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Protein

Elongation factor P

Gene

efp

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).By similarity

Pathwayi: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.
View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein biosynthesis.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1157-MONOMER.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor P
Short name:
EF-P
Gene namesi
Name:efp
Ordered Locus Names:TTHA1125
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184Elongation factor PPRO_0000094357Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1125.

Structurei

Secondary structure

1
184
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi12 – 154Combined sources
Beta strandi18 – 3013Combined sources
Beta strandi36 – 4712Combined sources
Beta strandi49 – 557Combined sources
Beta strandi59 – 624Combined sources
Beta strandi65 – 7612Combined sources
Beta strandi79 – 846Combined sources
Turni85 – 873Combined sources
Beta strandi90 – 945Combined sources
Helixi95 – 973Combined sources
Helixi101 – 1033Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi126 – 1349Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi147 – 1537Combined sources
Beta strandi158 – 1625Combined sources
Beta strandi170 – 1745Combined sources
Turni175 – 1784Combined sources
Beta strandi179 – 1835Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UEBX-ray1.65A/B1-184[»]
4V6AX-ray3.10AV/CV1-184[»]
ProteinModelPortaliQ76G20.
SMRiQ76G20. Positions 1-184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ76G20.

Family & Domainsi

Sequence similaritiesi

Belongs to the elongation factor P family.Curated

Phylogenomic databases

eggNOGiENOG4105DRH. Bacteria.
COG0231. LUCA.
HOGENOMiHOG000010047.
KOiK02356.
OMAiMTEDGSY.
OrthoDBiEOG6JQH6Q.
PhylomeDBiQ76G20.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 2 hits.
HAMAPiMF_00141. EF_P.
InterProiIPR015365. Elong-fact-P_C.
IPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR020599. Transl_elong_fac_P/YeiP.
IPR013185. Transl_elong_KOW-like.
IPR001059. Transl_elong_P/YeiP_cen.
IPR013852. Transl_elong_P/YeiP_CS.
IPR011768. Transl_elongation_fac_P.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF01132. EFP. 1 hit.
PF08207. EFP_N. 1 hit.
PF09285. Elong-fact-P_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005901. EF-P. 1 hit.
SMARTiSM01185. EFP. 1 hit.
SM00841. Elong-fact-P_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 2 hits.
TIGRFAMsiTIGR00038. efp. 1 hit.
PROSITEiPS01275. EFP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q76G20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISVTDLRPG TKVKMDGGLW ECVEYQHQKL GRGGAKVVAK FKNLETGATV
60 70 80 90 100
ERTFNSGEKL EDIYVETREL QYLYPEGEEM VFMDLETYEQ FAVPRSRVVG
110 120 130 140 150
AEFFKEGMTA LGDMYEGQPI KVTPPTVVEL KVVDTPPGVR GDTVSGGSKP
160 170 180
ATLETGAVVQ VPLFVEPGEV IKVDTRTGEY VGRA
Length:184
Mass (Da):20,225
Last modified:July 5, 2004 - v1
Checksum:i962699782753CB30
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB103477 Genomic DNA. Translation: BAD14383.1.
AP008226 Genomic DNA. Translation: BAD70948.1.
RefSeqiWP_011173195.1. NC_006461.1.
YP_144391.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70948; BAD70948; BAD70948.
GeneIDi3169027.
KEGGittj:TTHA1125.
PATRICi23957209. VBITheThe93045_1104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB103477 Genomic DNA. Translation: BAD14383.1.
AP008226 Genomic DNA. Translation: BAD70948.1.
RefSeqiWP_011173195.1. NC_006461.1.
YP_144391.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UEBX-ray1.65A/B1-184[»]
4V6AX-ray3.10AV/CV1-184[»]
ProteinModelPortaliQ76G20.
SMRiQ76G20. Positions 1-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70948; BAD70948; BAD70948.
GeneIDi3169027.
KEGGittj:TTHA1125.
PATRICi23957209. VBITheThe93045_1104.

Phylogenomic databases

eggNOGiENOG4105DRH. Bacteria.
COG0231. LUCA.
HOGENOMiHOG000010047.
KOiK02356.
OMAiMTEDGSY.
OrthoDBiEOG6JQH6Q.
PhylomeDBiQ76G20.

Enzyme and pathway databases

UniPathwayiUPA00345.
BioCyciTTHE300852:GH8R-1157-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ76G20.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 2 hits.
HAMAPiMF_00141. EF_P.
InterProiIPR015365. Elong-fact-P_C.
IPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR020599. Transl_elong_fac_P/YeiP.
IPR013185. Transl_elong_KOW-like.
IPR001059. Transl_elong_P/YeiP_cen.
IPR013852. Transl_elong_P/YeiP_CS.
IPR011768. Transl_elongation_fac_P.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF01132. EFP. 1 hit.
PF08207. EFP_N. 1 hit.
PF09285. Elong-fact-P_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005901. EF-P. 1 hit.
SMARTiSM01185. EFP. 1 hit.
SM00841. Elong-fact-P_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 2 hits.
TIGRFAMsiTIGR00038. efp. 1 hit.
PROSITEiPS01275. EFP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiEFP_THET8
AccessioniPrimary (citable) accession number: Q76G20
Secondary accession number(s): Q5SJ89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 90 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.