ID   RSGA_STAS1              Reviewed;         291 AA.
AC   Q49X02;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SSP1551;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18696.1; -; Genomic_DNA.
DR   RefSeq; WP_011303295.1; NZ_MTGA01000034.1.
DR   AlphaFoldDB; Q49X02; -.
DR   SMR; Q49X02; -.
DR   STRING; 342451.SSP1551; -.
DR   EnsemblBacteria; BAE18696; BAE18696; SSP1551.
DR   KEGG; ssp:SSP1551; -.
DR   PATRIC; fig|342451.11.peg.1553; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_2_1_9; -.
DR   OMA; CLVAAYD; -.
DR   OrthoDB; 908180at2; -.
DR   Proteomes; UP000006371; 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   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding; Zinc.
FT   CHAIN           1..291
FT                   /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT                   /id="PRO_0000171522"
FT   DOMAIN          63..221
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   BINDING         112..115
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   291 AA;  33871 MW;  65BC07D94871942B CRC64;
     MKTGRIIKSI SGVYRVDVDG EMYDTKPRGL FRKNKFSPIV GDVVDFEVEN VTEGYIHHVH
     ERKNEIKRPP VSNVDHLIIV MSAVEPDFST QLLDRFLVIA HSYHMRPRIL VTKKDLTSLE
     KQHDIEKLLE VYENMSYKTQ FISINEDIEQ VFSSWGDGLA VLSGQSGVGK STLLNKYFPN
     IEIETQHISK ALNRGRHTTR HVELFERAKG FIADTPGFSA LDYDHIQKDE IKNYFMEIHE
     YGATCKFRDC NHINEPKCNV KAELENGNIA QFRYDHYLQL FKEISNRKER Y