GenomeNet

Database: UniProt
Entry: I7JAT4_9RICK
LinkDB: I7JAT4_9RICK
Original site: I7JAT4_9RICK 
ID   I7JAT4_9RICK            Unreviewed;       599 AA.
AC   I7JAT4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Elongation factor 4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE            Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE            EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_00071};
DE   AltName: Full=Ribosomal back-translocase LepA {ECO:0000256|HAMAP-Rule:MF_00071};
GN   Name=lepA {ECO:0000256|HAMAP-Rule:MF_00071};
GN   ORFNames=wOo_06690 {ECO:0000313|EMBL:CCF78268.1};
OS   Wolbachia endosymbiont of Onchocerca ochengi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=100901 {ECO:0000313|EMBL:CCF78268.1, ECO:0000313|Proteomes:UP000007516};
RN   [1] {ECO:0000313|EMBL:CCF78268.1, ECO:0000313|Proteomes:UP000007516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Adamawa_Cameroon {ECO:0000313|Proteomes:UP000007516};
RX   PubMed=22919073; DOI=10.1101/gr.138420.112;
RA   Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA   Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA   Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT   "Analysis of gene expression from the Wolbachia genome of a filarial
RT   nematode supports both metabolic and defensive roles within the
RT   symbiosis.";
RL   Genome Res. 22:2467-2477(2012).
CC   -!- FUNCTION: Required for accurate and efficient protein synthesis under
CC       certain stress conditions. May act as a fidelity factor of the
CC       translation reaction, by catalyzing a one-codon backward translocation
CC       of tRNAs on improperly translocated ribosomes. Back-translocation
CC       proceeds from a post-translocation (POST) complex to a pre-
CC       translocation (PRE) complex, thus giving elongation factor G a second
CC       chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-
CC       dependent manner. {ECO:0000256|HAMAP-Rule:MF_00071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00071};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00071};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00071}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. LepA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005454, ECO:0000256|HAMAP-Rule:MF_00071}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE660029; CCF78268.1; -; Genomic_DNA.
DR   RefSeq; WP_014869053.1; NC_018267.1.
DR   AlphaFoldDB; I7JAT4; -.
DR   STRING; 100901.wOo_06690; -.
DR   KEGG; woo:wOo_06690; -.
DR   PATRIC; fig|100901.6.peg.544; -.
DR   eggNOG; COG0481; Bacteria.
DR   HOGENOM; CLU_009995_3_3_5; -.
DR   Proteomes; UP000007516; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR   CDD; cd03699; EF4_II; 1.
DR   CDD; cd16260; EF4_III; 1.
DR   CDD; cd01890; LepA; 1.
DR   CDD; cd03709; lepA_C; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00071; LepA; 1.
DR   InterPro; IPR006297; EF-4.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR038363; LepA_C_sf.
DR   InterPro; IPR013842; LepA_CTD.
DR   InterPro; IPR035654; LepA_IV.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   NCBIfam; TIGR01393; lepA; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF06421; LepA_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00071};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00071};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00071};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00071}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007516}.
FT   DOMAIN          2..184
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         14..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT   BINDING         131..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   599 AA;  67151 MW;  5FCABD6245E9AC45 CRC64;
     MNKIRNFAII AHIDHGKSTL ADRLIEWCNA LEAREMTNQV LDSMEIERKR GITIKAQTVK
     LSYTANDGNQ YCLNLIDTPG HVDFSYEVSR SLAACEGSLL IVDSSQGIEA QTLANVYRAI
     ENNHEIIVVL NKVDLPAADP EMVKLQIGEV IGIDTSNSIL ISAKTGLGIR DVLEAIVTKL
     PAPRGDIDAP LQAILIDSWY DTYLGVVILV RVKNGILKKG MRIIMMSNNA TYQVDNIGIF
     TPKKVMTGEL STGEIGFITA SIKKVTDCKV GDTITEEIRP CSKALPGFKE VHPVVFCSIF
     PDKTDNFKYL KEALEKLHLN DASFTFETET SNALGYGFRC GFLGILHLEV IQERLEREFN
     LSLTVTAPSV IYKITTQNGK ILNTHNSNEI PDLTKIKIVE EPWITATIIT PDQYLGEIIS
     LCEERRGKQK DLSYIGNTST TLLKYKLPLS EVVFDFYDRL KSISKGYSSL DWKVSDYQES
     QVDKLTFLVN GKLVDALTCI IHKSRVEKRG REICSRLKDL IPRQQYKIII QAAVSGKIIA
     KEIINPYRKD VTAKLYGGDV TRKMKLLEKQ KKGKKKLYSI GRVVNIPHNT FIQALKIND
//
DBGET integrated database retrieval system