ID   PEPDA_LACHE             Reviewed;         474 AA.
AC   Q48558; P71434;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Dipeptidase A;
DE            EC=3.4.13.19;
GN   Name=pepDA; Synonyms=pepD;
OS   Lactobacillus helveticus (Lactobacillus suntoryeus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNRZ 32;
RX   PubMed=8550503; DOI=10.1128/jb.178.3.701-704.1996;
RA   Dudley E.G., Husgen A.C., He W., Steele J.L.;
RT   "Sequencing, distribution, and inactivation of the dipeptidase A gene
RT   (pepDA) from Lactobacillus helveticus CNRZ32.";
RL   J. Bacteriol. 178:701-704(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=53/7;
RX   PubMed=8766699; DOI=10.1007/s002530050741;
RA   Vesanto E., Peltoniemi K., Purtsi T., Steele J.L., Palva A.;
RT   "Molecular characterization, over-expression and purification of a novel
RT   dipeptidase from Lactobacillus helveticus.";
RL   Appl. Microbiol. Biotechnol. 45:638-645(1996).
CC   -!- FUNCTION: Hydrolyzes a wide range of dipeptides but unable to hydrolyze
CC       dipeptides containing proline. Highest activity against Met-Ala.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC         Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:77460; EC=3.4.13.19;
CC   -!- ACTIVITY REGULATION: Inhibited by Zn(2+), Cu(2+), Ca(2+) and Cd(2+).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0.;
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.;
CC   -!- SUBUNIT: Homooctamer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase C69 family. {ECO:0000305}.
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DR   EMBL; U34257; AAC43971.1; -; Genomic_DNA.
DR   EMBL; Z38063; CAA86210.1; -; Genomic_DNA.
DR   PIR; JC6042; JC6042.
DR   RefSeq; WP_003630880.1; NZ_SCLQ01000118.1.
DR   RefSeq; WP_012211344.1; NZ_WCHF01000003.1.
DR   AlphaFoldDB; Q48558; -.
DR   SMR; Q48558; -.
DR   STRING; 326425.lhe_1838; -.
DR   MEROPS; C69.001; -.
DR   PRIDE; Q48558; -.
DR   eggNOG; COG4690; Bacteria.
DR   GO; GO:0070004; F:cysteine-type exopeptidase activity; IEA:InterPro.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR005322; Peptidase_C69.
DR   PANTHER; PTHR12994; PTHR12994; 1.
DR   Pfam; PF03577; Peptidase_C69; 1.
PE   1: Evidence at protein level;
KW   Dipeptidase; Hydrolase; Protease.
FT   CHAIN           1..474
FT                   /note="Dipeptidase A"
FT                   /id="PRO_0000220381"
FT   ACT_SITE        6
FT                   /evidence="ECO:0000255"
FT   CONFLICT        211
FT                   /note="T -> A (in Ref. 2; CAA86210)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   474 AA;  53513 MW;  3BFA79983D3ECEF2 CRC64;
     MKQTECTTIL VGKKASIDGS TMIARSEDGG RVIIPEGFKV VNPEDQPKHY TSVISKQKID
     DEDLAETPLR YTSAPDVSGK NGIWGAAGIN ADNVAMTATE TITTNSRIQG VDPILDPSEG
     GLGEEDFVTL TLPYLHSAFD GVKRVGYLVE KYGTYEMNGM AFSDKDNIWY LETIGGHHWI
     ARRIPDDAYV IAPNRLNIDT FDFDDSENFA TASDLKDLID EYHLNPDREG YNMRHIFGSS
     TIKDAHYNNP RAWYIHNYFD PDFGGTPADQ DQPFICRANR LISIEDIKWA ESSHYQDTPY
     DAYGDQGTPE QKKTFRPIGI NRNFETHILQ IRNDVPAEIA GVQWLAFGPN TFNSMLPFYT
     NVTTTPEAWQ TTPKFNLNKI FWLNKLTAQL GDTNYRVYGE LEDAFEQKSL AQCHKIQHET
     DKEVKNLSGK ELQDKLIAAN QKMSDTVYNN TVELLGQMVD EGHGLMTLKY DLLD