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.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Belongs to the 2Fe2S plant-type ferredoxin family.
2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.
Belongs to the reaction center PufL/M/PsbA/D family.
C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth.
Cyanobacteriota usually contain more than 2 copies of the psbA gene.
Cyanobacteriotal 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, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.
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.
Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
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 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.
Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Belongs to the sulfate adenylyltransferase family.
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.
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.
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.
A core subunit of photosystem II (PSII).
Belongs to the bacterial microcompartments protein family. CcmK subfamily.
Belongs to the bacterial microcompartments protein family. CsoS1 subfamily.
Homohexamer. Interacts with CcmN and CcmO in the carboxysome.
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 bacterial histone-like protein family.
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.
Belongs to the phosphoglycerate kinase family.
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.
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 CcmL/EutN family. CcmL subfamily.
Homopentamer. Interacts with full-length CcmM.
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.
Belongs to the geranylgeranyl reductase family. ChlP subfamily.
Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Belongs to the cytochrome b family. PetD subfamily.
Belongs to the phycobilisome linker protein 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.
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 1 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.
Seems to be required for the assembly of the photosystem I complex.
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.
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.
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.
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. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB to form the KaiB(6):KaiC(6) complex, leading to changes in output regulators CikA and SasA. KaiB switches to a thioredoxin-like fold (KaiB(fs)) when bound to KaiC. KaiB(6):KaiC(6) formation exposes a site for KaiA binding that sequesters KaiA from KaiC, making the KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC autodephosphorylation.
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. Undergoes a major conformational rearrangment; in the free state forms homotetramers as a dimer of dimers. When bound to the CI domain of KaiC switches to a monomeric thioredoxin-fold (KaiB(fs)). KaiB(fs) binds CikA, leading it to dephosphorylate phospho-RpaA.
Belongs to the aldehyde decarbonylase family.
Catalyzes the decarbonylation of fatty aldehydes to alkanes.
Belongs to the bacterial ribosomal protein bL28 family.
May help in the organization of the PsaE and PsaF subunits.
Lacks conserved residue(s) required for the propagation of feature annotation.
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
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 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 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 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 4-hydroxybenzoyl-CoA thioesterase family. DHNA-CoA hydrolase subfamily.
Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA), a reaction involved in phylloquinone (vitamin K1) biosynthesis.
Belongs to the adrenodoxin/putidaredoxin family.
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.
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.
Belongs to the bacterial ribosomal protein bS16 family.
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.
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.
Heterodimer of an alpha subunit and a beta subunit. Cyanobacterial 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, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
Heterodimer of an alpha subunit and a beta subunit. Cyanobacteriotal 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, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
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 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.
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 T.elongatus and T.vulcanus, this is probably not true.
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.
Monomer. Forms a complex with a monomeric, partially assembled PSII. This is probably the complex in which D1 is assembled and/or replaced.
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 some small extrinsic subunits and thus assembly of calcium-manganese-oxide cluster.
Belongs to the cytochrome c family. PsbV subfamily.
Binds 1 heme c group covalently per subunit.
Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
The cyanobacterial oxygen-evolving complex is composed of PsbO, PsbP, PsbQ, PsbV and PsbU.
Belongs to the PsbX family. Type 1 subfamily.
Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
PSII consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. PSII forms dimeric complexes.
Belongs to the bacterial ribosomal protein bS21 family.
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).
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Belongs to the universal ribosomal protein uS9 family.
Belongs to the RNA polymerase subunit omega family.
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.
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.
Belongs to the complex I subunit 4L 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. Cyanobacteriotal NDH-1 also plays a role in inorganic carbon-concentration.
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.
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 bacterial ribosomal protein bL36 family.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell.
The gas vesicle shell is 2 nm thick and consists of a single layer of this protein. It forms helical ribs nearly perpendicular to the long axis of the vesicle.