(data stored in ACNUC7421 zone)

SWISSPROT: Q47SI6_THEFY

ID   Q47SI6_THEFY            Unreviewed;       353 AA.
AC   Q47SI6;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 99.
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=Tfu_0543 {ECO:0000313|EMBL:AAZ54581.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54581.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01820};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01820};
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|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00720088}.
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DR   EMBL; CP000088; AAZ54581.1; -; Genomic_DNA.
DR   RefSeq; WP_011290990.1; NC_007333.1.
DR   STRING; 269800.Tfu_0543; -.
DR   EnsemblBacteria; AAZ54581; AAZ54581; Tfu_0543.
DR   KEGG; tfu:Tfu_0543; -.
DR   eggNOG; ENOG4105E06; Bacteria.
DR   eggNOG; COG1162; LUCA.
DR   HOGENOM; HOG000006959; -.
DR   KO; K06949; -.
DR   OMA; FRDCKHL; -.
DR   OrthoDB; 908180at2; -.
DR   BioCyc; TFUS269800:G1G4Q-554-MONOMER; -.
DR   Proteomes; UP000000434; 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; 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; Q47SI6.
DR   SWISS-2DPAGE; Q47SI6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
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:SAAS00064626};
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:SAAS00447475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
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      109    286       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      118    284       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     158    161       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     204    212       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       310    310       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       314    314       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       316    316       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       321    321       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   353 AA;  38253 MW;  EF65C8DA8612C6FD CRC64;
     MRDGRYLDID EDDVRVRARG GSRPRTRKRP KHENARLGFV TAVNRGRYQC LVGDLSVVAM
     KARELGRGSI VVGDIVALVG DLSGRPGTLA RIVRVEKRSS VLRRTADDTD PVERVIVANA
     DQMVIVTALA DPDPQPRFID RCLVAAYEAG LDPLLCLTKS DLASPDALLD IYAPLGLRWV
     VTRRDGDLSA LREQLMGRIS VLVGPSGVGK STLVNLLVPE ARRAVGDVNV VTGRGRHTST
     SAVALPIGAP ASAESVERLH AAREGRIDRS ELDYGWIIDT PGVRSFGLAH VTPDDLLAAF
     PDLDDAVADC PDHCSHLGDG CALDEWLARG ELNPARVTSF RRLLASREGE LER
//

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