Cytosol non-specific dipeptidase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P15288 (PEPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytosol non-specific dipeptidase
EC=3.4.13.18

Alternative name(s):
Aminoacyl-histidine dipeptidase
Beta-alanyl-histidine dipeptidase
Carnosinase
Cysteinylglycinase
Peptidase D
Xaa-His dipeptidase
Short name=X-His dipeptidase

Gene names

Name:	pepD
Synonyms:	pepH
Ordered Locus Names:	b0237, JW0227

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8 Ref.9
Catalytic activity	Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids. Ref.7 Ref.8
Cofactor	Binds 2 zinc ions per subunit. Can also use cobalt. Ref.8
Enzyme regulation	Inhibited by metal chelators. Ref.8
Sequence similarities	Belongs to the peptidase M20C family.
Biophysicochemical properties	pH dependence: Optimum pH is 9. Ref.8 Temperature dependence: Optimum temperature is 37 degrees Celsius.

Ontologies

Keywords
Ligand	Cobalt Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	peptide catabolic process Inferred from genetic interaction Ref.7. Source: EcoliWiki proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
hscB	P0A6L9	1	EBI-542419,EBI-561519
yggX	P0A8P3	1	EBI-542419,EBI-1123057

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 485

484

Cytosol non-specific dipeptidase

PRO_0000185354

Sites

Active site

By similarity

Active site

145

Proton acceptor By similarity

Metal binding

Zinc 2 By similarity

Metal binding

115

Zinc 1 By similarity

Metal binding

115

Zinc 2 By similarity

Metal binding

146

Zinc 1 By similarity

Metal binding

169

Zinc 2 By similarity

Metal binding

457

Zinc 1 By similarity

Amino acid modifications

Modified residue

296

N6-acetyllysine Ref.10

Sequences

Sequence

Length

Mass (Da)

Tools

P15288 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CD870032876460E1
Show »

FASTA

485

52,915

        10         20         30         40         50         60 
MSELSQLSPQ PLWDIFAKIC SIPHPSYHEE QLAEYIVGWA KEKGFHVERD QVGNILIRKP 

        70         80         90        100        110        120 
ATAGMENRKP VVLQAHLDMV PQKNNDTVHD FTKDPIQPYI DGEWVKARGT TLGADNGIGM 

       130        140        150        160        170        180 
ASALAVLADE NVVHGPLEVL LTMTEEAGMD GAFGLQGNWL QADILINTDS EEEGEIYMGC 

       190        200        210        220        230        240 
AGGIDFTSNL HLDREAVPAG FETFKLTLKG LKGGHSGGEI HVGLGNANKL LVRFLAGHAE 

       250        260        270        280        290        300 
ELDLRLIDFN GGTLRNAIPR EAFATIAVAA DKVDVLKSLV NTYQEILKNE LAEKEKNLAL 

       310        320        330        340        350        360 
LLDSVANDKA ALIAKSRDTF IRLLNATPNG VIRNSDVAKG VVETSLNVGV VTMTDNNVEI 

       370        380        390        400        410        420 
HCLIRSLIDS GKDYVVSMLD SLGKLAGAKT EAKGAYPGWQ PDANSPVMHL VRETYQRLFN 

       430        440        450        460        470        480 
KTPNIQIIHA GLECGLFKKP YPEMDMVSIG PTITGPHSPD EQVHIESVGH YWTLLTELLK 


EIPAK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Peptidase D gene (pepD) of Escherichia coli K-12: nucleotide sequence, transcript mapping, and comparison with other peptidase genes." Henrich B., Monnerjahn U., Plapp R. J. Bacteriol. 172:4641-4651(1990) [PubMed: 1695895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Accurate mapping of the Escherichia coli pepD gene by sequence analysis of its 5' flanking region." Henrich B., Schroeder U., Frank R.W., Plapp R. Mol. Gen. Genet. 215:369-373(1989) [PubMed: 2651887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56, PROTEIN SEQUENCE OF 2-13. Strain: K12.
[7]	"Peptidase-deficient mutants of Escherichia coli." Miller C.G., Schwartz G. J. Bacteriol. 135:603-611(1978) [PubMed: 355237] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[8]	"Peptidase D of Escherichia coli K-12, a metallopeptidase of low substrate specificity." Schroeder U., Henrich B., Fink J., Plapp R. FEMS Microbiol. Lett. 123:153-159(1994) [PubMed: 7988883] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12." Suzuki H., Kamatani S., Kim E.-S., Kumagai H. J. Bacteriol. 183:1489-1490(2001) [PubMed: 11157967] [Abstract] Cited for: FUNCTION.
[10]	"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 C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-296, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M34034 Unassigned DNA. Translation: AAA16111.1. U70214 Genomic DNA. Translation: AAB08657.1. U00096 Genomic DNA. Translation: AAC73341.1. AP009048 Genomic DNA. Translation: BAA77906.1. X14790 Genomic DNA. Translation: CAA32892.1.
PIR	JU0300.
RefSeq	NP_414772.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P15288.
SMR	P15288. Positions 2-485.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10456N.
IntAct	P15288. 69 interactions.
MINT	MINT-1252343.
Protein family/group databases
MEROPS	M20.007.
2D gel databases
SWISS-2DPAGE	P15288.
2DBase-Ecoli	P15288.
Proteomic databases
PRIDE	P15288.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000001258; EBESCP00000001258; EBESCG00000001043. EBESCT00000001259; EBESCP00000001259; EBESCG00000001043. EBESCT00000001260; EBESCP00000001260; EBESCG00000001043. EBESCT00000015525; EBESCP00000014816; EBESCG00000014585.
GeneID	945013.
GenomeReviews	Gene locus JW0227 in contig AP009048_GR. Gene locus b0237 in contig U00096_GR.
KEGG	ecj:JW0227. eco:b0237.
PATRIC	32115589. VBIEscCol129921_0239.
Organism-specific databases
EchoBASE	EB0689.
EcoGene	EG10695. pepD.
Phylogenomic databases
eggNOG	COG2195.
GeneTree	EBGT00050000011557.
HOGENOM	HBG354460.
OMA	NACPNGV.
PhylomeDB	P15288.
ProtClustDB	PRK15026.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10695-MONOMER. MetaCyc:EG10695-MONOMER.
Gene expression databases
Genevestigator	P15288.
Family and domain databases
InterPro	IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. IPR001160. Peptidase_M20C. [Graphical view]
KO	K01270.
PANTHER	PTHR11014:SF2. Peptidase_M20C. 1 hit.
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF016599. Xaa-His_dipept. 1 hit.
PRINTS	PR00934. XHISDIPTASE.
TIGRFAMs	TIGR01893. Aa-his-dipept. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PEPD_ECOLI

Accession

Primary (citable) accession number: P15288

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents