(data stored in ACNUC7421 zone)

SWISSPROT: C5BDM3_EDWI9

ID   C5BDM3_EDWI9            Unreviewed;       347 AA.
AC   C5BDM3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 2.
DT   07-JUN-2017, entry version 62.
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=NT01EI_0398 {ECO:0000313|EMBL:ACR67639.2};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67639.2, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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, ECO:0000256|SAAS:SAAS00828801}.
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00828796}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00820346}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC       RsgA subfamily. {ECO:0000256|SAAS:SAAS00720088}.
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DR   EMBL; CP001600; ACR67639.2; -; Genomic_DNA.
DR   RefSeq; WP_015869845.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0398; -.
DR   EnsemblBacteria; ACR67639; ACR67639; NT01EI_0398.
DR   GeneID; 7961226; -.
DR   KEGG; eic:NT01EI_0398; -.
DR   PATRIC; fig|634503.3.peg.361; -.
DR   eggNOG; ENOG4105E06; Bacteria.
DR   eggNOG; COG1162; LUCA.
DR   HOGENOM; HOG000006957; -.
DR   KO; K06949; -.
DR   OrthoDB; POG091H01WX; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   CDD; cd01854; YjeQ_EngC; 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;
DR   PRODOM; C5BDM3.
DR   SWISS-2DPAGE; C5BDM3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00820338};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698892};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720101};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720213};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720223};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720235};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00720226}.
FT   DOMAIN      100    270       CP-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      117    268       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     156    159       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     210    218       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       294    294       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       299    299       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       301    301       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       307    307       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   347 AA;  38464 MW;  1E1BF5859DA8CAEC CRC64;
     MSKKKLSHGQ QRRVHTNHQR RLQQTDNSAE MDDSLFGDAQ DGIVVSRFGK HADVEAADGT
     QQRCNIRRTL PSLVTGDRVV WRAALQAGSK GIIEAVHPRS SVLTRPDYYD GVKPIAANID
     QIVIVSAILP ELSLNIIDRY LVACETLCVE PLIVLNKVDL LDEEGREFVE QAMEIYRHIG
     YRVVLVSSHN GEGIVQLQDR LTQRISIFAG QSGVGKSSLL NALLPTLESQ IEVGAVSDNS
     GLGQHTTTAA RLYHFPHGGD VIDSPGVREF GLWHLDAEQI TQGFIEFRDY LGGCKFRDCK
     HGNDPGCALR EAVERGDIAE TRFDNYHRIL EGMAQVKLRK NFGNGDS
//

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