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P15288 (PEPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 485484Cytosol non-specific dipeptidase
PRO_0000185354

Sites

Active site781 By similarity
Active site1451Proton acceptor By similarity
Metal binding761Zinc 2 By similarity
Metal binding1151Zinc 1 By similarity
Metal binding1151Zinc 2 By similarity
Metal binding1461Zinc 1 By similarity
Metal binding1691Zinc 2 By similarity
Metal binding4571Zinc 1 By similarity

Amino acid modifications

Modified residue2961N6-acetyllysine Ref.10

Sequences

Sequence LengthMass (Da)Tools
P15288 [UniParc].

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

FASTA48552,915
        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' 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] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-296, IDENTIFICATION BY 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.
PIRJU0300.
RefSeqNP_414772.1. NC_000913.3.
YP_488532.1. NC_007779.1.

3D structure databases

ProteinModelPortalP15288.
SMRP15288. Positions 2-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10456N.
IntActP15288. 69 interactions.
MINTMINT-1252343.
STRING511145.b0237.

Protein family/group databases

MEROPSM20.007.

2D gel databases

SWISS-2DPAGEP15288.

Proteomic databases

PaxDbP15288.
PRIDEP15288.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73341; AAC73341; b0237.
BAA77906; BAA77906; BAA77906.
GeneID12930771.
945013.
KEGGecj:Y75_p0228.
eco:b0237.
PATRIC32115589. VBIEscCol129921_0239.

Organism-specific databases

EchoBASEEB0689.
EcoGeneEG10695. pepD.

Phylogenomic databases

eggNOGCOG2195.
HOGENOMHOG000282306.
KOK01270.
OMAKGGYPGW.
OrthoDBEOG6BCSRT.
PhylomeDBP15288.
ProtClustDBPRK15026.

Enzyme and pathway databases

BioCycEcoCyc:EG10695-MONOMER.
ECOL316407:JW0227-MONOMER.
MetaCyc:EG10695-MONOMER.

Gene expression databases

GenevestigatorP15288.

Family and domain databases

InterProIPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
IPR001160. Peptidase_M20C.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF016599. Xaa-His_dipept. 1 hit.
PRINTSPR00934. XHISDIPTASE.
TIGRFAMsTIGR01893. aa-his-dipept. 1 hit.
ProtoNetSearch...

Other

PROP15288.

Entry information

Entry namePEPD_ECOLI
AccessionPrimary (citable) accession number: P15288
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

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