DCP_SALTY
ID DCP_SALTY Reviewed; 680 AA.
AC P27236;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Dipeptidyl carboxypeptidase;
DE EC=3.4.15.5;
DE AltName: Full=Peptidyl-dipeptidase Dcp;
GN Name=dcp; OrderedLocusNames=STM1512;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=1537804; DOI=10.1128/jb.174.5.1626-1630.1992;
RA Miller C.G., Hamilton S.;
RT "Cloning and nucleotide sequence of the Salmonella typhimurium dcp gene
RT encoding dipeptidyl carboxypeptidase.";
RL J. Bacteriol. 174:1626-1630(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Removes dipeptides from the C-termini of N-blocked
CC tripeptides, tetrapeptides and larger peptides.
CC {ECO:0000250|UniProtKB:P24171}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P24171}.
CC -!- DISRUPTION PHENOTYPE: Unable to grow on N-acetyl-Ala-Ala-Ala as a
CC nitrogen source. {ECO:0000269|PubMed:1537804}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M84575; AAA27055.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20431.1; -; Genomic_DNA.
DR PIR; A42297; A42297.
DR RefSeq; NP_460472.1; NC_003197.2.
DR RefSeq; WP_000106265.1; NC_003197.2.
DR AlphaFoldDB; P27236; -.
DR SMR; P27236; -.
DR STRING; 99287.STM1512; -.
DR MEROPS; M03.005; -.
DR PaxDb; P27236; -.
DR EnsemblBacteria; AAL20431; AAL20431; STM1512.
DR GeneID; 1253030; -.
DR KEGG; stm:STM1512; -.
DR PATRIC; fig|99287.12.peg.1599; -.
DR HOGENOM; CLU_001805_4_0_6; -.
DR OMA; YQCMPLD; -.
DR PhylomeDB; P27236; -.
DR BioCyc; SENT99287:STM1512-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 Carboxypeptidase; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..680
FT /note="Dipeptidyl carboxypeptidase"
FT /id="PRO_0000078158"
FT ACT_SITE 470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 680 AA; 77261 MW; DDFD89B47B660B45 CRC64;
MSTNPLLDQS MLPYQAPRFD RIKDCHYRPA FDEGVRQKRV EIEAIVNHPA APDFTNTLLA
LEQSGALLSR VTSVFFAMTA AHTNDELQRL DEAFSAELAA LSNDIYLNSA LFARVDAVWQ
QRHSLGLDDE SLRLVDVIHQ RFVLAGAQLA EEDKARLKVL NTESATLMSQ FNQRLLAASK
AGGLAVDDAH CLAGLSPEEM TVAAEAAREK GLEERWFIPL LNTTQQPALA TLRDRQTREN
LFAASWTRAE KGDAHDTRAI VQRLVEIRRC QAKLLGFPNY AAWKMADQMA KTPQAALSFM
RGIVPPARQR VLNEQAEIQN VIDGEQGGYT VQAWDWMFYA EQVRREKYAL DEAQLKPYFA
LNTVLQEGVF WTANQLFGIT FVERFDIPVY HPDVRVWEIF DSDGVGMALF YGDFFARDSK
SGGAWMGNFV EQSTLNETRP VIYNVCNYQK PVDGQPALLL WDDVITLFHE FGHTLHGLFA
VQRYATLSGT NTPRDFVEFP SQINEHWASH PRVFERYARH VDSGEKMPAD LQERMRKASL
FNKGYDMTEL LGAALLDMRW HMLEESVAEQ SVAEFEQQAL AAEHLDLPAV PPRYRSSYFA
HIFGGGYAAG YYAYLWTQML ADDGYQWFVE QGGLTRENGQ RFRDAILARG NSTDLETLYS
AWRGHEPHID PMLQYRGLDR
