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Protein

Elongation factor P

Gene

efp

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation.UniRule annotation

Pathway: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.UniRule annotation
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-22-MONOMER.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor PUniRule annotation
Short name:
EF-PUniRule annotation
Gene namesi
Name:efpUniRule annotation
Ordered Locus Names:BUsg_021
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 187187Elongation factor PPRO_0000094216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341N6-(3,6-diaminohexanoyl)-5-hydroxylysineUniRule annotation

Post-translational modificationi

May be beta-lysylated on the epsilon-amino group of Lys-34 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC (if this protein is present). Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety may extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. Hydroxylation of the C5 position on Lys-34 may allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA.UniRule annotation

Keywords - PTMi

Hydroxylation

Interactioni

Protein-protein interaction databases

STRINGi198804.BUsg021.

Structurei

3D structure databases

ProteinModelPortaliQ8KA80.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the elongation factor P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0231.
KOiK02356.
OMAiDYVFMDM.
OrthoDBiEOG6JQH6Q.

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.
SMARTiSM00841. 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.

Q8KA80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVYHSNNFR SGRKIIFEKE PCLIESSEFV KPGKGQSFVR VKLRKLLTKQ
60 70 80 90 100
LIEKTFKSTD SLEIADVSEY TLSYLYNDGH FWYFINNNFE ELSVDKKIVG
110 120 130 140 150
VNKKWLSEQD TCVITFWNNQ AISITPNIFV ELKVIDTEIA LKSDTINTTT
160 170 180
KLATLSTGAI LKVPLFIQIG SLIKVDTRSG EYVSRIK
Length:187
Mass (Da):21,469
Last modified:October 1, 2002 - v1
Checksum:i86C6C324DACF059D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67593.1.
RefSeqiNP_660382.1. NC_004061.1.
WP_011053559.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67593; AAM67593; BUsg_021.
KEGGibas:BUsg021.
PATRICi21246799. VBIBucAph100086_0021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67593.1.
RefSeqiNP_660382.1. NC_004061.1.
WP_011053559.1. NC_004061.1.

3D structure databases

ProteinModelPortaliQ8KA80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198804.BUsg021.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM67593; AAM67593; BUsg_021.
KEGGibas:BUsg021.
PATRICi21246799. VBIBucAph100086_0021.

Phylogenomic databases

eggNOGiCOG0231.
KOiK02356.
OMAiDYVFMDM.
OrthoDBiEOG6JQH6Q.

Enzyme and pathway databases

UniPathwayiUPA00345.
BioCyciBAPH198804:GHMG-22-MONOMER.

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.
SMARTiSM00841. 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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiEFP_BUCAP
AccessioniPrimary (citable) accession number: Q8KA80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: April 29, 2015
This is version 82 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

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.