UniProt Accession

 PEPD_ECOLI; P15288 

Genbank Protein ID

 M34034; U70214; U00096; AP009048; X14790 

Genbank Nucleotide ID

 AAA16111.1; AAB08657.1; AAC73341.1; BAA77906.1; CAA32892.1 

Protein Name

 Cytosol non-specific dipeptidase 

Protein Synonyms/Alias

 Aminoacyl-histidine dipeptidase; Beta-alanyl-histidine dipeptidase; Carnosinase; Cysteinylglycinase; Peptidase D; Xaa-His dipeptidase; X-His dipeptidase 

Gene Name

 pepD 

Gene Synonyms/Alias

 pepH; b0237; JW0227 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
41	EYIVGWAKEKGFHVE	acetylation	[1]
43	IVGWAKEKGFHVERD	acetylation	[1]
69	TAGMENRKPVVLQAH	acetylation	[2]
93	DTVHDFTKDPIQPYI	acetylation	[1]
106	YIDGEWVKARGTTLG	acetylation	[1]
205	PAGFETFKLTLKGLK	acetylation	[1]
209	ETFKLTLKGLKGGHS	acetylation	[1]
212	KLTLKGLKGGHSGGE	acetylation	[2]
277	ADKVDVLKSLVNTYQ	acetylation	[1, 2]
288	NTYQEILKNELAEKE	acetylation	[1]
294	LKNELAEKEKNLALL	acetylation	[1]
296	NELAEKEKNLALLLD	acetylation	[1, 2, 3]
309	LDSVANDKAALIAKS	acetylation	[1, 2]
315	DKAALIAKSRDTFIR	acetylation	[1]
372	RSLIDSGKDYVVSML	acetylation	[1, 2]
384	SMLDSLGKLAGAKTE	acetylation	[1]
389	LGKLAGAKTEAKGAY	acetylation	[1, 2, 4]
393	AGAKTEAKGAYPGWQ	acetylation	[1]
421	TYQRLFNKTPNIQII	acetylation	[1]
438	GLECGLFKKPYPEMD	acetylation	[1, 2]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [3] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [4] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 

Functional Description

 Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also shows cysteinylglycinase activity, which is sufficient for E.coli to utilize cysteinylglycine as a cysteine source. 

Sequence Annotation

 ACT_SITE 78 78 By similarity.
 ACT_SITE 145 145 Proton acceptor (By similarity).
 METAL 76 76 Zinc 2 (By similarity).
 METAL 115 115 Zinc 1 (By similarity).
 METAL 115 115 Zinc 2 (By similarity).
 METAL 146 146 Zinc 1 (By similarity).
 METAL 169 169 Zinc 2 (By similarity).
 METAL 457 457 Zinc 1 (By similarity).
 MOD_RES 296 296 N6-acetyllysine.  

Keyword

 Acetylation; Cobalt; Complete proteome; Dipeptidase; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 485 AA 

Protein Sequence

Gene Ontology

 GO:0070573; F:metallodipeptidase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0043171; P:peptide catabolic process; IGI:EcoliWiki.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 

Interpro

 IPR002933; Peptidase_M20.
 IPR011650; Peptidase_M20_dimer.
 IPR001160; Peptidase_M20C. 

Pfam

 PF07687; M20_dimer
 PF01546; Peptidase_M20 

SMART

  

PROSITE

  

PRINTS

 PR00934; XHISDIPTASE.