http://togogenome.org/gene/2860336:K1X15_RS09575 ^@ http://purl.uniprot.org/uniprot/A0A8G0G1N1 ^@ Function|||Similarity|||Subunit ^@ Belongs to the universal ribosomal protein uS10 family.|||Involved in the binding of tRNA to the ribosomes.|||Part of the 30S ribosomal subunit. http://togogenome.org/gene/2860336:K1X15_RS18985 ^@ http://purl.uniprot.org/uniprot/A0A8G0CN43 ^@ Similarity|||Subcellular Location Annotation ^@ Belongs to the binding-protein-dependent transport system permease family.|||Cell inner membrane|||Cell membrane http://togogenome.org/gene/2860336:K1X15_RS08635 ^@ http://purl.uniprot.org/uniprot/A0A8G0CRS4 ^@ Similarity ^@ Belongs to the bacterial ribosomal protein bL33 family. http://togogenome.org/gene/2860336:K1X15_RS03080 ^@ http://purl.uniprot.org/uniprot/A0A8G0CRX7 ^@ Function|||Similarity|||Subcellular Location Annotation ^@ Belongs to the ATPase C chain family.|||Cell membrane|||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.|||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.|||Membrane http://togogenome.org/gene/2860336:K1X15_RS19000 ^@ http://purl.uniprot.org/uniprot/A0A8G0CNC5 ^@ Subcellular Location Annotation ^@ Cell inner membrane http://togogenome.org/gene/2860336:K1X15_RS18975 ^@ http://purl.uniprot.org/uniprot/A0A8G0G575 ^@ Similarity|||Subcellular Location Annotation ^@ Belongs to the ABC transporter superfamily.|||Cell inner membrane|||Membrane http://togogenome.org/gene/2860336:K1X15_RS20740 ^@ http://purl.uniprot.org/uniprot/A0A8G0CPN3 ^@ Similarity ^@ Belongs to the bacterial ribosomal protein bL35 family. http://togogenome.org/gene/2860336:K1X15_RS05860 ^@ http://purl.uniprot.org/uniprot/A0A8G0G167 ^@ Function|||PTM|||Similarity|||Subcellular Location Annotation ^@ 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.|||Cytoplasm http://togogenome.org/gene/2860336:K1X15_RS17050 ^@ http://purl.uniprot.org/uniprot/A0A8G0CPE6 ^@ Similarity ^@ Belongs to the bacterial ribosomal protein bL36 family. http://togogenome.org/gene/2860336:K1X15_RS02325 ^@ http://purl.uniprot.org/uniprot/A0A8G0CTC2 ^@ Function|||Similarity|||Subcellular Location Annotation|||Subunit ^@ Belongs to the IF-1 family.|||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.|||Cytoplasm|||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. http://togogenome.org/gene/2860336:K1X15_RS15970 ^@ http://purl.uniprot.org/uniprot/A0A8G0CLY3 ^@ Similarity ^@ Belongs to the bacterial ribosomal protein bL34 family. http://togogenome.org/gene/2860336:K1X15_RS20650 ^@ http://purl.uniprot.org/uniprot/A0A8G0CRM5 ^@ Function|||Similarity|||Subunit ^@ Belongs to the bacterial histone-like protein family.|||Heterodimer of an alpha and a beta chain.|||This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. http://togogenome.org/gene/2860336:K1X15_RS09595 ^@ http://purl.uniprot.org/uniprot/A0A8G0CV55 ^@ Function|||Similarity|||Subunit ^@ 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. http://togogenome.org/gene/2860336:K1X15_RS07770 ^@ http://purl.uniprot.org/uniprot/A0A8G0G1H6 ^@ Function|||Similarity|||Subunit ^@ Belongs to the P(II) protein family.|||Homotrimer.|||In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. 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 uridylylated to P-II-UMP, these events are reversed. http://togogenome.org/gene/2860336:K1X15_RS07320 ^@ http://purl.uniprot.org/uniprot/A0A8G0CR09 ^@ Function|||Similarity|||Subcellular Location Annotation ^@ 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).|||Cytoplasm http://togogenome.org/gene/2860336:K1X15_RS09480 ^@ http://purl.uniprot.org/uniprot/A0A8G0CU57 ^@ Similarity|||Subunit ^@ Belongs to the universal ribosomal protein uL30 family.|||Part of the 50S ribosomal subunit. http://togogenome.org/gene/2860336:K1X15_RS07800 ^@ http://purl.uniprot.org/uniprot/A0A8G0CUH8 ^@ Similarity ^@ Belongs to the bacterial histone-like protein family. http://togogenome.org/gene/2860336:K1X15_RS09455 ^@ http://purl.uniprot.org/uniprot/A0A8G0CRS1 ^@ Function|||Similarity|||Subunit ^@ 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. http://togogenome.org/gene/2860336:K1X15_RS01615 ^@ http://purl.uniprot.org/uniprot/A0A8G0CUI9 ^@ Similarity|||Subcellular Location Annotation ^@ Belongs to the chromate ion transporter (CHR) (TC 2.A.51) family.|||Membrane http://togogenome.org/gene/2860336:K1X15_RS09535 ^@ http://purl.uniprot.org/uniprot/A0A8G0CT81 ^@ Function|||Similarity|||Subunit ^@ 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.|||Part of the 50S ribosomal subunit. http://togogenome.org/gene/2860336:K1X15_RS02605 ^@ http://purl.uniprot.org/uniprot/A0A8G0G1D1 ^@ Function|||Similarity|||Subcellular Location Annotation|||Subunit ^@ Belongs to the GroES chaperonin family.|||Cytoplasm|||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.