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LEPA_CLAM3
ID   LEPA_CLAM3              Reviewed;         615 AA.
AC   A5CR97;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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}; OrderedLocusNames=CMM_1555;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382;
RX   PubMed=18192381; DOI=10.1128/jb.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA   Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00071};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00071};
CC       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; AM711867; CAN01602.1; -; Genomic_DNA.
DR   RefSeq; WP_012038242.1; NC_009480.1.
DR   AlphaFoldDB; A5CR97; -.
DR   SMR; A5CR97; -.
DR   STRING; 443906.CMM_1555; -.
DR   EnsemblBacteria; CAN01602; CAN01602; CMM_1555.
DR   GeneID; 56885874; -.
DR   KEGG; cmi:CMM_1555; -.
DR   eggNOG; COG0481; Bacteria.
DR   HOGENOM; CLU_009995_3_3_11; -.
DR   OMA; MVQIAIQ; -.
DR   OrthoDB; 182107at2; -.
DR   Proteomes; UP000001564; 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; 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; 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; 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 membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..615
FT                   /note="Elongation factor 4"
FT                   /id="PRO_1000031987"
FT   DOMAIN          17..198
FT                   /note="tr-type G"
FT   BINDING         29..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   BINDING         145..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   615 AA;  67049 MW;  76063D383011BAA3 CRC64;
     MSPLASKALR PAATDPASIR NFCIIAHIDH GKSTLADRML QMTGVVDSRS MRAQYLDRMD
     IERERGITIK SQAVRMPWEL DGQTYALNMI DTPGHVDFSY EVSRSLAACE GAILLVDAAQ
     GIEAQTLANL YLALENDLTI IPVLNKIDLP AADPDKYAAE LASLIGGDPS DVLRVSGKTG
     AGVEDLLDRV SRTIPAPVGD PDAAARAMIF DSVYDAYRGV VTYVRMIDGK LSPREKISMM
     STRATHEILE IGVSSPEPTP SDGLGVGEVG YLITGVKDVR QSKVGDTVTT AARPATEALP
     GYTEPLPMVF SGLYPIDGSD YPDLRDALDK LKLSDAALVY EPETSVALGF GFRCGFLGLL
     HLEIITERLS REFGLDLITT APSVIYEVTS EDKKTVTVTN PSEFPGGKIV SVSEPVVKAA
     ILAPKDYVGT IMELCQSRRG ILLGMEYLGE DRVEVRYTMP LGEIVFDFFD NLKSKTAGYA
     SLDYEPAGSQ DSDLVKVDIL LQGEQVDAFS AIVHRDKAYA YGVLMTGRLR ELIPRQQFEV
     PIQAAIGARI IARESIRAMR KDVLAKCYGG DITRKRKLLE KQKEGKKRMK MVGRVEVPQE
     AFIAALSGDT EKKAK
 
 
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