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LEPA_PSEAE
ID   LEPA_PSEAE              Reviewed;         599 AA.
AC   Q9I5G8;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
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}; Synonyms=le;
GN   OrderedLocusNames=PA0767;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG04156.1; -; Genomic_DNA.
DR   PIR; G83550; G83550.
DR   RefSeq; NP_249458.1; NC_002516.2.
DR   RefSeq; WP_003085555.1; NZ_QZGE01000007.1.
DR   AlphaFoldDB; Q9I5G8; -.
DR   SMR; Q9I5G8; -.
DR   STRING; 287.DR97_1216; -.
DR   PaxDb; Q9I5G8; -.
DR   PRIDE; Q9I5G8; -.
DR   EnsemblBacteria; AAG04156; AAG04156; PA0767.
DR   GeneID; 881998; -.
DR   KEGG; pae:PA0767; -.
DR   PATRIC; fig|208964.12.peg.797; -.
DR   PseudoCAP; PA0767; -.
DR   HOGENOM; CLU_009995_3_3_6; -.
DR   InParanoid; Q9I5G8; -.
DR   OMA; MVQIAIQ; -.
DR   PhylomeDB; Q9I5G8; -.
DR   BioCyc; PAER208964:G1FZ6-780-MON; -.
DR   Proteomes; UP000002438; 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:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
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; 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   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   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR01393; lepA; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 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; Reference proteome.
FT   CHAIN           1..599
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000176323"
FT   DOMAIN          5..187
FT                   /note="tr-type G"
FT   BINDING         17..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   599 AA;  66295 MW;  5F9F4A56427AE4FC CRC64;
     MSDLSHIRNF SIIAHIDHGK STLADRFIQM CGGLSDREME AQVLDSMDLE RERGITIKAH
     SVTLHYKAQD GKTYQLNFID TPGHVDFTYE VSRSLAACEG ALLVVDAGQG VEAQSVANCY
     TAIEQGLEVM PVLNKMDLPQ AEPERVKEEI ESIIGIDATD AVACSAKSGM GVLEVLERLV
     TAIPAPEGEI EAPLQALIID SWFDNYLGVV SLVRVKNGRV KKGDKILVKS TGKVHQVDSV
     GVFTPKHTET VDLKAGEVGF IIAGIKDIHG APVGDTLTLN NTPDVEVLPG FKRVKPQVYA
     GLFPVSSDDF EDFRDALQKL TLNDSSLQYE PESSEALGFG FRCGFLGMLH MEIIQERLER
     EYDLDLITTA PTVVFEIVQK NGEIIYVDNP SKLPDLASIQ EMREPICRAT ILVPKDHLGN
     VITLCIEKRG VQRDMHFLSG QVQVVYDLPM NEVVLDFFDR LKSTSRGYAS LDYSFDRFEP
     SNLVRLDVLI NGEKVDALAL IVHRDNAPYK GRQLVEKMKE LIPRQMFDVA IQAAIGGQII
     ARSTVKALRK NVLAKCYGGD VSRKRKLLEK QKAGKKRMKQ VGSVEIPQEA FLAVLKVDS
 
 
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