ID   LEPA_VIBC1              Reviewed;         597 AA.
AC   A7MZB0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Elongation factor 4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE            Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE            EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071};
DE   AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071};
GN   Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071};
GN   OrderedLocusNames=VIBHAR_03538;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_00071};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00071}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00071}; Cytoplasmic side {ECO:0000255|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:0000255|HAMAP-Rule:MF_00071}.
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DR   EMBL; CP000789; ABU72474.1; -; Genomic_DNA.
DR   RefSeq; WP_005531645.1; NC_022269.1.
DR   AlphaFoldDB; A7MZB0; -.
DR   SMR; A7MZB0; -.
DR   EnsemblBacteria; ABU72474; ABU72474; VIBHAR_03538.
DR   KEGG; vha:VIBHAR_03538; -.
DR   PATRIC; fig|338187.25.peg.2672; -.
DR   OMA; MVQIAIQ; -.
DR   OrthoDB; 182107at2; -.
DR   Proteomes; UP000008152; Chromosome I.
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: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; cd03709; lepA_C; 1.
DR   Gene3D; 3.30.70.2570; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00071; LepA; 1.
DR   InterPro; IPR006297; EF-4.
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   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43512; PTHR43512; 1.
DR   Pfam; PF00679; EFG_C; 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   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR01393; lepA; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..597
FT                   /note="Elongation factor 4"
FT                   /id="PRO_1000032068"
FT   DOMAIN          2..184
FT                   /note="tr-type G"
FT   BINDING         14..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   BINDING         131..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   597 AA;  65992 MW;  C809B6D11003A79A CRC64;
     MKHIRNFSII AHIDHGKSTL SDRLIQVCGG LSDREMAAQV LDSMDLERER GITIKSQSVT
     LNYTAKDGET YQLNFIDTPG HVDFAYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAI
     EMDLEVVPIL NKIDLPAADP ERVAEEIEEI VGIDAMEATR CSAKTGIGVD DVLENIVSAI
     PAPEGDPDAP LQALIIDSWF DNYLGVVSLV RIKNGSLKKN DKIKVMSTGQ TWGVDRLGIF
     TPKQVDTDVL RTGEVGWVVC GIKDILGAPV GDTLTLAKNG SEKPLPGFKK VKPQVYAGLF
     PVSSDDYENF RDALGKLSLN DASLFYEPEN SAALGFGFRC GFLGMLHMEI IQERLEREYD
     LDLITTAPTV VYEVEQTNGE TMYVDSPAKL PAVNDIEEIR EPISRCNILV PADYLGNVIT
     LCVEKRGVQV DMVYHGNQVA ITYDIPMAEV VLDFFDRLKS TSRGYASLDY NFQRFEASNM
     VRVDVLLNGD KVDALALITH KDQSQTRGRQ LVEKMKEFIP RQMFDIAIQA AIGNHIIARS
     TVKQLRKNVI AKCYGGDVSR KKKLLKKQKE GKKRMKQIGN VELPQEAFLA ILHVGKD