ID   RSGA_CLOBJ              Reviewed;         292 AA.
AC   C1FSS3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000255|HAMAP-Rule:MF_01820};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820};
GN   Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820}; OrderedLocusNames=CLM_2803;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) 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:0000255|HAMAP-Rule:MF_01820}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01820};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820};
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_01820}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01820}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01820}.
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DR   EMBL; CP001581; ACO85769.1; -; Genomic_DNA.
DR   RefSeq; WP_003388605.1; NC_012563.1.
DR   AlphaFoldDB; C1FSS3; -.
DR   SMR; C1FSS3; -.
DR   STRING; 536232.CLM_2803; -.
DR   EnsemblBacteria; ACO85769; ACO85769; CLM_2803.
DR   KEGG; cby:CLM_2803; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_2_1_9; -.
DR   OMA; CLVAAYD; -.
DR   Proteomes; UP000001374; 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; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   PANTHER; PTHR32120; PTHR32120; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   Pfam; PF16745; RsgA_N; 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   Cytoplasm; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Ribosome biogenesis; RNA-binding; rRNA-binding; Zinc.
FT   CHAIN           1..292
FT                   /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT                   /id="PRO_1000188049"
FT   DOMAIN          64..221
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   BINDING         113..116
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         164..172
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   292 AA;  33764 MW;  FA3EDC68B67EBA38 CRC64;
     MKGTIIKGIG GFYYIKIDNS EEIIECKARG KFRHTELTPM IGDYVEISID KNNKGAIEKI
     YERRSELFRP AVANVTQALV VFSFKNPDIN IDLLNKFLLL CEYNNLKAIV CFNKMDLVNK
     EDYKDIISMI EQAGYDIIFL NAKEERNMDI IKKLIKDNVT VFCGPSGVGK STMLNKIIGK
     ETMITGNISE KLKRGKHTTR HSELIYVDEG LLVDTPGFSS LDINFMEKED LLHCIPEFRD
     FIGECKFTGC LHHREPNCAV KKAVEEGHIH KNRYDFYIKT LEEFMNRRKK KW