LEPA_ECOLI
ID LEPA_ECOLI Reviewed; 599 AA.
AC P60785; P07682; P76590; Q2MAG1;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
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=b2569, JW2553;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2987248; DOI=10.1016/s0021-9258(17)39594-7;
RA March P.E., Inouye M.;
RT "Characterization of the lep operon of Escherichia coli. Identification of
RT the promoter and the gene upstream of the signal peptidase I gene.";
RL J. Biol. Chem. 260:7206-7213(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SIMILARITY TO GTP-BINDING PROTEINS, AND SUBCELLULAR LOCATION.
RX PubMed=2999765; DOI=10.1073/pnas.82.22.7500;
RA March P.E., Inouye M.;
RT "GTP-binding membrane protein of Escherichia coli with sequence homology to
RT initiation factor 2 and elongation factors Tu and G.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7500-7504(1985).
RN [6]
RP SIMILARITY TO GTP-BINDING PROTEINS.
RX PubMed=2826164; DOI=10.1111/j.1432-1033.1987.tb13671.x;
RA Kushiro A., Shimizu M., Tomita K.;
RT "Molecular cloning and sequence determination of the tuf gene coding for
RT the elongation factor Tu of Thermus thermophilus HB8.";
RL Eur. J. Biochem. 170:93-98(1987).
RN [7]
RP FUNCTION.
RX PubMed=17110332; DOI=10.1016/j.cell.2006.09.037;
RA Qin Y., Polacek N., Vesper O., Staub E., Einfeldt E., Wilson D.N.,
RA Nierhaus K.H.;
RT "The highly conserved LepA is a ribosomal elongation factor that back-
RT translocates the ribosome.";
RL Cell 127:721-733(2006).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20045415; DOI=10.1016/j.jmb.2009.12.043;
RA Liu H., Pan D., Pech M., Cooperman B.S.;
RT "Interrupted catalysis: the EF4 (LepA) effect on back-translocation.";
RL J. Mol. Biol. 396:1043-1052(2010).
RN [9]
RP STRUCTURE BY NMR OF 1-545.
RX PubMed=19172743; DOI=10.1038/nsmb.1469;
RA Connell S.R., Topf M., Qin Y., Wilson D.N., Mielke T., Fucini P.,
RA Nierhaus K.H., Spahn C.M.;
RT "A new tRNA intermediate revealed on the ribosome during EF4-mediated back-
RT translocation.";
RL Nat. Struct. Mol. Biol. 15:910-915(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=18362332; DOI=10.1073/pnas.0801308105;
RA Evans R.N., Blaha G., Bailey S., Steitz T.A.;
RT "The structure of LepA, the ribosomal back translocase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4673-4678(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 ECO:0000269|PubMed:17110332, ECO:0000269|PubMed:20045415}.
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 ECO:0000269|PubMed:20045415};
CC -!- INTERACTION:
CC P60785; P60785: lepA; NbExp=2; IntAct=EBI-544544, EBI-544544;
CC P60785; P64423: zntB; NbExp=4; IntAct=EBI-544544, EBI-553267;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:2999765};
CC Peripheral membrane protein {ECO:0000305|PubMed:2999765}; Cytoplasmic
CC side {ECO:0000305|PubMed:2999765}.
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; K00426; AAA24063.1; -; Genomic_DNA.
DR EMBL; D64044; BAA10916.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75622.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76745.1; -; Genomic_DNA.
DR PIR; H65034; BVECLA.
DR RefSeq; NP_417064.1; NC_000913.3.
DR RefSeq; WP_000790168.1; NZ_STEB01000011.1.
DR PDB; 3CB4; X-ray; 2.80 A; A/B/C/D/E/F=1-599.
DR PDB; 3DEG; EM; -; C=1-545.
DR PDB; 3JCD; EM; 3.70 A; x=1-599.
DR PDB; 3JCE; EM; 3.20 A; x=1-599.
DR PDBsum; 3CB4; -.
DR PDBsum; 3DEG; -.
DR PDBsum; 3JCD; -.
DR PDBsum; 3JCE; -.
DR AlphaFoldDB; P60785; -.
DR SMR; P60785; -.
DR BioGRID; 4260596; 259.
DR BioGRID; 851389; 3.
DR DIP; DIP-29868N; -.
DR IntAct; P60785; 62.
DR STRING; 511145.b2569; -.
DR jPOST; P60785; -.
DR PaxDb; P60785; -.
DR PRIDE; P60785; -.
DR EnsemblBacteria; AAC75622; AAC75622; b2569.
DR EnsemblBacteria; BAE76745; BAE76745; BAE76745.
DR GeneID; 66673542; -.
DR GeneID; 947051; -.
DR KEGG; ecj:JW2553; -.
DR KEGG; eco:b2569; -.
DR PATRIC; fig|1411691.4.peg.4165; -.
DR EchoBASE; EB0524; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_6; -.
DR InParanoid; P60785; -.
DR OMA; MVQIAIQ; -.
DR PhylomeDB; P60785; -.
DR BioCyc; EcoCyc:EG10529-MON; -.
DR BioCyc; MetaCyc:EG10529-MON; -.
DR BRENDA; 3.6.5.3; 2026.
DR EvolutionaryTrace; P60785; -.
DR PRO; PR:P60785; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:EcoCyc.
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 GO; GO:0009409; P:response to cold; IMP:EcoCyc.
DR GO; GO:0009268; P:response to pH; IMP:EcoCyc.
DR GO; GO:0009651; P:response to salt stress; IMP:EcoCyc.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:EcoCyc.
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 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; GTP-binding; Hydrolase;
KW Membrane; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..599
FT /note="Elongation factor 4"
FT /id="PRO_0000176271"
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"
FT CONFLICT 156..185
FT /note="TDAVRCSAKTGVGVQDVLERLVRDIPPPEG -> HRRGALFSENRRWCAGRS
FT RTSGARHSAAGS (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="Missing (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3CB4"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3CB4"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 192..201
FT /evidence="ECO:0007829|PDB:3CB4"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 205..215
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3CB4"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 236..246
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 307..318
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:3CB4"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 335..344
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 345..357
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 396..411
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 415..424
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 447..451
FT /evidence="ECO:0007829|PDB:3CB4"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 467..477
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 480..487
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 490..500
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:3CB4"
FT HELIX 504..518
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:3CB4"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:3CB4"
SQ SEQUENCE 599 AA; 66570 MW; 91E3678557A46D49 CRC64;
MKNIRNFSII AHIDHGKSTL SDRIIQICGG LSDREMEAQV LDSMDLERER GITIKAQSVT
LDYKASDGET YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAM
EMDLEVVPVL NKIDLPAADP ERVAEEIEDI VGIDATDAVR CSAKTGVGVQ DVLERLVRDI
PPPEGDPEGP LQALIIDSWF DNYLGVVSLI RIKNGTLRKG DKVKVMSTGQ TYNADRLGIF
TPKQVDRTEL KCGEVGWLVC AIKDIHGAPV GDTLTLARNP AEKALPGFKK VKPQVYAGLF
PVSSDDYEAF RDALGKLSLN DASLFYEPES SSALGFGFRC GFLGLLHMEI IQERLEREYD
LDLITTAPTV VYEVETTSRE VIYVDSPSKL PAVNNIYELR EPIAECHMLL PQAYLGNVIT
LCVEKRGVQT NMVYHGNQVA LTYEIPMAEV VLDFFDRLKS TSRGYASLDY NFKRFQASDM
VRVDVLINGE RVDALALITH RDNSQNRGRE LVEKMKDLIP RQQFDIAIQA AIGTHIIARS
TVKQLRKNVL AKCYGGDISR KKKLLQKQKE GKKRMKQIGN VELPQEAFLA ILHVGKDNK
