Q8KA80 (EFP_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor P
Short name=EF-P

Gene names

Name:	efp
Ordered Locus Names:	BUsg_021

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
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 process	Protein biosynthesis
Cellular component	Cytoplasm
Molecular function	Elongation factor
PTM	Hydroxylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	peptide biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	translation elongation factor activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 187	187	Elongation factor P HAMAP-Rule MF_00141		PRO_0000094216
Amino acid modifications
	Modified residue	34	1	N6-(3,6-diaminohexanoyl)-5-hydroxylysine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8KA80 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 86C6C324DACF059D	FASTA	187	21,469
	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

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.
RefSeq	NP_660382.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8KA80.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg021.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67593; AAM67593; BUsg_021.
GeneID	1005837.
KEGG	bas:BUsg021.
PATRIC	21246799. VBIBucAph100086_0021.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0231.
KO	K02356.
OMA	DSAKWLQ.
ProtClustDB	PRK00529.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-94-MONOMER.
UniPathway	UPA00345.
Family and domain databases
Gene3D	2.30.30.30. 1 hit. 2.40.50.140. 2 hits.
HAMAP	MF_00141. EF-P.
InterPro	IPR015365. 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]
Pfam	PF01132. EFP. 1 hit. PF08207. EFP_N. 1 hit. PF09285. Elong-fact-P_C. 1 hit. [Graphical view]
PIRSF	PIRSF005901. EF-P. 1 hit.
SMART	SM00841. Elong-fact-P_C. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 2 hits. SSF50104. Transl_SH3_like. 1 hit.
TIGRFAMs	TIGR00038. efp. 1 hit.
PROSITE	PS01275. EFP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EFP_BUCAP

Accession

Primary (citable) accession number: Q8KA80

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program