DCP_ECOLI
ID DCP_ECOLI Reviewed; 681 AA.
AC P24171; P78305;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Dipeptidyl carboxypeptidase {ECO:0000303|PubMed:8226676};
DE EC=3.4.15.5;
DE AltName: Full=Peptidyl-dipeptidase Dcp;
GN Name=dcp {ECO:0000303|PubMed:8226676}; OrderedLocusNames=b1538, JW1531;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10, FUNCTION,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=8226676; DOI=10.1128/jb.175.22.7290-7300.1993;
RA Henrich B., Becker S., Schroeder U., Plapp R.;
RT "dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and
RT characterization of the gene product.";
RL J. Bacteriol. 175:7290-7300(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Removes dipeptides from the C-termini of N-blocked
CC tripeptides, tetrapeptides and larger peptides.
CC {ECO:0000269|PubMed:8226676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of unblocked, C-terminal dipeptides from
CC oligopeptides, with broad specificity. Does not hydrolyze bonds in
CC which P1' is Pro, or both P1 and P1' are Gly.; EC=3.4.15.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Stimulated by Mn(2+), Mg(2+), Co(2+) and Ca(2+),
CC inhibited by Cu(2+), Ni(2+), Zn(2+), chymostatin and 1,10-
CC phenanthroline. {ECO:0000269|PubMed:8226676}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8226676}.
CC -!- DISRUPTION PHENOTYPE: Unable to grow on N-benzoyl-Gly-His-Leu as a
CC nitrogen source. {ECO:0000269|PubMed:8226676}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR EMBL; X57947; CAA41014.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74611.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15228.1; -; Genomic_DNA.
DR PIR; E64908; E64908.
DR RefSeq; NP_416056.1; NC_000913.3.
DR RefSeq; WP_000210373.1; NZ_SSZK01000001.1.
DR PDB; 1Y79; X-ray; 2.00 A; 1=2-681.
DR PDBsum; 1Y79; -.
DR AlphaFoldDB; P24171; -.
DR SMR; P24171; -.
DR BioGRID; 4261739; 52.
DR IntAct; P24171; 4.
DR STRING; 511145.b1538; -.
DR BindingDB; P24171; -.
DR ChEMBL; CHEMBL3259514; -.
DR MEROPS; M03.005; -.
DR jPOST; P24171; -.
DR PaxDb; P24171; -.
DR PRIDE; P24171; -.
DR EnsemblBacteria; AAC74611; AAC74611; b1538.
DR EnsemblBacteria; BAA15228; BAA15228; BAA15228.
DR GeneID; 946084; -.
DR KEGG; ecj:JW1531; -.
DR KEGG; eco:b1538; -.
DR PATRIC; fig|1411691.4.peg.727; -.
DR EchoBASE; EB0208; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_6; -.
DR InParanoid; P24171; -.
DR OMA; YQCMPLD; -.
DR PhylomeDB; P24171; -.
DR BioCyc; EcoCyc:EG10212-MON; -.
DR BioCyc; MetaCyc:EG10212-MON; -.
DR BRENDA; 3.4.15.5; 2026.
DR EvolutionaryTrace; P24171; -.
DR PRO; PR:P24171; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IMP:EcoCyc.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; PTHR43660; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carboxypeptidase; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8226676"
FT CHAIN 2..681
FT /note="Dipeptidyl carboxypeptidase"
FT /id="PRO_0000078157"
FT ACT_SITE 471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CONFLICT 139..140
FT /note="IH -> LL (in Ref. 1; CAA41014)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 28..46
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 86..107
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 152..181
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 294..325
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 337..349
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 362..368
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 407..416
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:1Y79"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 462..479
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 495..507
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 512..518
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 530..538
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 539..543
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 544..561
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 573..583
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 609..612
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 613..631
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 637..646
FT /evidence="ECO:0007829|PDB:1Y79"
FT TURN 647..652
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 656..664
FT /evidence="ECO:0007829|PDB:1Y79"
FT HELIX 671..676
FT /evidence="ECO:0007829|PDB:1Y79"
SQ SEQUENCE 681 AA; 77516 MW; 659C5FD659566391 CRC64;
MTTMNPFLVQ STLPYLAPHF DQIANHHYRP AFDEGMQQKR AEIAAIALNP QMPDFNNTIL
ALEQSGELLT RVTSVFFAMT AAHTNDELQR LDEQFSAELA ELANDIYLNG ELFARVDAVW
QRRESLGLDS ESIRLVEVIH QRFVLAGAKL AQADKAKLKV LNTEAATLTS QFNQRLLAAN
KSGGLVVNDI AQLAGMSEQE IALAAEAARE KGLDNKWLIP LLNTTQQPAL AEMRDRATRE
KLFIAGWTRA EKNDANDTRA IIQRLVEIRA QQATLLGFPH YAAWKIADQM AKTPEAALNF
MREIVPAARQ RASDELASIQ AVIDKQQGGF SAQPWDWAFY AEQVRREKFD LDEAQLKPYF
ELNTVLNEGV FWTANQLFGI KFVERFDIPV YHPDVRVWEI FDHNGVGLAL FYGDFFARDS
KSGGAWMGNF VEQSTLNKTH PVIYNVCNYQ KPAAGEPALL LWDDVITLFH EFGHTLHGLF
ARQRYATLSG TNTPRDFVEF PSQINEHWAT HPQVFARYAR HYQSGAAMPD ELQQKMRNAS
LFNKGYEMSE LLSAALLDMR WHCLEENEAM QDVDDFELRA LVAENMDLPA IPPRYRSSYF
AHIFGGGYAA GYYAYLWTQM LADDGYQWFV EQGGLTRENG LRFREAILSR GNSEDLERLY
RQWRGKAPKI MPMLQHRGLN I
