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Q8KA80 (EFP_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor P

Short name=EF-P
Gene names
Name:efp
Ordered Locus Names:BUsg_021
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00141

Pathway

Protein biosynthesis; polypeptide chain elongation. HAMAP-Rule MF_00141

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00141.

Post-translational modification

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 By similarity. HAMAP-Rule MF_00141

Sequence similarities

Belongs to the elongation factor P family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   Molecular functionElongation factor
   PTMHydroxylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpeptide biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontranslation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 187187Elongation factor P HAMAP-Rule MF_00141
PRO_0000094216

Amino acid modifications

Modified residue341N6-(3,6-diaminohexanoyl)-5-hydroxylysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q8KA80 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 86C6C324DACF059D

FASTA18721,469
        10         20         30         40         50         60 
MRVYHSNNFR SGRKIIFEKE PCLIESSEFV KPGKGQSFVR VKLRKLLTKQ LIEKTFKSTD 

        70         80         90        100        110        120 
SLEIADVSEY TLSYLYNDGH FWYFINNNFE ELSVDKKIVG VNKKWLSEQD TCVITFWNNQ 

       130        140        150        160        170        180 
AISITPNIFV ELKVIDTEIA LKSDTINTTT KLATLSTGAI LKVPLFIQIG SLIKVDTRSG 


EYVSRIK 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67593.1.
RefSeqNP_660382.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8KA80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg021.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67593; AAM67593; BUsg_021.
GeneID1005837.
KEGGbas:BUsg021.
PATRIC21246799. VBIBucAph100086_0021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0231.
KOK02356.
OMAGKGQAFS.
OrthoDBEOG6JQH6Q.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-22-MONOMER.
UniPathwayUPA00345.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
2.40.50.140. 2 hits.
HAMAPMF_00141. EF_P.
InterProIPR015365. 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]
PfamPF01132. EFP. 1 hit.
PF08207. EFP_N. 1 hit.
PF09285. Elong-fact-P_C. 1 hit.
[Graphical view]
PIRSFPIRSF005901. EF-P. 1 hit.
SMARTSM00841. Elong-fact-P_C. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 2 hits.
TIGRFAMsTIGR00038. efp. 1 hit.
PROSITEPS01275. EFP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEFP_BUCAP
AccessionPrimary (citable) accession number: Q8KA80
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names