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Protein

Elongation factor 4

Gene

lepA

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

GTP + H2O = GDP + phosphate.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 216GTPUniRule annotation1 Publication
Nucleotide bindingi133 – 1364GTPUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-1235-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 4UniRule annotation (EC:3.6.5.n1UniRule annotation)
Short name:
EF-4UniRule annotation
Alternative name(s):
Ribosomal back-translocase LepAUniRule annotation
Gene namesi
Name:lepAUniRule annotation
Ordered Locus Names:aq_1725
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 600600Elongation factor 4PRO_0000176223Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224324.aq_1725.

Structurei

Secondary structure

1
600
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi6 – 127Combined sources
Helixi19 – 3012Combined sources
Beta strandi60 – 667Combined sources
Beta strandi72 – 787Combined sources
Helixi84 – 863Combined sources
Helixi87 – 959Combined sources
Beta strandi98 – 1058Combined sources
Turni106 – 1083Combined sources
Helixi112 – 12312Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi137 – 1393Combined sources
Helixi142 – 15110Combined sources
Helixi157 – 1593Combined sources
Beta strandi161 – 1644Combined sources
Turni165 – 1684Combined sources
Helixi171 – 18111Combined sources
Beta strandi194 – 20310Combined sources
Turni204 – 2063Combined sources
Beta strandi207 – 21913Combined sources
Beta strandi224 – 2274Combined sources
Turni228 – 2303Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi238 – 25013Combined sources
Beta strandi257 – 2637Combined sources
Helixi267 – 2693Combined sources
Beta strandi275 – 2817Combined sources
Beta strandi297 – 3037Combined sources
Helixi309 – 32012Combined sources
Beta strandi327 – 3337Combined sources
Turni334 – 3363Combined sources
Beta strandi337 – 34610Combined sources
Helixi347 – 36115Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi374 – 3785Combined sources
Beta strandi385 – 3895Combined sources
Helixi390 – 3923Combined sources
Helixi397 – 3993Combined sources
Beta strandi400 – 41516Combined sources
Helixi416 – 4183Combined sources
Helixi419 – 42810Combined sources
Beta strandi432 – 4409Combined sources
Beta strandi443 – 4519Combined sources
Helixi452 – 46615Combined sources
Turni467 – 4693Combined sources
Beta strandi472 – 48211Combined sources
Beta strandi485 – 49612Combined sources
Helixi498 – 5003Combined sources
Beta strandi502 – 5054Combined sources
Helixi506 – 5083Combined sources
Helixi509 – 52315Combined sources
Beta strandi531 – 5377Combined sources
Beta strandi540 – 5478Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YWEX-ray2.05A1-600[»]
2YWFX-ray2.24A1-600[»]
2YWGX-ray2.94A1-600[»]
2YWHX-ray2.24A1-600[»]
ProteinModelPortaliO67618.
SMRiO67618. Positions 1-551.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67618.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 186183tr-type GAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C4S. Bacteria.
COG0481. LUCA.
HOGENOMiHOG000020624.
InParanoidiO67618.
KOiK03596.
OMAiKPMVFCG.
OrthoDBiEOG6ZKXQ4.

Family and domain databases

Gene3Di3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00071. LepA.
InterProiIPR006297. EF-4.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR031157. G_TR_CS.
IPR013842. LepA_GTP-bd_C.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF06421. LepA_C. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR01393. lepA. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O67618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQKNVRNFC IIAHVDHGKS TLADRLLEYT GAISEREKRE QLLDTLDVER
60 70 80 90 100
ERGITVKMQA VRMFYKAKDG NTYKLHLIDT PGHVDFSYEV SRALAACEGA
110 120 130 140 150
LLLIDASQGI EAQTVANFWK AVEQDLVIIP VINKIDLPSA DVDRVKKQIE
160 170 180 190 200
EVLGLDPEEA ILASAKEGIG IEEILEAIVN RIPPPKGDPQ KPLKALIFDS
210 220 230 240 250
YYDPYRGAVA FVRIFDGEVK PGDKIMLMST GKEYEVTEVG AQTPKMTKFD
260 270 280 290 300
KLSAGDVGYI AASIKDVRDI RIGDTITHAK NPTKEPVPGF QPAKPMVYAG
310 320 330 340 350
IYPAEDTTYE ELRDALEKYA INDAAIVYEP ESSPALGMGF RVGFLGLLHM
360 370 380 390 400
EIVQERLERE YGVKIITTAP NVIYRVKKKF TDEVIEVRNP MDFPDNAGLI
410 420 430 440 450
EYVEEPFVLV TIITPKEYVG PIIQLCQEKR GIQKNMTYLD PNTVYLEYEM
460 470 480 490 500
PLSEIIVDFH DKIKSISRGF ASYDYEFIGY RPSDLIKLTV LINKKPVDAL
510 520 530 540 550
SFIVHADRAQ KFARRVAEKL RETIPRQLFE VHIQVAKGGK VIASERIKPL
560 570 580 590 600
RANVTAKCYG GDVTRKKKLL ENQKEGKKRM KQFGKVQLPQ EAFLSVLKVE
Length:600
Mass (Da):67,657
Last modified:August 1, 1998 - v1
Checksum:iEA69B32A062D3081
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07583.1.
PIRiH70448.
RefSeqiNP_214184.1. NC_000918.1.
WP_010881121.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07583; AAC07583; aq_1725.
GeneIDi1193333.
KEGGiaae:aq_1725.
PATRICi20960442. VBIAquAeo85532_1326.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07583.1.
PIRiH70448.
RefSeqiNP_214184.1. NC_000918.1.
WP_010881121.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YWEX-ray2.05A1-600[»]
2YWFX-ray2.24A1-600[»]
2YWGX-ray2.94A1-600[»]
2YWHX-ray2.24A1-600[»]
ProteinModelPortaliO67618.
SMRiO67618. Positions 1-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_1725.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07583; AAC07583; aq_1725.
GeneIDi1193333.
KEGGiaae:aq_1725.
PATRICi20960442. VBIAquAeo85532_1326.

Phylogenomic databases

eggNOGiENOG4105C4S. Bacteria.
COG0481. LUCA.
HOGENOMiHOG000020624.
InParanoidiO67618.
KOiK03596.
OMAiKPMVFCG.
OrthoDBiEOG6ZKXQ4.

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-1235-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO67618.

Family and domain databases

Gene3Di3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00071. LepA.
InterProiIPR006297. EF-4.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR031157. G_TR_CS.
IPR013842. LepA_GTP-bd_C.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF06421. LepA_C. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR01393. lepA. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.
  2. "Crystal structures of GTP-binding protein lepA from Aquifex aeolicus."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GTP.

Entry informationi

Entry nameiLEPA_AQUAE
AccessioniPrimary (citable) accession number: O67618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: February 17, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.