Elongation factor 4 - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P60785 (LEPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Elongation factor 4
Short name=EF-4
EC=3.6.5.n1

Alternative name(s):
Ribosomal back-translocase LepA

Gene names

Name:	lepA
Ordered Locus Names:	b2569, JW2553

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner. Ref.7 Ref.8
Catalytic activity	GTP + H₂O = GDP + phosphate. Ref.8
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Probable Ref.5.
Sequence similarities	Belongs to the GTP-binding elongation factor family. LepA subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay Ref.7. Source: EcoCyc translation elongation factor activity Inferred from direct assay Ref.7. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 599

599

Elongation factor 4 HAMAP MF_00071

PRO_0000176271

Regions

Nucleotide binding

14 – 19

GTP By similarity

Nucleotide binding

131 – 134

GTP By similarity

Experimental info

Sequence conflict

156 – 185

TDAVR…PPPEG → HRRGALFSENRRWCAGRSRT SGARHSAAGS Ref.1

Sequence conflict

156 – 185

TDAVR…PPPEG → HRRGALFSENRRWCAGRSRT SGARHSAAGS Ref.2

Sequence conflict

266

Missing Ref.1

Sequence conflict

266

Missing Ref.2

Secondary structure

599

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P60785 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: 91E3678557A46D49
Show »

FASTA

599

66,570

        10         20         30         40         50         60 
MKNIRNFSII AHIDHGKSTL SDRIIQICGG LSDREMEAQV LDSMDLERER GITIKAQSVT 

        70         80         90        100        110        120 
LDYKASDGET YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAM 

       130        140        150        160        170        180 
EMDLEVVPVL NKIDLPAADP ERVAEEIEDI VGIDATDAVR CSAKTGVGVQ DVLERLVRDI 

       190        200        210        220        230        240 
PPPEGDPEGP LQALIIDSWF DNYLGVVSLI RIKNGTLRKG DKVKVMSTGQ TYNADRLGIF 

       250        260        270        280        290        300 
TPKQVDRTEL KCGEVGWLVC AIKDIHGAPV GDTLTLARNP AEKALPGFKK VKPQVYAGLF 

       310        320        330        340        350        360 
PVSSDDYEAF RDALGKLSLN DASLFYEPES SSALGFGFRC GFLGLLHMEI IQERLEREYD 

       370        380        390        400        410        420 
LDLITTAPTV VYEVETTSRE VIYVDSPSKL PAVNNIYELR EPIAECHMLL PQAYLGNVIT 

       430        440        450        460        470        480 
LCVEKRGVQT NMVYHGNQVA LTYEIPMAEV VLDFFDRLKS TSRGYASLDY NFKRFQASDM 

       490        500        510        520        530        540 
VRVDVLINGE RVDALALITH RDNSQNRGRE LVEKMKDLIP RQQFDIAIQA AIGTHIIARS 

       550        560        570        580        590 
TVKQLRKNVL AKCYGGDISR KKKLLQKQKE GKKRMKQIGN VELPQEAFLA ILHVGKDNK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the lep operon of Escherichia coli. Identification of the promoter and the gene upstream of the signal peptidase I gene." March P.E., Inouye M. J. Biol. Chem. 260:7206-7213(1985) [PubMed: 2987248] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	Nashimoto H., Saito N. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"GTP-binding membrane protein of Escherichia coli with sequence homology to initiation factor 2 and elongation factors Tu and G." March P.E., Inouye M. Proc. Natl. Acad. Sci. U.S.A. 82:7500-7504(1985) [PubMed: 2999765] [Abstract] Cited for: SIMILARITY TO GTP-BINDING PROTEINS, SUBCELLULAR LOCATION.
[6]	"Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8." Kushiro A., Shimizu M., Tomita K. Eur. J. Biochem. 170:93-98(1987) [PubMed: 2826164] [Abstract] Cited for: SIMILARITY TO GTP-BINDING PROTEINS.
[7]	"The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome." Qin Y., Polacek N., Vesper O., Staub E., Einfeldt E., Wilson D.N., Nierhaus K.H. Cell 127:721-733(2006) [PubMed: 17110332] [Abstract] Cited for: FUNCTION.
[8]	"Interrupted catalysis: the EF4 (LepA) effect on back-translocation." Liu H., Pan D., Pech M., Cooperman B.S. J. Mol. Biol. 396:1043-1052(2010) [PubMed: 20045415] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[9]	"A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation." Connell S.R., Topf M., Qin Y., Wilson D.N., Mielke T., Fucini P., Nierhaus K.H., Spahn C.M. Nat. Struct. Mol. Biol. 15:910-915(2008) [PubMed: 19172743] [Abstract] Cited for: STRUCTURE BY NMR OF 1-545.
[10]	"The structure of LepA, the ribosomal back translocase." Evans R.N., Blaha G., Bailey S., Steitz T.A. Proc. Natl. Acad. Sci. U.S.A. 105:4673-4678(2008) [PubMed: 18362332] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K00426 Genomic DNA. Translation: AAA24063.1.
D64044 Genomic DNA. Translation: BAA10916.1.
U00096 Genomic DNA. Translation: AAC75622.1.
AP009048 Genomic DNA. Translation: BAE76745.1.

PIR

BVECLA. H65034.

RefSeq

NP_417064.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CB4	X-ray	2.80	A/B/C/D/E/F	1-599	[»]
3DEG	electron microscopy	-	C	1-545	[»]

ProteinModelPortal

P60785.

SMR

P60785. Positions 1-555.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29868N.

IntAct

P60785. 20 interactions.

MINT

MINT-1225739.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000357; EBESCP00000000357; EBESCG00000000291.
EBESCT00000016683; EBESCP00000015974; EBESCG00000015742.

GeneID

947051.

GenomeReviews

Gene locus JW2553 in contig AP009048_GR.
Gene locus b2569 in contig U00096_GR.

KEGG

ecj:JW2553.
eco:b2569.

PATRIC

32120537. VBIEscCol129921_2671.

Organism-specific databases

EchoBASE

EB0524.

EcoGene

EG10529. lepA.

Phylogenomic databases

eggNOG

COG0481.

GeneTree

EBGT00050000008367.

HOGENOM

HBG286375.

OMA

KCYGGDA.

PhylomeDB

P60785.

ProtClustDB

PRK05433.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10529-MONOMER.

Gene expression databases

Genevestigator

P60785.

Family and domain databases

HAMAP

MF_00071. LepA.
[Tree]

InterPro

IPR006297. EF-4.
IPR009022. Elongation_fac_G/III/V.
IPR013842. LepA_GTP-bd_C.
IPR000795. ProtSyn_GTP-bd.
IPR005225. Small_GTP-bd_dom.
IPR000640. Transl_elong_EFG/EF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

Gene3D

G3DSA:3.30.70.240. Transl_elong_EFG/EF2_C. 1 hit.

K03596.

PANTHER

PTHR23115:SF40. PTHR23115:SF40. 1 hit.

Pfam

PF00679. EFG_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF06421. LepA_C. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

SMART

SM00838. EFG_C. 1 hit.
[Graphical view]

SUPFAM

SSF54980. EFG_III_V. 2 hits.
SSF50447. Translat_factor. 1 hit.

TIGRFAMs

TIGR01393. LepA. 1 hit.
TIGR00231. Small_GTP. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LEPA_ECOLI

Accession

Primary (citable) accession number: P60785
Secondary accession number(s): P07682, P76590, Q2MAG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 13, 2004
Last modified:	January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents