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RSGA1_LISMO
ID   RSGA1_LISMO             Reviewed;         346 AA.
AC   Q8Y7F0;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA 1 {ECO:0000255|HAMAP-Rule:MF_01820};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820};
GN   Name=rsgA1 {ECO:0000255|HAMAP-Rule:MF_01820}; OrderedLocusNames=lmo1332;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591978; CAC99410.1; -; Genomic_DNA.
DR   PIR; AD1241; AD1241.
DR   RefSeq; NP_464857.1; NC_003210.1.
DR   RefSeq; WP_010990097.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y7F0; -.
DR   SMR; Q8Y7F0; -.
DR   STRING; 169963.lmo1332; -.
DR   PaxDb; Q8Y7F0; -.
DR   EnsemblBacteria; CAC99410; CAC99410; CAC99410.
DR   GeneID; 987715; -.
DR   KEGG; lmo:lmo1332; -.
DR   PATRIC; fig|169963.11.peg.1369; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_0_1_9; -.
DR   OMA; RFHDCAH; -.
DR   PhylomeDB; Q8Y7F0; -.
DR   BioCyc; LMON169963:LMO1332-MON; -.
DR   Proteomes; UP000000817; 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; cd01854; YjeQ_EngC; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01820; GTPase_RsgA; 1.
DR   InterPro; IPR030378; G_CP_dom.
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; 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..346
FT                   /note="Small ribosomal subunit biogenesis GTPase RsgA 1"
FT                   /id="PRO_0000171492"
FT   DOMAIN          93..248
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         190..198
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   346 AA;  39107 MW;  D88DD421E8976378 CRC64;
     MILEQYGITS FFKEQKIAAT SSYGRVTAVF RDYYRVITEN EEFLASLKRG NFYELSSTSL
     PTVGDFVEIS GDLQILSVLE RKTVFSRMNK DSAEQLIAAN FDYALIVMSL NHDFNLNRLE
     RYLTVAWDSG ATPIIILTKA DLVEDLSFYA QQLEAVAYGV PAYYVDNLSH HGFEALESDL
     KPNSTLILLG SSGVGKSSFI NSLAGTDLMK TAGIREDDSK GKHTTTHREM HLLSNGWIVI
     DTPGMREFGV GFNQAGLETT FSDVEELAEG CRFHDCSHTQ EPNCAVQAAL EDGTLTMQHY
     ENWLKLQREM AYHARKNSPA LARQERDRWK VIQKSMRTHF KTRPKK
 
 
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