Escherichia coli K-12 substr. MG1655 Enzyme: peptidase E, a dipeptidase where amino-terminal residue is aspartate

Gene: pepE Accession Numbers: EG11920 (EcoCyc), b4021, ECK4013

Regulation Summary Diagram: ?

Regulation summary diagram for pepE

PepE hydrolyzes peptides bond in dipeptides where the first amino acid is aspartate [Zhang98e].

Locations: cytosol

Map Position: [4,227,476 <- 4,228,165] (91.12 centisomes, 328°)
Length: 690 bp / 229 aa

Molecular Weight of Polypeptide: 24.57 kD (from nucleotide sequence)

pI: 4.7 [Zhang98e]

Unification Links: ASAP:ABE-0013146 , CGSC:34261 , DIP:DIP-48072N , EchoBASE:EB1864 , EcoGene:EG11920 , EcoliWiki:b4021 , Mint:MINT-1236370 , ModBase:P0A7C6 , OU-Microarray:b4021 , PortEco:pepE , PR:PRO_000023510 , Pride:P0A7C6 , Protein Model Portal:P0A7C6 , RefSeq:NP_418445 , RegulonDB:EG11920 , SMR:P0A7C6 , String:511145.b4021 , Swiss-Model:P0A7C6 , UniProt:P0A7C6

Relationship Links: InterPro:IN-FAMILY:IPR005320 , InterPro:IN-FAMILY:IPR023172 , InterPro:IN-FAMILY:IPR029062 , Pfam:IN-FAMILY:PF03575

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006508 - proteolysis Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
Molecular Function: GO:0008233 - peptidase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Zhang98e]
GO:0008236 - serine-type peptidase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016805 - dipeptidase activity Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer protein related turnover, degradation
metabolism degradation of macromolecules proteins/peptides/glycopeptides

Essentiality data for pepE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Enzymatic reaction of: dipeptidase

EC Number:

a dipetide with an N-terminal L-aspartate + H2O <=> L-aspartate + a standard α amino acid

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

T(opt): 25 °C [Zhang98e]

pH(opt): 7.2 [Zhang98e]

Sequence Features

Protein sequence of peptidase E, a dipeptidase where amino-terminal residue is aspartate with features indicated

Feature Class Location Citations Comment
Active-Site 120
UniProt: Charge relay system; Non-Experimental Qualifier: by similarity;
Active-Site 135
UniProt: Charge relay system; Non-Experimental Qualifier: by similarity;
Active-Site 157
UniProt: Charge relay system; Non-Experimental Qualifier: by similarity;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b4021 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11920.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Zhang98e: Zhang H, Zhang J, Wang X, Yang W, Lu J (1998). "Biochemical characterization of alpha-aspartyl dipeptidase. Cloning and expression of its gene." Ann N Y Acad Sci 864;621-5. PMID: 9928148

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Oct 9, 2015, biocyc13.