P0A7C6 (PEPE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidase E
EC=3.4.13.21

Alternative name(s):
Alpha-aspartyl dipeptidase
Asp-specific dipeptidase
Dipeptidase E

Gene names

Name:	pepE
Ordered Locus Names:	b4021, JW3981

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids By similarity. HAMAP-Rule MF_00510
Catalytic activity	Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides. HAMAP-Rule MF_00510
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase S51 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Dipeptidase Hydrolase Protease Serine protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dipeptidase activity Inferred from electronic annotation. Source: HAMAP peptidase activity Inferred from direct assay PubMed 9928148. Source: EcoCyc serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pepB	P37095	1	EBI-555623,EBI-549539

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 229	229	Peptidase E HAMAP-Rule MF_00510		PRO_0000209955
Sites
	Active site	120	1	Charge relay system By similarity
	Active site	135	1	Charge relay system By similarity
	Active site	157	1	Charge relay system By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A7C6 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 53D4D8395DFC63FD	FASTA	229	24,570
	10 20 30 40 50 60 MELLLLSNST LPGKAWLEHA LPLIAEQLQG RRSAVFIPFA GVTQTWDDYT AKTAAVLAPL 70 80 90 100 110 120 GVSVTGIHSV VDPVAAIENA EIVIVGGGNT FQLLKQCRER GLLAPITDVV KRGALYIGWS 130 140 150 160 170 180 AGANLACPTI RTTNDMPIVD PQGFDALNLF PLQINPHFTN ALPEGHKGET REQRIRELLV 190 200 210 220 VAPELTIIGL PEGNWITVSK GHATLGGPNT TYVFKAGEEA VPLEAGHRF

References

[1]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00006 Genomic DNA. Translation: AAC43115.1. U00096 Genomic DNA. Translation: AAC76991.1. AP009048 Genomic DNA. Translation: BAE78023.1.
PIR	D65209.
RefSeq	NP_418445.1. NC_000913.2. YP_492164.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A7C6.
SMR	P0A7C6. Positions 1-229.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48072N.
IntAct	P0A7C6. 4 interactions.
MINT	MINT-1236370.
STRING	511145.b4021.
Protein family/group databases
MEROPS	S51.001.
Proteomic databases
PaxDb	P0A7C6.
PRIDE	P0A7C6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76991; AAC76991; b4021. BAE78023; BAE78023; BAE78023.
GeneID	12933661. 948520.
KEGG	ecj:Y75_p3908. eco:b4021.
PATRIC	32123571. VBIEscCol129921_4134.
Organism-specific databases
EchoBASE	EB1864.
EcoGene	EG11920. pepE.
Phylogenomic databases
eggNOG	COG3340.
HOGENOM	HOG000281834.
KO	K05995.
OMA	SIHTTND.
ProtClustDB	PRK05282.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11920-MONOMER. ECOL316407:JW3981-MONOMER. MetaCyc:EG11920-MONOMER.
Gene expression databases
Genevestigator	P0A7C6.
Family and domain databases
HAMAP	MF_00510. Peptidase_E.
InterPro	IPR005320. Peptidase_S51. IPR023172. Peptidase_S51_dipeptidase-E. [Graphical view]
Pfam	PF03575. Peptidase_S51. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PEPE_ECOLI

Accession

Primary (citable) accession number: P0A7C6
Secondary accession number(s): P32666, Q2M6T3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program