ID A1VMA3_POLNA Unreviewed; 302 AA. AC A1VMA3; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 107. 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 OrderedLocusNames=Pnap_1467 {ECO:0000313|EMBL:ABM36781.1}; OS Polaromonas naphthalenivorans (strain CJ2). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM36781.1, ECO:0000313|Proteomes:UP000000644}; RN [1] {ECO:0000313|Proteomes:UP000000644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644}; RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x; RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.; RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal RT tar-contaminated sediment, reveals physiological and metabolic versatility RT and evolution through extensive horizontal gene transfer."; RL Environ. Microbiol. 11:2253-2270(2009). 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; Evidence={ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; CP000529; ABM36781.1; -; Genomic_DNA. DR AlphaFoldDB; A1VMA3; -. DR STRING; 365044.Pnap_1467; -. DR KEGG; pna:Pnap_1467; -. DR eggNOG; COG1162; Bacteria. DR HOGENOM; CLU_033617_2_0_4; -. DR Proteomes; UP000000644; Chromosome. 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; cd04466; S1_YloQ_GTPase; 1. 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 InterPro; IPR031944; RsgA_N. DR NCBIfam; TIGR00157; ribosome small subunit-dependent GTPase A; 1. 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 PROSITE; PS50936; ENGC_GTPASE; 1. DR PROSITE; PS51721; G_CP; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01820}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_01820}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01820}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01820}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01820}; Reference proteome {ECO:0000313|Proteomes:UP000000644}; KW 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 60..230 FT /note="CP-type G" FT /evidence="ECO:0000259|PROSITE:PS51721" FT DOMAIN 71..228 FT /note="EngC GTPase" FT /evidence="ECO:0000259|PROSITE:PS50936" FT BINDING 110..113 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" FT BINDING 170..178 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" 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 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" FT BINDING 261 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" FT BINDING 267 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820" SQ SEQUENCE 302 AA; 33313 MW; 79B7B89F2939C4D9 CRC64; MVVAGFGRHV LVETESGQRL ICHPRGKKSQ VVVGDRIRWL PSQDEGTIEK IEERSNLFYR QDEMRTKSFA ANLDQILILI AAEPEFSESQ LTRALIAAEA ERIKPIIALN KSDLAEPFGR AWTKLAPYRA MGYQVLPLAI KPKTAAAPAN DGQTAELMAL LHGKKTLVLG PSGAGKSSLT NLLVPQAKVL TAEISQALNS GKHTTTSTTL YWVDEARTTA LIDSPGFQEF GLHHIDPMQL ANYMPDFKAH AQDCKFYNCT HLHEPGCGVI SEVKSTVSAS SISANRYRLY SELFAELSQT RY //