ID A0A432Q1C2_9AQUI Unreviewed; 295 AA. AC A0A432Q1C2; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 28-JUN-2023, entry version 14. DE RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000256|HAMAP-Rule:MF_01820}; DE EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01820}; GN Name=rsgA {ECO:0000256|HAMAP-Rule:MF_01820, GN ECO:0000313|EMBL:RUM32051.1}; GN ORFNames=DSY42_01770 {ECO:0000313|EMBL:RUM32051.1}; OS Aquifex sp. OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=313370 {ECO:0000313|EMBL:RUM32051.1, ECO:0000313|Proteomes:UP000287362}; RN [1] {ECO:0000313|EMBL:RUM32051.1, ECO:0000313|Proteomes:UP000287362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAG 11 {ECO:0000313|EMBL:RUM32051.1}; RA Trembath-Reichert E., Huber J.A.; RT "Combined omics and stable isotope probing to characterize newly discovered RT Mariana Back-Arc vent microbial communities."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: One of several proteins that assist in the late maturation CC steps of the functional core of the 30S ribosomal subunit. Helps CC release RbfA from mature subunits. May play a role in the assembly of CC ribosomal proteins into the subunit. Circularly permuted GTPase that CC catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S CC ribosomal subunit. {ECO:0000256|HAMAP-Rule:MF_01820}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01820}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01820}; CC -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S CC rRNA. {ECO:0000256|HAMAP-Rule:MF_01820}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820}. CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01820}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RUM32051.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QNXQ01000037; RUM32051.1; -; Genomic_DNA. DR AlphaFoldDB; A0A432Q1C2; -. DR Proteomes; UP000287362; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule. DR CDD; cd01854; YjeQ_EngC; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_01820; GTPase_RsgA; 1. DR InterPro; IPR030378; G_CP_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA. DR InterPro; IPR010914; RsgA_GTPase_dom. DR PANTHER; PTHR32120; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA; 1. DR PANTHER; PTHR32120:SF11; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA 1, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF03193; RsgA_GTPase; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00157; ribosome small subunit-dependent GTPase A; 1. DR PROSITE; PS50936; ENGC_GTPASE; 1. DR PROSITE; PS51721; G_CP; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_01820}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01820}; Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01820}. FT DOMAIN 64..224 FT /note="CP-type G" FT /evidence="ECO:0000259|PROSITE:PS51721" FT DOMAIN 73..222 FT /note="EngC GTPase" FT /evidence="ECO:0000259|PROSITE:PS50936" FT BINDING 113..116 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" FT BINDING 167..175 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" FT BINDING 254 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" FT BINDING 260 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" SQ SEQUENCE 295 AA; 34138 MW; 5B892DEA58EB7549 CRC64; MKRAIVIDRE AQMIEVYTLD DKETYRGIPR GKVLKKTKIY AGDYVWGEVI DKNTFAIEEV EERKNLLIRP RVANVNRIIV VQTLKMPEFN NYLLDNLLVV YEYFGVEPVI VFNKVDILDE EERKELDYWI NIYKNAGYDV LKVSAKLSEG IDNLVNYLEG FICILAGPSG VGKSSILSKL TGTQLRTQEV SEKTERGRHT TTGVRLIPFG KGSFIGDTPG FSKVEATMFI KWREIRKYFR EFLAYQCKYP DCTHTNEPEC AVKEAVKEGE ISCERYKSYL KMIKVYLEDI KELCK //