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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)DescriptionActionsGraphical viewLength
Metal bindingi470Zinc; catalyticPROSITE-ProRule annotation1
Active sitei471PROSITE-ProRule annotation1
Metal bindingi474Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi477Zinc; catalyticPROSITE-ProRule annotation1

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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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 databases

ChEMBLiCHEMBL3259514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000781572 – 681Peptidyl-dipeptidase dcpAdd BLAST680

Proteomic databases

EPDiP24171.
PaxDbiP24171.
PRIDEiP24171.

Interactioni

Protein-protein interaction databases

BioGridi4261739. 15 interactors.
IntActiP24171. 4 interactors.
STRINGi511145.b1538.

Chemistry databases

BindingDBiP24171.

Structurei

Secondary structure

1681
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Helixi14 – 16Combined sources3
Turni20 – 22Combined sources3
Helixi25 – 27Combined sources3
Helixi28 – 46Combined sources19
Beta strandi49 – 52Combined sources4
Turni55 – 58Combined sources4
Helixi59 – 64Combined sources6
Helixi67 – 82Combined sources16
Helixi86 – 107Combined sources22
Helixi110 – 121Combined sources12
Turni122 – 125Combined sources4
Helixi130 – 146Combined sources17
Turni147 – 149Combined sources3
Helixi152 – 181Combined sources30
Beta strandi184 – 188Combined sources5
Helixi190 – 193Combined sources4
Helixi198 – 210Combined sources13
Beta strandi217 – 219Combined sources3
Beta strandi223 – 226Combined sources4
Helixi228 – 231Combined sources4
Helixi236 – 247Combined sources12
Turni248 – 250Combined sources3
Beta strandi252 – 254Combined sources3
Helixi259 – 275Combined sources17
Helixi281 – 286Combined sources6
Helixi294 – 325Combined sources32
Helixi334 – 336Combined sources3
Helixi337 – 349Combined sources13
Helixi353 – 355Combined sources3
Helixi357 – 359Combined sources3
Helixi362 – 368Combined sources7
Helixi370 – 378Combined sources9
Beta strandi381 – 388Combined sources8
Beta strandi396 – 401Combined sources6
Beta strandi407 – 416Combined sources10
Beta strandi426 – 431Combined sources6
Turni435 – 438Combined sources4
Beta strandi442 – 449Combined sources8
Helixi462 – 479Combined sources18
Helixi486 – 488Combined sources3
Helixi495 – 507Combined sources13
Helixi508 – 510Combined sources3
Helixi512 – 518Combined sources7
Turni522 – 524Combined sources3
Helixi530 – 538Combined sources9
Turni539 – 543Combined sources5
Helixi544 – 561Combined sources18
Helixi566 – 568Combined sources3
Helixi573 – 583Combined sources11
Helixi597 – 599Combined sources3
Helixi601 – 604Combined sources4
Turni609 – 612Combined sources4
Helixi613 – 631Combined sources19
Helixi637 – 646Combined sources10
Turni647 – 652Combined sources6
Helixi656 – 664Combined sources9
Helixi671 – 676Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y79X-ray2.0012-681[»]
ProteinModelPortaliP24171.
SMRiP24171.
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)DescriptionActionsGraphical viewLength
Sequence conflicti139 – 140IH → LL in CAA41014 (PubMed:8226676).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y79X-ray2.0012-681[»]
ProteinModelPortaliP24171.
SMRiP24171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261739. 15 interactors.
IntActiP24171. 4 interactors.
STRINGi511145.b1538.

Chemistry databases

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.
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: November 2, 2016
This is version 144 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.