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Database: UniProt
Entry: A0A075TZD6_9LACT
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ID   A0A075TZD6_9LACT        Unreviewed;       304 AA.
AC   A0A075TZD6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 26.
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=WS74_0324 {ECO:0000313|EMBL:AIM62576.1};
OS   Weissella ceti.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae;
OC   Weissella.
OX   NCBI_TaxID=759620 {ECO:0000313|EMBL:AIM62576.1, ECO:0000313|Proteomes:UP000029079};
RN   [1] {ECO:0000313|Proteomes:UP000029079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS74 {ECO:0000313|Proteomes:UP000029079};
RA   Figueiredo H.C.P., Leal C.A.G., Pereira F.L., Soares S.C.,
RA   Dorella F.A., Carvalho A.F., Azevedo V.A.C.;
RT   "Complete genome of Weissella ceti strain WS74 isolated from diseased
RT   rainbow trout in Brazil.";
RL   Submitted (AUG-2014) 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: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}.
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DR   EMBL; CP009223; AIM62576.1; -; Genomic_DNA.
DR   RefSeq; WP_009495874.1; NZ_CP009224.1.
DR   EnsemblBacteria; AIM62576; AIM62576; WS74_0324.
DR   KEGG; wce:WS08_0324; -.
DR   KEGG; wci:WS105_0322; -.
DR   KEGG; wct:WS74_0324; -.
DR   PATRIC; fig|759620.7.peg.310; -.
DR   KO; K06949; -.
DR   Proteomes; UP000029079; 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:UP000029079};
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:UP000029079};
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       66    227       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN       75    225       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     115    118       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     170    178       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       251    251       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       256    256       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       258    258       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       264    264       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   304 AA;  34362 MW;  63B53CC8AE6ED288 CRC64;
     MPNYHGQIQL SLAGFYDVMT DDGQLIRTRA RGNFRKRDIK PMVGDFVEFS VEPPEDGYIL
     SIDERRNSLV RPPVSNVDQA IVVTSVKIPE FSTNLLDRQL VALEEKSIEP VIYISKTDLL
     SAEEFAELSE IIDGYRAAGY DAILPESSFD DASLAEVKER MPNQLTVLMG QTGAGKSTLL
     NHLVPGLELE TGEVSEALMR GKHTTRQVGL IEMFDGLVAD TPGFSAFEVF DMDARDLTHY
     FREFNRLSPM CKYRGCVHLN EPECAVKEAL EAGDIMASRY HNYKEFYDLI EGRRPVYNKH
     DKKH
//
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