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Database: UniProt
Entry: K6U9R1_9CLOT
LinkDB: K6U9R1_9CLOT
Original site: K6U9R1_9CLOT 
ID   K6U9R1_9CLOT            Unreviewed;       290 AA.
AC   K6U9R1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-SEP-2017, entry version 39.
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=A370_03443 {ECO:0000313|EMBL:EKQ53999.1};
OS   Clostridium sp. Maddingley MBC34-26.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ53999.1, ECO:0000313|Proteomes:UP000001325};
RN   [1] {ECO:0000313|EMBL:EKQ53999.1, ECO:0000313|Proteomes:UP000001325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX   PubMed=23405323;
RA   Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA   Midgley D.J., Hendry P.;
RT   "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from
RT   Coal-Seam Gas Formation Water.";
RL   Genome Announc. 1:E00081-12(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:EKQ53999.1}.
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DR   EMBL; ALXI01000110; EKQ53999.1; -; Genomic_DNA.
DR   PATRIC; fig|1196322.3.peg.3355; -.
DR   Proteomes; UP000001325; 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; 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:UP000001325};
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:UP000001325};
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       61    218       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN       70    216       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     110    113       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     161    169       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   290 AA;  33094 MW;  585C4ED85B7DB276 CRC64;
     MDGKIIKGIG GFYYIKTDAG LIECKARGKF RHKDIKPMVG DNVTIKMEHG KGVIEEIHKR
     KSQLVRPTVA NVSLAFIVFA VKNPDINFDL LNKFLILCEF NNIEVIVCLN KIDLVTEEER
     EEIKKRINDI GYEVLFINAK VGIGIDGLKE KIKGNTTVFC GPSGAGKSTL INKLSNAEHM
     ETGKVSEKIG RGKHTTRHSE LIEVSDGYIV DTPGFSTLEI KDLMDKDSLK YCFPEFEQYN
     DKCKFRGCLH FKEPNCAVKE AVQEEKINKY RYDFYIKTLE EIIEEEKNKW
//
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