ID A0A432Q1C2_9AQUI Unreviewed; 295 AA. AC A0A432Q1C2; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 31-JUL-2019, entry version 4. 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; 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 RT discovered 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 CC maturation steps of the functional core of the 30S ribosomal CC subunit. Helps release RbfA from mature subunits. May play a role CC in the assembly of ribosomal proteins into the subunit. Circularly CC permuted GTPase that catalyzes slow GTP hydrolysis, GTPase CC activity is stimulated by the 30S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_01820}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01820}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC 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. CC RsgA subfamily. {ECO:0000256|HAMAP-Rule:MF_01820, CC ECO:0000256|SAAS:SAAS00535129}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 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; PTHR32120; 1. DR Pfam; PF03193; RsgA_GTPase; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00157; TIGR00157; 1. DR PROSITE; PS50936; ENGC_GTPASE; 1. DR PROSITE; PS51721; G_CP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000287362}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820, KW ECO:0000256|SAAS:SAAS00064626}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820, KW ECO:0000256|SAAS:SAAS00211110}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820, KW ECO:0000256|SAAS:SAAS00211158}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01820, KW ECO:0000256|SAAS:SAAS00447475}; KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820, KW ECO:0000256|SAAS:SAAS01203909}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820, KW ECO:0000256|SAAS:SAAS01203910}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820, KW ECO:0000256|SAAS:SAAS01203911}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00211157}. FT DOMAIN 64 224 CP-type G. {ECO:0000259|PROSITE:PS51721}. FT DOMAIN 73 222 EngC GTPase. {ECO:0000259|PROSITE: FT PS50936}. FT NP_BIND 113 116 GTP. {ECO:0000256|HAMAP-Rule:MF_01820}. FT NP_BIND 167 175 GTP. {ECO:0000256|HAMAP-Rule:MF_01820}. FT METAL 247 247 Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}. FT METAL 252 252 Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}. FT METAL 254 254 Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}. FT METAL 260 260 Zinc. {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 //