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Protein

Peptidyl-dipeptidase dcp

Gene

dcp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides.

Catalytic activityi

Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyze bonds in which P1' is Pro, or both P1 and P1' are Gly.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Enzyme regulationi

It is stimulated by manganese, magnesium, cobalt and calcium ions and is inhibited by zinc, copper and nickel.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi470 – 4701Zinc; catalyticPROSITE-ProRule annotation
Active sitei471 – 4711PROSITE-ProRule annotation
Metal bindingi474 – 4741Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi477 – 4771Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  • carboxypeptidase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: GO_Central

GO - Biological processi

  • peptide metabolic process Source: GO_Central
  • proteolysis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10212-MONOMER.
ECOL316407:JW1531-MONOMER.
MetaCyc:EG10212-MONOMER.
RETL1328306-WGS:GSTH-4004-MONOMER.
BRENDAi3.4.15.5. 2026.

Protein family/group databases

MEROPSiM03.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-dipeptidase dcp (EC:3.4.15.5)
Alternative name(s):
Dipeptidyl carboxypeptidase
Gene namesi
Name:dcp
Ordered Locus Names:b1538, JW1531
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10212. dcp.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: EcoCyc
  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3259514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 681680Peptidyl-dipeptidase dcpPRO_0000078157Add
BLAST

Proteomic databases

EPDiP24171.
PaxDbiP24171.
PRIDEiP24171.

Interactioni

Protein-protein interaction databases

BioGridi4261739. 15 interactions.
IntActiP24171. 4 interactions.
STRINGi511145.b1538.

Chemistry

BindingDBiP24171.

Structurei

Secondary structure

1
681
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Helixi14 – 163Combined sources
Turni20 – 223Combined sources
Helixi25 – 273Combined sources
Helixi28 – 4619Combined sources
Beta strandi49 – 524Combined sources
Turni55 – 584Combined sources
Helixi59 – 646Combined sources
Helixi67 – 8216Combined sources
Helixi86 – 10722Combined sources
Helixi110 – 12112Combined sources
Turni122 – 1254Combined sources
Helixi130 – 14617Combined sources
Turni147 – 1493Combined sources
Helixi152 – 18130Combined sources
Beta strandi184 – 1885Combined sources
Helixi190 – 1934Combined sources
Helixi198 – 21013Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi223 – 2264Combined sources
Helixi228 – 2314Combined sources
Helixi236 – 24712Combined sources
Turni248 – 2503Combined sources
Beta strandi252 – 2543Combined sources
Helixi259 – 27517Combined sources
Helixi281 – 2866Combined sources
Helixi294 – 32532Combined sources
Helixi334 – 3363Combined sources
Helixi337 – 34913Combined sources
Helixi353 – 3553Combined sources
Helixi357 – 3593Combined sources
Helixi362 – 3687Combined sources
Helixi370 – 3789Combined sources
Beta strandi381 – 3888Combined sources
Beta strandi396 – 4016Combined sources
Beta strandi407 – 41610Combined sources
Beta strandi426 – 4316Combined sources
Turni435 – 4384Combined sources
Beta strandi442 – 4498Combined sources
Helixi462 – 47918Combined sources
Helixi486 – 4883Combined sources
Helixi495 – 50713Combined sources
Helixi508 – 5103Combined sources
Helixi512 – 5187Combined sources
Turni522 – 5243Combined sources
Helixi530 – 5389Combined sources
Turni539 – 5435Combined sources
Helixi544 – 56118Combined sources
Helixi566 – 5683Combined sources
Helixi573 – 58311Combined sources
Helixi597 – 5993Combined sources
Helixi601 – 6044Combined sources
Turni609 – 6124Combined sources
Helixi613 – 63119Combined sources
Helixi637 – 64610Combined sources
Turni647 – 6526Combined sources
Helixi656 – 6649Combined sources
Helixi671 – 6766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y79X-ray2.0012-681[»]
ProteinModelPortaliP24171.
SMRiP24171. Positions 2-681.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24171.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Phylogenomic databases

eggNOGiENOG4105DGW. Bacteria.
COG0339. LUCA.
HOGENOMiHOG000245984.
InParanoidiP24171.
KOiK01284.
OMAiGTSFSHH.
PhylomeDBiP24171.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTMNPFLVQ STLPYLAPHF DQIANHHYRP AFDEGMQQKR AEIAAIALNP
60 70 80 90 100
QMPDFNNTIL ALEQSGELLT RVTSVFFAMT AAHTNDELQR LDEQFSAELA
110 120 130 140 150
ELANDIYLNG ELFARVDAVW QRRESLGLDS ESIRLVEVIH QRFVLAGAKL
160 170 180 190 200
AQADKAKLKV LNTEAATLTS QFNQRLLAAN KSGGLVVNDI AQLAGMSEQE
210 220 230 240 250
IALAAEAARE KGLDNKWLIP LLNTTQQPAL AEMRDRATRE KLFIAGWTRA
260 270 280 290 300
EKNDANDTRA IIQRLVEIRA QQATLLGFPH YAAWKIADQM AKTPEAALNF
310 320 330 340 350
MREIVPAARQ RASDELASIQ AVIDKQQGGF SAQPWDWAFY AEQVRREKFD
360 370 380 390 400
LDEAQLKPYF ELNTVLNEGV FWTANQLFGI KFVERFDIPV YHPDVRVWEI
410 420 430 440 450
FDHNGVGLAL FYGDFFARDS KSGGAWMGNF VEQSTLNKTH PVIYNVCNYQ
460 470 480 490 500
KPAAGEPALL LWDDVITLFH EFGHTLHGLF ARQRYATLSG TNTPRDFVEF
510 520 530 540 550
PSQINEHWAT HPQVFARYAR HYQSGAAMPD ELQQKMRNAS LFNKGYEMSE
560 570 580 590 600
LLSAALLDMR WHCLEENEAM QDVDDFELRA LVAENMDLPA IPPRYRSSYF
610 620 630 640 650
AHIFGGGYAA GYYAYLWTQM LADDGYQWFV EQGGLTRENG LRFREAILSR
660 670 680
GNSEDLERLY RQWRGKAPKI MPMLQHRGLN I
Length:681
Mass (Da):77,516
Last modified:January 23, 2007 - v4
Checksum:i659C5FD659566391
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1402IH → LL in CAA41014 (PubMed:8226676).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57947 Genomic DNA. Translation: CAA41014.1.
U00096 Genomic DNA. Translation: AAC74611.1.
AP009048 Genomic DNA. Translation: BAA15228.1.
PIRiE64908.
RefSeqiNP_416056.1. NC_000913.3.
WP_000210373.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74611; AAC74611; b1538.
BAA15228; BAA15228; BAA15228.
GeneIDi946084.
KEGGiecj:JW1531.
eco:b1538.
PATRICi32118376. VBIEscCol129921_1608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57947 Genomic DNA. Translation: CAA41014.1.
U00096 Genomic DNA. Translation: AAC74611.1.
AP009048 Genomic DNA. Translation: BAA15228.1.
PIRiE64908.
RefSeqiNP_416056.1. NC_000913.3.
WP_000210373.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y79X-ray2.0012-681[»]
ProteinModelPortaliP24171.
SMRiP24171. Positions 2-681.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261739. 15 interactions.
IntActiP24171. 4 interactions.
STRINGi511145.b1538.

Chemistry

BindingDBiP24171.
ChEMBLiCHEMBL3259514.

Protein family/group databases

MEROPSiM03.005.

Proteomic databases

EPDiP24171.
PaxDbiP24171.
PRIDEiP24171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74611; AAC74611; b1538.
BAA15228; BAA15228; BAA15228.
GeneIDi946084.
KEGGiecj:JW1531.
eco:b1538.
PATRICi32118376. VBIEscCol129921_1608.

Organism-specific databases

EchoBASEiEB0208.
EcoGeneiEG10212. dcp.

Phylogenomic databases

eggNOGiENOG4105DGW. Bacteria.
COG0339. LUCA.
HOGENOMiHOG000245984.
InParanoidiP24171.
KOiK01284.
OMAiGTSFSHH.
PhylomeDBiP24171.

Enzyme and pathway databases

BioCyciEcoCyc:EG10212-MONOMER.
ECOL316407:JW1531-MONOMER.
MetaCyc:EG10212-MONOMER.
RETL1328306-WGS:GSTH-4004-MONOMER.
BRENDAi3.4.15.5. 2026.

Miscellaneous databases

EvolutionaryTraceiP24171.
PROiP24171.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDCP_ECOLI
AccessioniPrimary (citable) accession number: P24171
Secondary accession number(s): P78305
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.