaiB switches to a thioredoxin-like fold (KaiB(fs)) in complex with KaiC (PubMed:26113641, PubMed:28302851). KaiB(6):KaiC(6) formation exposes a site for KaiA binding that sequesters KaiA from the CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator (PubMed:28302851).
Undergoes a major conformational rearrangment; in the free state forms homotetramers with 2 dimers (PubMed:16227211, PubMed:18497745). When bound to the CI domain of KaiC, KaiA or CikA switches to a monomeric thioredoxin-fold (KaiB(fs)) (PubMed:26113641, PubMed:28302851). The KaiABC complex composition changes during the circadian cycle to control KaiC phosphorylation. Complexes KaiC(6), KaiA(2-4):KaiC(6), KaiB(6):KaiC(6) and KaiC(6):KaiB(6):KaiA(12) are among the most important forms, many form cooperatively (PubMed:28302851). Binds to KaiA; 1 KaiB(fs) binds to the KaiA homodimer. Binds to the B-loop in the CI domain of KaiC; SasA and KaiB compete to bind to the CI domain (PubMed:24112939). Binding to KaiC CI domain occurs 1:1 (PubMed:26113641, PubMed:28302851). KaiA and CikA bind to the same region of KaiB(fs) and therefore compete (PubMed:28302851).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
Belongs to the ribose 5-phosphate isomerase family.
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
Belongs to the urease gamma subunit family.
Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.
Belongs to the acetylglutamate kinase family. ArgB subfamily.
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Belongs to the adrenodoxin/putidaredoxin family.
Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Belongs to the ATPase alpha/beta chains family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(9-12).
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
The complex from the organism is particularly stable to disruption and remains functional after 6 hrs at 55 degrees Celsius.
Belongs to the PsbQ family. CyanoQ subfamily.
One of the extrinsic, lumenal subunits of photosystem II (PSII), which stabilize and protect the oxygen-evolving complex. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. Plays a role in the stability of the oxygen-evolving center on the luminal side of PSII.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes (Probable). Purifies with PSII, present at about 0.4 CyanoQ/PSII monomer; is not usually seen in crystal structures of the whole complex in this organism (PubMed:24838684).
Belongs to the CpcT/CpeT biliprotein lyase family.
Covalently attaches a chromophore to Cys residue(s) of phycobiliproteins.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily.
Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
The active site is located at the dimer interface.
Belongs to the phosphoribulokinase family.
Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA family.
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Belongs to the helicase family. DnaB subfamily.
Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
Belongs to the precorrin methyltransferase family.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth.
Cyanobacteria usually contain more than 2 copies of the psbA gene; this strain encodes 3.
Herbicides such as terbutryn, atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes (By similarity) (PubMed:14764885, PubMed:16355230, PubMed:19219048, PubMed:20558739, PubMed:21367867, PubMed:22665786, PubMed:23413188, PubMed:25006873, PubMed:25043005, Ref.3). Precursor protein interacts with Ycf48 (PubMed:30061392). Part of a photosystem II (PSII) assembly intermediate complex PSII-I; crystallized from a strain deleted of psbJ, it forms monomeric PSII before addition of the oxygen evolving complex. PSII-I includes 3 assembly factors not found in mature PSII (Psb27, Psb28 and Psb34). In PSII-I the C-terminus of D1 (this subunit) is already processed but not yet found at its final position (PubMed:33846594).
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution (PubMed:19219048, PubMed:21367867). PSII binds additional chlorophylls, carotenoids and specific lipids.
Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily.
Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity.
Belongs to the class-II aminoacyl-tRNA synthetase family.
SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.
Belongs to the bacterial ribosomal protein bL32 family.
Subunit R is required for both nuclease and ATPase activities, but not for modification.
The type I restriction/modification system is composed of three polypeptides R, M and S.
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Belongs to the GatB/GatE family. GatB subfamily.
Catalyzes the synthesis of activated sulfate.
Belongs to the glycosyl hydrolase 24 family.
Belongs to the 4-toluene sulfonate uptake permease (TSUP) (TC 2.A.102) family.
Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Belongs to the glycosyl hydrolase 38 family.
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Belongs to the methyl-accepting chemotaxis (MCP) protein family.
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.
Belongs to the LytR/CpsA/Psr (LCP) family.
Belongs to the bacterial ribosomal protein bL21 family.
Part of the 50S ribosomal subunit. Contacts protein L20.
This protein binds to 23S rRNA in the presence of protein L20.
Belongs to the aldehyde dehydrogenase family.
Belongs to the N(4)/N(6)-methyltransferase family.
Belongs to the auxin efflux carrier (TC 2.A.69) family.
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Divalent metal cations. Prefers magnesium or manganese.
Belongs to the bacterial ribosomal protein bS18 family.
Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein bS6.
Belongs to the bacterial ribosomal protein bL33 family.
Belongs to the heat shock protein 70 family.
By stress conditions e.g. heat shock (By similarity).
Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Belongs to the methylthiotransferase family. MiaB subfamily.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. SDR39U1 subfamily.
Belongs to the bacterial ribosomal protein bL19 family.
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
Belongs to the uracil-DNA glycosylase (UDG) superfamily. Type 4 (UDGa) family.
Belongs to the helicase family. UvrD subfamily.
Belongs to the beta sliding clamp family.
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
Forms a ring-shaped head-to-tail homodimer around DNA.
Belongs to the Mg-chelatase subunits D/I family.
Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Belongs to the short-chain dehydrogenases/reductases (SDR) family. POR subfamily.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.
ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.
Belongs to the CPA3 antiporters (TC 2.A.63) subunit E family.
Belongs to the ATPase gamma chain family.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Converts the D-glycero-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL). Cooperates with RbcX in RbcL folding, plays the major role in assembly of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces Raf1, leading to holoenzyme formation.
Has 3 domains, the N-terminal alpha-helical domain, an extended flexible linker and the C-terminal beta-sheet domain. The 2 C-terminal beta-sheet domains are swapped and pack against each other to form the dimer interface.
Homodimer. Forms an RbcL(8)-Raf1(8) complex. Forms complexes of many stoichiometries with RbcL with and without RbcS. RbcX and Raf1 can bind simultaneously to RbcL.
Required for optimal reconstitution of RuBisCO upon expression of rbcL-rbcS subunits in E.coli. Only interacts with the large subunit (cbbL, rbcL). Probably acts in the final stages of RuBisCO assembly, possibly participating in the addition of the small subunit (ccbS, rbcS).
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Belongs to the binding-protein-dependent transport system permease family.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the cytidine and deoxycytidylate deaminase family.
Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
A carbonic anhydrase, catalyzes the reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation, supplies CO(2) to ribulose bisphosphate carboxylase (RuBisCO) in the carboxysome. Active when the disulfide bond (194-200) is oxidized, suggesting the interior of the carboxysome is oxidizing.
Belongs to the gamma-class carbonic anhydrase family.
Beta-carboxysome assembly initiates when soluble RuBisCO is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both forms of CcmM (Probable). CcmN interacts with the N-terminus of full length CcmM, and then recruits the shell proteins (CcmK) via CcmN's encapsulation peptide. Shell formation requires both CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton (By similarity).
Carbonic anhydrase (CA) activity is probably under redox control to remain inactive in the cytoplasm. CA activity of full-length protein inhibited by ethoxyzolamide, and for both full-length and CcmM 1-209 construct by reducing agents.
Functions as a scaffold protein for the assembly of beta-carboxysomes, initiates carboxysome assembly by coalescing RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) (Probable). Produced as a full-length and a shorter form; both forms are required for correct carboxysome assembly and growth (By similarity).
The N-terminal structure crystallizes as a homotrimer; zinc is bound between adjacent monomers (PubMed:20133749). The C-terminal RbcS-like domains bind to holo-RuBisCO (PubMed:30591587). Full length protein interacts with CcmN (By similarity).
The N-terminus (residues 1-164) forms a trimer with a partially blocked channel forms at the trimer interface (PubMed:20133749). The C-terminus has 4 domains that resemble the small subunit of RuBisCO (rbcS) joined by flexible linkers; the first one (CcmMS1) has been crystallized and folds much like RbcS. CcmMS1 binds to holo-RuBisCO (RbcL(8)-RbcS(8)), a CcmMS1-CcmMS2 constructs binds about 10-fold better, while the entire C-terminus with all 4 CcmMS domains binds with an intermediate affinity. CcmMS1 binds to a different region of RbcL than does RbcS, up to 5 CcmMS1 domains can bind to the intact holo enzyme (PubMed:30591587).
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).
In the C-terminal section; belongs to the MurCDEF family.
Belongs to the PEP-utilizing enzyme family.
Belongs to the aspartate/glutamate racemases family.
Provides the (R)-glutamate required for cell wall biosynthesis.
May be involved in photosynthetic membrane biogenesis.
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
A core subunit of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. Helps stabilize PSII (PubMed:20359460).
No visible growth effect at 10 umol or 60 umol photons/m(2)/s, loss of the PsbY subunit from PSII, no change in O(2) evolution under medium light, increased susceptibility to photodamage, cytochrome b559 (PsbE and PsbF) is in a low potential state in isolated thylakoids.
PSII binds multiple chlorophylls, carotenoids and specific lipids.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Belongs to the methylthiotransferase family. RimO subfamily.
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
May help in the organization of the PsaE and PsaF subunits.
Belongs to the isochorismate synthase family.
Heterodimer of an alpha and a beta chain.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Belongs to the MsrA Met sulfoxide reductase family.
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
Belongs to the ABC transporter superfamily. Ycf16 family.
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Belongs to the anti-sigma-factor antagonist family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Belongs to the ferredoxin thioredoxin reductase alpha subunit family.
Heterodimer of subunit A (variable subunit) and subunit B (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin and thioredoxin.
Variable subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
In the C-terminal section; belongs to the helicase family. RecG subfamily.
In the N-terminal section; belongs to the UvrB family.
ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.
Belongs to the ParA family. MinD subfamily.
Belongs to the ABC transporter superfamily. Sulfate/tungstate importer (TC 3.A.1.6) family.
Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Belongs to the universal ribosomal protein uL3 family.
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.
Belongs to the radical SAM superfamily. CofG family.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.
Consists of two subunits, CofG and CofH.
Associates with stalled 50S ribosomal subunits.
Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Belongs to the CugP-type UDP-glucose pyrophosphorylase family.
Catalyzes the formation of UDP-glucose, from UTP and glucose 1-phosphate.
Belongs to the cytochrome c oxidase subunit 3 family.
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA.
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Belongs to the pseudouridine synthase RluA family.
Responsible for synthesis of pseudouridine from uracil.
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.
Catalyzes the oxidation of L-aspartate to iminoaspartate.
Belongs to the radical SAM superfamily. CofH family.
Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
Belongs to the anthranilate synthase component I family.
Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
The glycine cleavage system catalyzes the degradation of glycine.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Belongs to the transaldolase family. Type 1 subfamily.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
Belongs to the complex I NdhN subunit family.
Binds 1 dipyrromethane group covalently.
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
The porphobilinogen subunits are added to the dipyrromethane group.
Belongs to the helicase family. RecG subfamily.
Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Carboxylation allows a single lysine to coordinate two nickel ions.
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity).
Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.
Belongs to the bacterial solute-binding protein 3 family.
Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
Belongs to the glucose-6-phosphate dehydrogenase family.
Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Belongs to the ferredoxin thioredoxin reductase beta subunit family.
Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI (By similarity).
Belongs to the complex I subunit 4 family.
Rod linker protein, associated with allophycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer (By similarity).
Belongs to the radical SAM superfamily. RlmN family.
Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex.
This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
In the C-terminal section; belongs to the HTP reductase family.
In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
Non-discriminating glutamyl-tRNA synthetase. Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). Acylates both tRNA(Glu) and tRNA(Gln) with glutamate, but has 13-fold higher efficiency with tRNA(Glu).
This organism lacks a tRNA synthetase for tRNA(Gln). Instead, tRNA(Gln) is first charged with Glu, and then the bound glutamate is converted to glutamine by GatCAB.
Belongs to the universal ribosomal protein uS14 family.
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Part of the 30S ribosomal subunit. Contacts proteins S3 and S10.
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Belongs to the universal ribosomal protein uS4 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.
With S5 and S12 plays an important role in translational accuracy.
Belongs to the ABC-3 integral membrane protein family.
Belongs to the universal ribosomal protein uL16 family.
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Belongs to the ABC transporter superfamily. Nitrate/nitrite/cyanate uptake transporter (NitT) (TC 3.A.1.16) family.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family.
Probable transporter of a GTP-driven Fe(2+) uptake system.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.
Catalyzes the biosynthesis of agmatine from arginine.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily.
Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature.
Belongs to the thioester dehydratase family. FabZ subfamily.
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Contains one covalently linked phycocyanobilin chromophore.
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Belongs to the acetolactate synthase small subunit family.
Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
Belongs to the cyclophilin-type PPIase family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY.
Belongs to the universal ribosomal protein uL5 family.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Belongs to the carotenoid/retinoid oxidoreductase family.
This enzyme converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene.
Belongs to the PsbP family. CyanoP subfamily.
Crystallizes with Zn(2+), but it is not known if this is physiologically relevant.
Monomer (PubMed:20698571). Present in very small amounts in PSII (PubMed:24838684).
Plays a role in the early stages of photosystem II (PSII) assembly; binds to D2 (psbD) and may facilitate its incorporation into PSII (By similarity). Present in less than 1% of PSII preparations (PubMed:24838684).
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Binds 1 thiamine pyrophosphate per subunit.
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Found at the monomer-monomer interface of the photosystem II (PS II) dimer, plays a role in assembly and dimerization of PSII. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.
No detectable dimeric PSII, loss of another protein that may be PsbM.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes (By similarity) (PubMed:14764885, PubMed:16355230, PubMed:19219048, PubMed:20558739, PubMed:21367867, PubMed:22665786, PubMed:23413188, PubMed:25006873, PubMed:25043005). Part of a photosystem II (PSII) assembly intermediate complex PSII-I; crystallized from a strain deleted of psbJ, it forms monomeric PSII before addition of the oxygen evolving complex. PSII-I includes 3 assembly factors not found in mature PSII (Psb27, Psb28 and Psb34) (PubMed:33846594).
Belongs to the EPSP synthase family. MurA subfamily.
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
In the C-terminal section; belongs to the PEP-utilizing enzyme family.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer.
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Belongs to the GHMP kinase family. IspE subfamily.
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Belongs to the tRNA pseudouridine synthase TruA family.
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Belongs to the asparagine synthetase family.
Belongs to the universal ribosomal protein uL14 family.
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8.
Belongs to the pseudouridine synthase RsuA family.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Belongs to the phosphoglycerate kinase family.
Belongs to the universal ribosomal protein uL22 family.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).
Belongs to the MurCDEF family. MurF subfamily.
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Belongs to the sigma-70 factor family. ECF subfamily.
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Belongs to the PsbB/PsbC family. PsbB subfamily.
Binds multiple chlorophylls. PSII binds additional chlorophylls, carotenoids and specific lipids.
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Belongs to the PTPS family. QueD subfamily.
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Participates in transcription elongation, termination and antitermination.
Cyanobacteria usually contain more than 2 copies of the psbA gene.
Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes (By similarity) (PubMed:19219048). Precursor protein interacts with Ycf48 (By similarity).
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Belongs to the CcmL/EutN family. CcmL subfamily.
Homopentamer (PubMed:23949415, PubMed:24504539). May interact with CcmK2, this occurs at very high CcmK2 concentrations (Probable). Interacts with full-length CcmM (By similarity).
Probably forms vertices in the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Has been modeled to induce curvature upon insertion into an otherwise flat hexagonal molecular layer of CcmK subunits.
The tight homopentamer forms a pore with an opening of 4-5 Angstroms in diameter which opens into a wider tunnel at the base of the truncated pyramid. The pore is positively charged.
One of the extrinsic, lumenal subunits of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. The extrinsic proteins stabilize the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protect the OEC against heat-induced inactivation.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
Belongs to the chaperonin (HSP60) family.
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Belongs to the PsbB/PsbC family. PsbC subfamily.
Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. Part of a photosystem II (PSII) assembly intermediate complex PSII-I; crystallized from a strain deleted of psbJ, it forms monomeric PSII before addition of the oxygen evolving complex. PSII-I includes 3 assembly factors not found in mature PSII (Psb27, Psb28 and Psb34), and CP43 (this protein) is not in its mature conformation (PubMed:33846594).
Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Belongs to the topoisomerase GyrA/ParC subunit family.
Belongs to the type II topoisomerase GyrA/ParC subunit family.
Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.
Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Belongs to the universal ribosomal protein uS7 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
Part of the 30S ribosomal subunit. Contacts proteins S9 and S11.
Belongs to the 2Fe2S plant-type ferredoxin family.
Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition.
CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Belongs to the adenylate cyclase family. DacA/CdaA subfamily.
Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Belongs to the BPG-independent phosphoglycerate mutase family.
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Involved in photosystem II (PSII) assembly and/or repair, probably in conversion of late PSII assembly intermediates into mature dimeric PSII.
Part of photosystem II (PSII) assembly intermediate complex PSII-I; crystallized from a strain without psbJ, it forms monomeric PSII before addition of the oxygen evolving complex. PSII-I includes 3 assembly factors not found in mature PSII (Psb27, Psb28 and Psb34). The N-terminus of Psb34 (this protein) binds to CP47 (psbB) in close proximity to PsbH on the cytoplasmic face of PSII.
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Belongs to the bacterial ribosomal protein bL25 family.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA independently of L5 and L18.
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Not essential for photoautotrophic growth, however PSII is less stable, a considerable amount is missing the oxygen evolving complex, and it is missing PsbX.
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Belongs to the complex I subunit 2 family.
Belongs to the MurCDEF family. MurE subfamily.
Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
Belongs to the transketolase family. DXPS subfamily.
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
DNA polymerase III contains a core (composed of alpha, epsilon and theta chains) that associates with a tau subunit. This core dimerizes to form the POLIII' complex. PolIII' associates with the gamma complex (composed of gamma, delta, delta', psi and chi chains) and with the beta chain to form the complete DNA polymerase III complex.
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
One of the extrinsic, lumenal subunits of photosystem II (PSII), which stabilize and protect the oxygen-evolving complex. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation (PubMed:20558739, PubMed:25006873). Required for dimerization of PSII and for binding of PsbQ to PSII (By similarity).
Catalyzes the synthesis of GMP from XMP.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Belongs to the complex I subunit 6 family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Belongs to the diaminopimelate epimerase family.
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Coproporphyrinogen III oxidase subfamily.
Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Belongs to the prokaryotic sulfate-binding protein family.
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
Binds to the N-terminal domain of the chaperone ClpA.
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Belongs to the sulfate adenylyltransferase family.
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Belongs to the bacterial ribosomal protein bL28 family.
A 7-bladed beta-propeller torus, about 54 by 46 Angstroms, with a depth of about 25 Angstroms and a central pore.
A factor required for optimal assembly of photosystem II (PSII), acting in the early stages of PSII assembly. Also plays a role in replacement of photodamaged D1 (psbA). Assists YidC in synthesis of chlorophyll-binding proteins.
Interacts with the D1 protein (crystallized with PsbA1 or PsbA3), via the latter's C-terminal prepropeptide, may interact with parts of the mature D1 protein as well.
By homology with NorV in E.coli, may be involved in nitric oxide detoxification.
In the C-terminal section; belongs to the flavodoxin reductase family.
In the N-terminal section; belongs to the zinc metallo-hydrolase group 3 family.
Mediates electron transfer from NADH to oxygen, reducing it to water. This modular protein has 3 redox cofactors, in other organisms the same activity requires 2 or 3 proteins (By similarity).
Belongs to the universal ribosomal protein uS19 family.
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Belongs to the universal ribosomal protein uL29 family.
Belongs to the methyltransferase superfamily. PrmA family.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2A subfamily.
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Belongs to the threonine synthase family.
Belongs to the bacterial ribosomal protein bL34 family.
Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
The cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
Decreased yields of PSII dimers with increased PSII monomers, slightly slower photoautotrophic growth, about 20% less oxygen evolution. Formed PSII dimers are stable.
One of the components of the core complex of photosystem II (PSII). May be required for formation of PSII dimers but not their subsequent stability (PubMed:21195048). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Belongs to the chloroplast-specific ribosomal protein cS23 family.
Probably a ribosomal protein or a ribosome-associated protein.
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Belongs to the universal ribosomal protein uL11 family.
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
One or more lysine residues are methylated.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the universal ribosomal protein uL18 family.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Belongs to the 2-oxoacid dehydrogenase family.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
Belongs to the anthranilate phosphoribosyltransferase family.
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Belongs to the RuBisCO large chain family. Type I subfamily.
Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked (PubMed:25041569, Ref.4). The disulfide link is formed within the large subunit homodimers (Ref.4). Interacts with assembly factor Raf1 which helps form the holoenzyme, most interaction (and folding) occurs in the cytoplasm (PubMed:25041569).
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.
Belongs to the N(4)/N(6)-methyltransferase family. N(4) subfamily.
Belongs to the SecD/SecF family. SecF subfamily.
Forms a complex with SecD. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Probably participates in protein translocation into and across both the cytoplasmic and thylakoid membranes in cyanobacterial cells.
Belongs to the carotenoid oxygenase family.
Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Autophosphorylates, probably on His-160.
Homotrimer with a small amount of possible homohexamer; a protein fragment of 109-380 is also a homotrimer. Interacts with KaiC, probably as 1 SasA trimer:1 KaiC homohexamer; unphosphorylated SasA has the highest affinity (PubMed:22512339). Homodimer (PubMed:34618577) (Probable). Binds to the B-loop in the CI domain of KaiC; SasA and KaiB(fs) compete to bind to the CI domain (PubMed:24112939, PubMed:26113641, PubMed:34618577). Binds preferentially to doubly phosphorylated KaiC (PubMed:34618577).
Member of the two-component regulatory system SasA/RpaA involved in genome-wide circadian gene expression. One of several clock output pathways. Participates in the Kai clock protein complex, the main circadian regulator in cyanobacteria, via its interaction with KaiC. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. In addition to its output function, recruits fold-shifted KaiB (KaiB(fs)) to KaiC to cooperatively form the KaiB(6):KaiC(6) complex (independent of SasA kinase activity). Required for robustness of the circadian rhythm of gene expression and is involved in clock output, also required for adaptation to light/dark cycles.
The N-terminus (residues 1-108) interacts with KaiC, while the C-terminus (109-380) autophosphorylates and is probably responsible for self-association. The N-terminal domain stimulates the C-terminus to autophosphorylate; KaiC does not stimulate autophosphorylation of the C-terminal domain.
Belongs to the type-I restriction system S methylase family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily.
Contains two covalently linked bilin chromophores.
Heterodimer of an alpha and a beta subunit, which further assembles into trimers (PubMed:12460674, PubMed:12615541). The trimers assemble into hexamers (Probable).
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.
Belongs to the ATPase epsilon chain family.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
The complex from the organism is particularly stable to disruption and remains functional after 6 hours at 55 degrees Celsius.
Belongs to the bacterial solute-binding protein 9 family.
Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
Rod-core linker protein required for attachment of phycocyanin to allophycocyanin in cores of phycobilisomes.
The phycobilisome is a hemidiscoidal structure that is composed of two distinct substructures: a core complex and a number of rods radiating from the core.
Binds 1 heme c group covalently per subunit. PSII binds multiple chlorophylls, carotenoids and specific lipids.
Cells do not grow photoautotrophically under low CO(2) concentrations.
One of the extrinsic, lumenal subunits of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. The extrinsic proteins stabilize the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protect the OEC against heat-induced inactivation. Low-potential cytochrome c that plays a role in the OEC of PSII.
Belongs to the Rieske iron-sulfur protein family.
The Rieske iron-sulfur protein is a high potential 2Fe-2S protein.
Belongs to the MsrB Met sulfoxide reductase family.
Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Belongs to the four-carbon acid sugar kinase family.
Belongs to the glutamate 5-kinase family.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Belongs to the glutamate synthase family.
Belongs to the LysR transcriptional regulatory family.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Maintains high levels of reduced glutathione.
Belongs to the MnmG family. TrmFO subfamily.
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Belongs to the kinesin light chain family.
Could be involved in insertion of integral membrane proteins into the membrane.
Belongs to the universal ribosomal protein uS13 family.
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome.
Belongs to the bacterial secretin family.
Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
Interacts with the Sec translocase complex via SecD. Specifically interacts with transmembrane segments of nascent integral membrane proteins during membrane integration (By similarity).
Probably also aids protein insertion, folding and/or assembly of membrane complexes destined for the thylakoid.
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (By similarity).
Belongs to the complex I subunit 4L family.
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacteriotal NDH-1 also plays a role in inorganic carbon-concentration.
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Belongs to the alpha-IPM synthase/homocitrate synthase family.
Associates with the 50S ribosomal subunit.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Belongs to the aldehyde decarbonylase family.
Catalyzes the decarbonylation of fatty aldehydes to alkanes.
Belongs to the glutamyl-tRNA reductase family.
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Heterodimer of an alpha subunit and a beta subunit. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. Part of a photosystem II (PSII) assembly intermediate complex PSII-I; crystallized from a strain deleted of psbJ, it forms monomeric PSII before addition of the oxygen evolving complex. PSII-I includes 3 assembly factors not found in mature PSII (Psb27, Psb28 and Psb34) (PubMed:33846594).
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Belongs to the major facilitator superfamily. Folate-biopterin transporter (TC 2.A.71) family.
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Involved in the catabolism of quinolinic acid (QA).
Belongs to the glycosyltransferase 1 family.
Catalyzes the reversible conversion of sucrose and a nucleotide disphosphate (NDP) into fructose and NDP-glucose; although the reaction is freely reversible in vitro, the physiological reaction seems to be sucrose cleavage. Unlike characterized plant enzymes prefers ADP as a cosubstrate, whereas plants prefer UDP (PubMed:23196182). Its preference for ADP over UDP suggests it may directly link sucrose and glycogen metabolism (Probable).
Probably a homotetramer (PubMed:23196182).
The IMP cyclohydrolase activity resides in the N-terminal region.
Belongs to the KHG/KDPG aldolase family.
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
In the C-terminal section; belongs to the peptidase M41 family.
In the central section; belongs to the AAA ATPase family.
Belongs to the polypeptide deformylase family.
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.
Homohexamer. The oligomerization is ATP-dependent (By similarity).
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).
Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME).
Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily.
Heteromultimer composed of HisG and HisZ subunits.
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
This function is generally fulfilled by the C-terminal part of HisG, which is missing in some bacteria such as this one.
Belongs to the universal ribosomal protein uL6 family.
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Belongs to the geranylgeranyl reductase family. ChlP subfamily.
Belongs to the universal ribosomal protein uS3 family.
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14.
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Belongs to the class II fructose-bisphosphate aldolase family.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
One is catalytic and the other provides a structural contribution.
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Belongs to the sulfur carrier protein TusA family.
Belongs to the 6-phosphogluconate dehydrogenase family.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Forms a complex with heterodimeric ferredoxin-thioredoxin reductase (FTR) and thioredoxin.
Belongs to the urease beta subunit family.
Belongs to the universal ribosomal protein uS9 family.
Belongs to the elongation factor P family.
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Belongs to the complex I 23 kDa subunit family.
NDH-1 is composed of at least 11 different subunits.
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalyzes the reversible phosphorylation of UMP to UDP.
A monovalent cation. Ammonium or potassium.
Belongs to the type III pantothenate kinase family.
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Belongs to the glycosyl hydrolase 57 family.
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis.
PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Belongs to the ATP-dependent AMP-binding enzyme family.
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Interacts with UvrB in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Belongs to the type IA topoisomerase family.
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Belongs to the bacterial ribosomal protein bS21 family.
An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily.
Homodimer, may be a subunit of the RNA degradosome.
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Belongs to the bacterial microcompartments protein family. CcmK subfamily.
Homohexamer. Interacts preferentially with CcmK2 and CcmK4a rather than itself in vitro.
One of the shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The hexamer central pore probably regulates metabolite flux.
The tight homohexamer forms a small pore which is positively charged.
Belongs to the methyltransferase superfamily. RsmH family.
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization. This subunit may make specific contacts with lipid(s) (PubMed:16355230).
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
Tetramer of two alpha and two beta subunits.
Belongs to the transferase hexapeptide repeat family.
Belongs to the type II topoisomerase GyrB family.
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Belongs to the mannose-6-phosphate isomerase type 2 family.
With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Belongs to the universal ribosomal protein uL23 family.
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
Part of the 50S ribosomal subunit. Contacts protein L29, and trigger factor when it is bound to the ribosome.
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
The C-terminal coiled-coil domain is crucial for aminoacylation activity.
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family.
Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family.
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (PstB), two transmembrane proteins (PstC and PstA) and a solute-binding protein (PstS).
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
In the C-terminal section; belongs to the PRA-PH family.
In the N-terminal section; belongs to the PRA-CH family.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Involved in DNA repair and RecF pathway recombination.
Belongs to the creatininase superfamily.
Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin.
Belongs to the HPF/YfiA ribosome-associated protein family. Long HPF subfamily.
Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth.
Belongs to the cytochrome c family. PetJ subfamily.
Binds 1 heme c group covalently per subunit.
Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
Belongs to the RNA polymerase alpha chain family.
Homodimer. In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (By similarity).
The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Belongs to the RecA family. RadA subfamily.
DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Plays a role in repairing double-strand DNA breaks, probably involving stabilizing or processing branched DNA or blocked replication forks.
The middle region has homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition.
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Belongs to the bacterial microcompartments protein family. CsoS1 subfamily.
Belongs to the glutamine synthetase family.
Belongs to the universal ribosomal protein uL4 family.
Forms part of the polypeptide exit tunnel.
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Belongs to the bacterial ribosomal protein bL12 family.
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors.
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Belongs to the shikimate dehydrogenase family.
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Belongs to the SAM hydrolase / SAM-dependent halogenase family.
Decreased yields of PSII dimers with increased PSII monomers, slightly slower photoautotrophic growth, about 20% less oxygen evolution. Formed PSII dimers are less stable than wild-type.
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface. Probably involved in dimerization of PSII; at the monomer-monomer interface the only protein-protein contacts observed are between the 2 PsbM subunits. Lipids, chlorophylls and carotenoids contribute strongly to PSII dimerization.
Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Belongs to the anaerobic coproporphyrinogen-III oxidase family.
Belongs to the histone deacetylase family.
Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Belongs to the endoribonuclease YbeY family.
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Belongs to the universal ribosomal protein uS17 family.
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily.
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Belongs to the glycogen phosphorylase family.
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.
Methyltransferase required for the conversion of 2-phytyl-1,4-beta-naphthoquinol to phylloquinol.
Belongs to the DNA polymerase type-A family.
In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Belongs to the quinolinate synthase family. Type 2 subfamily.
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 1 subfamily.
Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:24872444). Does not show N-succinylamino acid racemase (NSAR) activity with N-succinyl-L-phenylglycine as substrate (PubMed:24872444).
Belongs to the ABC transporter superfamily.
Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
Belongs to the complex I NdhL subunit family.
Belongs to the prokaryotic/mitochondrial release factor family.
Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Belongs to the universal stress protein A family.
Involved in protein export. Participates in an early event of protein translocation.
Belongs to the outer membrane factor (OMF) (TC 1.B.17) family.
Belongs to the iron/manganese superoxide dismutase family.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the anion channel-forming bestrophin (TC 1.A.46) family.
An RbcL-specific chaperone. Required for assembly of the RbcL8 core (PubMed:19081849) (Probable). The central cleft of the RbcX homodimer (RbcX2) binds the C-terminus of a RbcL monomer, stabilizing the C-terminus and probably preventing its reassociation with chaperonin GroEL-ES. At the same time the peripheral region of RbcX2 binds a second RbcL monomer, bridging the RbcL homodimers in the correct orientation. The RbcX2(2)-bound RbcL dimers then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of RbcX2 (By similarity).
Homodimer (PubMed:19081849, PubMed:21821880). Interacts with the exposed C-terminal peptide of RbcL via its central cleft, contacts a second RbcL monomer via its peripheral polar surface (By similarity).
The homodimer has 2 functional domains, a central cleft essential for production of soluble RbcL in which the RbcL peptide binds, and a polar surface which plays a role in correct RbcL subunit arrangement.
Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily.
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Belongs to the heme-copper respiratory oxidase family.
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Belongs to the universal ribosomal protein uS5 family.
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
Part of the 30S ribosomal subunit. Contacts proteins S4 and S8.
The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
With S4 and S12 plays an important role in translational accuracy.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Cells grow normally under all light regimes tested; it is dispensable for photoautotrophic growth. The deletion strain is more tolerant to photoinhibition, while isolated PSII complex contains less PsbK and Psb30/Ycf12 than wild-type and also has reduced oxygen-evolving capacity.
May also aid in binding of PsbK, Psb30/Ycf12 and the oxygen-evolving complex to PSII, at least in vitro (PubMed:17967798).
May control the interaction of photosystem II (PSII) cores with the light-harvesting antenna, regulates electron flow through the 2 photosystem reaction centers. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes (By similarity) (PubMed:14764885, PubMed:16355230, PubMed:17935689, PubMed:17967798, PubMed:19219048, PubMed:20558739, PubMed:21367867, PubMed:22665786, PubMed:23413188, PubMed:25006873, PubMed:25043005). Part of a photosystem II (PSII) assembly intermediate complex PSII-I; crystallized from a strain deleted of psbJ, it forms monomeric PSII before addition of the oxygen evolving complex. PSII-I includes 3 assembly factors not found in mature PSII (Psb27, Psb28 and Psb34) (PubMed:33846594).
Belongs to the ABC-2 integral membrane protein family.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Binds 1 Mn(2+) or Fe(2+) ion per subunit.
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Belongs to the phosphohexose mutase family.
Belongs to the Mg-chelatase subunits D/I family. ComM subfamily.
Belongs to the universal ribosomal protein uS12 family.
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex.
With S4 and S5 plays an important role in translational accuracy.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity).
In the C-terminal section; belongs to the NnrD/CARKD family.
In the N-terminal section; belongs to the NnrE/AIBP family.
Belongs to the DNA mismatch repair MutS family.
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Belongs to the bacterial ribosomal protein bL20 family.
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Catalyzes the NADP-dependent reduction of long-chain acyl-ACP to the corresponding fatty aldehyde. Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane, by producing the fatty aldehydes used by aldehyde decarbonylase.
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Belongs to the cytochrome ubiquinol oxidase subunit 2 family.
Belongs to the universal ribosomal protein uS8 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts proteins S5 and S12.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Belongs to the orange carotenoid-binding protein family.
Belongs to the bacterial ribosomal protein bL9 family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the bacterial ribosomal protein bS6 family.
Binds together with bS18 to 16S ribosomal RNA.
Belongs to the class-I DAHP synthase family.
Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Belongs to the bacterial ribosomal protein bS20 family.
Belongs to the RNA polymerase subunit omega family.
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
Belongs to the universal ribosomal protein uL24 family.
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
In the N-terminal section; belongs to the aldehyde dehydrogenase family.
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.
Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Seems to be required for the assembly of the photosystem I complex.
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
Belongs to the bacterial ribosomal protein bS16 family.
Belongs to the carbon-nitrogen hydrolase superfamily.
Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.
Monomer. Associates with 30S ribosomal subunit, binds 16S rRNA.
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Involved in light-induced Na(+)-dependent proton extrusion. Also seems to be involved in CO(2) transport.
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively.
In the C-terminal section; belongs to the cytidylate kinase family. Type 1 subfamily.
In the N-terminal section; belongs to the pantothenate synthetase family.
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
Belongs to the complex I subunit 5 family.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Belongs to the chorismate synthase family.
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
May play a role in photosystem I and II biogenesis.
Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in this organism and T.vulcanus, this is probably not true.
Belongs to the bacterial ribosomal protein bL36 family.
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family.
Belongs to the cytochrome b family. PetB subfamily.
Binds 2 heme b groups non-covalently with two histidine residues as axial ligands.
Binds one heme group covalently by a single cysteine link with no axial amino acid ligand. This heme was named heme ci.
Heme 1 (or BH or b566) is high-potential and absorbs at about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs at about 562 nm.
Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Homotetramer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Homohexamer. Stacked hexamers, with the concave faces together, have also been crystallized. Interacts preferentially with itself, then with CcmK1 and CcmK4a in vitro (PubMed:22748766). May interact with CcmL, this occurs at very high CcmK2 concentrations (Probable). Interacts with CcmN and CcmO in the carboxysome (By similarity).
Probably the major shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The hexamer central pore probably regulates metabolite flux.
The tight homhexamer forms an irregular pore with an opening about 4.8 X 6.5 Angstroms.
Belongs to the small heat shock protein (HSP20) family.
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Belongs to the cytochrome b family. PetD subfamily.
Belongs to the peroxiredoxin family. Prx6 subfamily.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.
Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Homodimer. The tRNA molecule binds across the dimer.
Involved in correct processing of both the 5' and 3' ends of 23S rRNA precursor. Processes 30S rRNA precursor transcript even in absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller rRNA precursors.
Belongs to the tRNA(Ile)-lysidine synthase family.
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Part of a photosystem II (PSII) assembly intermediate complex PSII-I; crystallized from a strain deleted of psbJ, it forms monomeric PSII before addition of the oxygen evolving complex. PSII-I includes 3 assembly factors not found in mature PSII (Psb27, Psb28 and Psb34). Binds to the lumenal side of PSII, adjacent to the CP43 (psbC) subunit (PubMed:17114356, PubMed:33846594).
Plays a role in the repair and/or biogenesis of the calcium-manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of other extrinsic subunits PsbO, PsbU and PsbV, and thus assembly of calcium-manganese-oxide cluster. Psb27-containing complexes lack oxygen evolving activity and an oxidizable calcium-manganese-oxide cluster, but have a normal reaction center.
Belongs to the SecD/SecF family. SecD subfamily.
Forms a complex with SecF. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily.
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits (By similarity).
Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
Belongs to the zeta carotene desaturase family.
Belongs to the complex I 20 kDa subunit family.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Belongs to the bacterial ribosomal protein bL17 family.
Part of the 50S ribosomal subunit. Contacts protein L32.
Belongs to the uroporphyrinogen decarboxylase family.
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Belongs to the D-alanine--D-alanine ligase family.
Binds 2 magnesium or manganese ions per subunit.
Belongs to the adenylosuccinate synthetase family.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a, b, b' and c.
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Belongs to the universal ribosomal protein uL2 family.
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome.
Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Lacks the C-terminal regulatory region which is replaced by HisZ.
Belongs to the thymidylate kinase family.
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.
Belongs to the class I-like SAM-binding methyltransferase superfamily. gTMT family.
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Belongs to the RNA methyltransferase TrmD family.
Specifically methylates guanosine-37 in various tRNAs.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
Homodimer. UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
Belongs to the ATPase delta chain family.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Belongs to the ferredoxin--NADP reductase type 1 family.
Belongs to the vitamin-B12 independent methionine synthase family.
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Belongs to the glycosyltransferase 39 family.
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Belongs to the heat shock protein 90 family.
Belongs to the TPP enzyme family. MenD subfamily.
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Belongs to the complex I NdhM subunit family.
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Belongs to the thiolase-like superfamily. FabH family.
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Belongs to the universal ribosomal protein uS11 family.
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18. Binds to IF-3.
Belongs to the histidinol dehydrogenase family.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
May help in the organization of the PsaL subunit.
Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6-phosphate and sedoheptulose 7-phosphate, respectively.
Belongs to the complex I 49 kDa subunit family.
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Belongs to the inositol monophosphatase superfamily.
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Belongs to the universal ribosomal protein uS15 family.
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.
Belongs to the universal ribosomal protein uL13 family.
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Belongs to the GTP-binding SRP family. FtsY subfamily.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Belongs to the cyclic nucleotide phosphodiesterase class-III family.
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Autophosphorylates, possibly on His-161.
Belongs to the chloroplast sensor kinase protein family.
Hexamers; upon treatment with 0.5 M NaCl only tetramers are seen. The tetramers are probably inactive.
Member of 2 two-component regulatory system(s) Hik2/Rre1 and Hik2/RppA. Transduces PQ (plastoquinone) redox signals to photosystem gene expression machinery during the adjustment of photosystem stoichiometry. Reduced PQ suppresses its autophosphorylation activity (i.e. kinase activity is higher under oxidizing conditions). As part of a two-component regulatory system with Rre1, controls expression of sigB and several other genes in response to hyperosmotic stress. May transfer phosphate to RppA in a possible Hik2/RppA two-component system.
Oligomerization seems to be mediated by the histidine kinase domain (residues 142-386) which forms tetramers and hexamers. The DHp subdomain (dimerization and phosphotransfer, residues 142-270) forms hexamers and octamers. NaCl treatment reduces the histidine kinase domain to tetramers and the DHp domain to hexamers, suggests the DHp domain senses NaCl.
The 3Fe-4S cluster is redox-responsive, binds 1 cluster per monomer.
Essential for recycling GMP and indirectly, cGMP.
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
The PRC barrel domain binds ribosomal protein uS19.
Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
Belongs to the enoyl-CoA hydratase/isomerase family. MenB subfamily.
Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible SMC hinge near the middle of the molecule. These domains are separated by coiled-coil structures.
Required for chromosome condensation and partitioning.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Belongs to the bacterial ribosomal protein bL35 family.
The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
Belongs to the prokaryotic GSH synthase family.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.