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Database: UniProt
Entry: W6TGU1_9SPIR
LinkDB: W6TGU1_9SPIR
Original site: W6TGU1_9SPIR 
ID   W6TGU1_9SPIR            Unreviewed;       313 AA.
AC   W6TGU1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-SEP-2017, entry version 31.
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   ORFNames=BDCR2A_00120 {ECO:0000313|EMBL:ETZ18147.1};
OS   Borrelia duttonii CR2A.
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=1432657 {ECO:0000313|EMBL:ETZ18147.1, ECO:0000313|Proteomes:UP000019148};
RN   [1] {ECO:0000313|EMBL:ETZ18147.1, ECO:0000313|Proteomes:UP000019148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR2A {ECO:0000313|EMBL:ETZ18147.1,
RC   ECO:0000313|Proteomes:UP000019148};
RA   Schwan T.G., Raffel S.J., Porcella S.F.;
RT   "Comparative genomics of relapsing fever spirochetes.";
RL   Submitted (DEC-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ETZ18147.1}.
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DR   EMBL; AZIT01000001; ETZ18147.1; -; Genomic_DNA.
DR   RefSeq; WP_038365934.1; NZ_AZIT01000001.1.
DR   EnsemblBacteria; ETZ18147; ETZ18147; BDCR2A_00120.
DR   PATRIC; fig|1432657.3.peg.114; -.
DR   Proteomes; UP000019148; Unassembled WGS sequence.
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   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   Complete proteome {ECO:0000313|Proteomes:UP000019148};
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, ECO:0000313|EMBL:ETZ18147.1};
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:UP000019148};
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       79    237       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN       89    235       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     129    132       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     180    188       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       261    261       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       266    266       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       268    268       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       274    274       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   313 AA;  36068 MW;  4692D58BCED9D371 CRC64;
     MNSSTFEVLW GVNNIYSVVE VNTNTVYEGV IKGKFLNTRE KEYSPLVPGD FVCGDIYDEH
     KVYIKERMER RNVFWRYNKK VALRQVIVSN IDNILIVSSA TLPEFKNSFI DRTLIVAEEQ
     GITPIILVNK VDEGINLRVD SFIKIYEYLG YRVIKTSVVT LQGIDEVKKI IKNSRTSFIG
     QSGVGKSSLI NVIDLNASQA INEISYKYAR GRHTTVYAVA FHSDNKILID TPGIKEFGIE
     GLGYLELKYH FKEFKYFNDL CRFNSCLHIN EPNCFVISQI GFKIAEARYN SYLKIFSELK
     RYKSYAREIF GKN
//
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