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A6LJK6 (A6LJK6_THEM4) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Elongation factor 4 HAMAP-Rule MF_00071

Short name=EF-4 HAMAP-Rule MF_00071
EC=3.6.5.n1 HAMAP-Rule MF_00071
Alternative name(s):
Ribosomal back-translocase LepA HAMAP-Rule MF_00071
Gene names
Name:lepA HAMAP-Rule MF_00071
Ordered Locus Names:Tmel_0233 EMBL ABR30107.1
OrganismThermosipho melanesiensis (strain BI429 / DSM 12029) [Complete proteome] [HAMAP] EMBL ABR30107.1
Taxonomic identifier391009 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00071

Catalytic activity

GTP + H2O = GDP + phosphate. HAMAP-Rule MF_00071

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP-Rule MF_00071.

Sequence similarities

Belongs to the GTP-binding elongation factor family. LepA subfamily. HAMAP-Rule MF_00071

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding14 – 196GTP By similarity HAMAP-Rule MF_00071
Nucleotide binding132 – 1354GTP By similarity HAMAP-Rule MF_00071

Sequences

Sequence LengthMass (Da)Tools
A6LJK6 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: F9C84D751045143E

FASTA60367,748
        10         20         30         40         50         60 
MKNVRNISII AHIDHGKTTL SDRILEITGA VEKRKMREQF LDSMDIERER GITIKSHPLR 

        70         80         90        100        110        120 
VFYKSKKNGK VYEINIVDTP GHVDFTYEVD RSLAAVEGVI LLVDASQGVQ AQTVANAYKA 

       130        140        150        160        170        180 
IEHNLEIIPV INKIDLPNAN IPETELEIED LIGISSEEIL KVSAKEGIGV EDVLEAIIGR 

       190        200        210        220        230        240 
VPSPKGTENE KLSALIFDAK YDKYRGVITY VRVFNGEIKP GDKIMTYSNK QVYEVVETGV 

       250        260        270        280        290        300 
FTPDMTPIEK LKAGDIGYII AGIKEVSLAK IGDTITNATD PVEEPLPGYK EIKPMVFAGM 

       310        320        330        340        350        360 
YPGVPEYYEE LRKALEKLKL NDSSLTFYPD HSPALGFGFR CGFLGLLHMD VVRERLEREF 

       370        380        390        400        410        420 
EMTVILTAPN VEYKVILKNG EEVIVNDPAK FPDESMIQEV YEPYVKLSII TPPEYLGKLM 

       430        440        450        460        470        480 
NLVQNEKRGI MTSTENAGFE RVVLNFEVPL AEIIFDFFDK MKASSRGYAS MDYEMIGYRK 

       490        500        510        520        530        540 
SELVKITILV NKEPVDALSI IAHKNKAYAM ARKLVDKLAE LIPQHQFEIP VQARAGGRII 

       550        560        570        580        590        600 
ARSTIKALRK DVLAKCYGGD VTRKMKLLQK QKEGKKRLRE IGSVSIPQEA FLALLKVGED 


ENK 

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References

[1]"Complete sequence of Thermosipho melanesiensis BI429."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BI429 / DSM 12029.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000716 Genomic DNA. Translation: ABR30107.1.
RefSeqYP_001305492.1. NC_009616.1.

3D structure databases

ProteinModelPortalA6LJK6.
SMRA6LJK6. Positions 1-549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391009.Tmel_0233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR30107; ABR30107; Tmel_0233.
GeneID5298035.
KEGGtme:Tmel_0233.
PATRIC23921577. VBITheMel19269_0242.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0481.
HOGENOMHOG000020624.
KOK03596.
OMAKPMVFCG.
OrthoDBEOG6ZKXQ4.
ProtClustDBPRK05433.

Enzyme and pathway databases

BioCycTMEL391009:GHM1-246-MONOMER.

Family and domain databases

Gene3D3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_00071. LepA.
InterProIPR006297. EF-4.
IPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR013842. LepA_GTP-bd_C.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamPF00679. EFG_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF06421. LepA_C. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SMARTSM00838. EFG_C. 1 hit.
[Graphical view]
SUPFAMSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsTIGR01393. lepA. 1 hit.
TIGR00231. small_GTP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA6LJK6_THEM4
AccessionPrimary (citable) accession number: A6LJK6
Entry history
Integrated into UniProtKB/TrEMBL: July 24, 2007
Last sequence update: July 24, 2007
Last modified: April 16, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)