ID   PEPT_FUSNP              Reviewed;          20 AA.
AC   P81207;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Peptidase T;
DE            EC=3.4.11.4;
DE   AltName: Full=Aminotripeptidase;
DE            Short=Tripeptidase;
DE   AltName: Full=Tripeptide aminopeptidase;
DE   Flags: Fragment;
GN   Name=pepT;
OS   Fusobacterium nucleatum subsp. polymorphum.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=76857;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 10953 / DSM 20482 / CCUG 9126 / JCM 12990 / NCTC 10562 / 555A;
RX   PubMed=9695913; DOI=10.1099/00221287-144-7-1807;
RA   Rogers A.H., Gunadi A., Gully N.J., Zilm P.S.;
RT   "An aminopeptidase nutritionally important to Fusobacterium nucleatum.";
RL   Microbiology 144:1807-1813(1998).
CC   -!- FUNCTION: Cleaves a wide range of dipeptides and tripeptides, but does
CC       not display activity against larger peptides. May have a role in the
CC       survival of F.nucleatum in the subgingival environment of the mouth.
CC       {ECO:0000269|PubMed:9695913}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of the N-terminal residue from a tripeptide.;
CC         EC=3.4.11.4;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:9695913};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:9695913};
CC       Note=Binds 2 Zn(2+) or Co(2+) ions per subunit.
CC       {ECO:0000269|PubMed:9695913};
CC   -!- ACTIVITY REGULATION: Inhibited by the chelating agents EDTA and 1,10-
CC       phenanthroline, by bestatin and amastatin, p-hydroxymercuribenzoate and
CC       some divalent cations at high concentration.
CC       {ECO:0000269|PubMed:9695913}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.66 mM for dipeptide Leu-Ala {ECO:0000269|PubMed:9695913};
CC         KM=4.0 mM for tripeptide Leu-Gly-Gly {ECO:0000269|PubMed:9695913};
CC         Vmax=0.12 umol/min/mg enzyme with Leu-Ala as substrate
CC         {ECO:0000269|PubMed:9695913};
CC         Vmax=0.09 umol/min/mg enzyme with Leu-Gly-Gly as substrate
CC         {ECO:0000269|PubMed:9695913};
CC       pH dependence:
CC         Optimum pH is 7.5-8. {ECO:0000269|PubMed:9695913};
CC   -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000269|PubMed:9695913}.
CC       Note=Cell envelope associated.
CC   -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000305}.
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DR   GO; GO:0031975; C:envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cobalt; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..>20
FT                   /note="Peptidase T"
FT                   /id="PRO_0000185296"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2587 MW;  97095B948262C71B CRC64;
     MDXKXYVDLK ERFLRYVKFN