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Database: UniProt
Entry: T0VBT6_9ENTE
LinkDB: T0VBT6_9ENTE
Original site: T0VBT6_9ENTE 
ID   T0VBT6_9ENTE            Unreviewed;       294 AA.
AC   T0VBT6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-SEP-2017, entry version 36.
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=HSIEG1_2655 {ECO:0000313|EMBL:EQC78934.1};
OS   Enterococcus sp. HSIEG1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1316414 {ECO:0000313|EMBL:EQC78934.1, ECO:0000313|Proteomes:UP000015939};
RN   [1] {ECO:0000313|EMBL:EQC78934.1, ECO:0000313|Proteomes:UP000015939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSIEG1 {ECO:0000313|EMBL:EQC78934.1};
RX   PubMed=24336366;
RA   van den Bogert B., Boekhorst J., Smid E.J., Zoetendal E.G.,
RA   Kleerebezem M.;
RT   "Draft Genome Sequence of Enterococcus sp. Strain HSIEG1, Isolated
RT   from the Human Small Intestine.";
RL   Genome Announc. 1:e01013-13(2013).
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:SAAS00711467}.
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00711466}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00711460}.
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:EQC78934.1}.
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DR   EMBL; ASKG01000120; EQC78934.1; -; Genomic_DNA.
DR   EnsemblBacteria; EQC78934; EQC78934; HSIEG1_2655.
DR   PATRIC; fig|1316414.3.peg.996; -.
DR   OrthoDB; POG091H01WX; -.
DR   Proteomes; UP000015939; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000015939};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00711465};
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:UP000015939};
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       62    219       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN       71    217       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     111    114       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     162    170       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       243    243       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       248    248       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       250    250       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       256    256       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   294 AA;  33535 MW;  2F28789F12F4942C CRC64;
     MKGQIIKALS GFYYVESEDT IFQTRARGNF RNRKITPLVG DEVIFESSNP TDGYLLEILP
     RKNELIRPPV ANVDQGVVVT SLIQPNFSFN LLDRFLVTLE YKEIEPIIFL SKTDLVSDQS
     EVQKIAALYQ QIGYQVIVSK ADNSDLLELQ RIFPERLTVF MGQSGAGKST LLNRIVPELD
     LETAEISESL GRGKHTTRHV ELLTLYDGLV ADTPGFSSID FLEIDSGQLP KQFPEFLALA
     HQCRFRECMH LNEPNCAVKE AVEQQTVALT RYKNYVQFLE EIENRRPIYK KKNK
//
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