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Database: UniProt
Entry: G9ESJ4_9GAMM
LinkDB: G9ESJ4_9GAMM
Original site: G9ESJ4_9GAMM 
ID   G9ESJ4_9GAMM            Unreviewed;       323 AA.
AC   G9ESJ4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-SEP-2017, entry version 42.
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=LDG_8268 {ECO:0000313|EMBL:EHL29975.1};
OS   Legionella drancourtii LLAP12.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=658187 {ECO:0000313|EMBL:EHL29975.1, ECO:0000313|Proteomes:UP000002770};
RN   [1] {ECO:0000313|EMBL:EHL29975.1, ECO:0000313|Proteomes:UP000002770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LLAP12 {ECO:0000313|EMBL:EHL29975.1,
RC   ECO:0000313|Proteomes:UP000002770};
RX   PubMed=22047552; DOI=10.1186/1471-2164-12-542;
RA   Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D.,
RA   Fournier P.E., Greub G.;
RT   "Insight into cross-talk between intra-amoebal pathogens.";
RL   BMC Genomics 12:542-542(2011).
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}.
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DR   EMBL; JH413843; EHL29975.1; -; Genomic_DNA.
DR   RefSeq; WP_006872150.1; NZ_JH413843.1.
DR   STRING; 658187.LDG_8268; -.
DR   EnsemblBacteria; EHL29975; EHL29975; LDG_8268.
DR   eggNOG; ENOG4105E06; Bacteria.
DR   eggNOG; COG1162; LUCA.
DR   OrthoDB; POG091H01WX; -.
DR   Proteomes; UP000002770; 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:UP000002770};
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};
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:UP000002770};
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       98    256       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      107    254       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     146    149       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     197    205       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       280    280       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       285    285       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       287    287       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       293    293       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   323 AA;  36060 MW;  F106F2CBD48672EA CRC64;
     MSKRRINKQQ SARIEKIQQT YQQNKEHHED LADGLIITRF SRHVALEDKQ GKLIRCSIRP
     NLETLVAGDR VIWQNEGTNQ GVVVSLYPRT SILAKPTHTG LSKPVAANIT QLIIVIAPKP
     EISWPLLDSY LVMAEILHLH AVILLNKTDL PCVSLKKQLT TDYQNLNYPI ILVNKDSPEG
     IEKLKELLNH QVSVFVGQSG VGKSSLISGI LPHEHDIATG ALSEISELGK HTTSNSKYYH
     LPSGGALIDS PGVREFSLGH ISAAEIARGY TEFRHYLSQC KFRNCTHKDT PNCAIINAVD
     EGIISPKRYE NFIKLCAQYM QNS
//
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