ID   LEPA_PSEFL              Reviewed;         161 AA.
AC   P26843;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Elongation factor 4;
DE            Short=EF-4;
DE            EC=3.6.5.n1;
DE   AltName: Full=Ribosomal back-translocase LepA;
DE   Flags: Fragment;
GN   Name=lepA;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49323 / NCIMB 10586;
RX   PubMed=1546969; DOI=10.1042/bj2820539;
RA   Black M.T., Munn J.G.R., Allsop A.E.;
RT   "On the catalytic mechanism of prokaryotic leader peptidase 1.";
RL   Biochem. J. 282:539-543(1992).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. LepA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X56466; CAA39838.1; -; Genomic_DNA.
DR   PIR; S36680; S36680.
DR   AlphaFoldDB; P26843; -.
DR   SMR; P26843; -.
DR   STRING; 690597.JH730941_gene3340; -.
DR   eggNOG; COG0481; Bacteria.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.2570; -; 1.
DR   InterPro; IPR006297; EF-4.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR038363; LepA_C_sf.
DR   InterPro; IPR013842; LepA_CTD.
DR   PANTHER; PTHR43512; PTHR43512; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF06421; LepA_C; 1.
DR   SUPFAM; SSF54980; SSF54980; 1.
PE   3: Inferred from homology;
KW   Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           <1..161
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000176324"
FT   NON_TER         1
SQ   SEQUENCE   161 AA;  18210 MW;  5FB6924B6C47BB50 CRC64;
     GTQVQVTYDM PMNEVVLDFF DRLKSTSRGY ASLDYHFDRY QSANLVKLDL LINGDKVDAL
     ALIVHKDNAH YKGRQLTEKM KELIPRQMFD VAIQAAIGGQ IIARTSVKAL RKNVLAKCYG
     GDVSRKRKLL EKQKAGKKRM KQVGNVEVPQ EAFLAVLRLD S