ID   APE_CAPGI               Reviewed;          10 AA.
AC   P80474;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Aminopeptidase;
DE            EC=3.4.11.-;
DE   Flags: Fragment;
OS   Capnocytophaga gingivalis.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=553178;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 33624 / DSM 3290 / CIP 102945 / JCM 12953 / NCTC 12372 / 27;
RX   PubMed=8574402; DOI=10.1099/13500872-141-12-3087;
RA   Spratt D.A., Greenman J., Schaffer A.G.;
RT   "Capnocytophaga gingivalis aminopeptidase: a potential virulence factor.";
RL   Microbiology 141:3087-3093(1995).
CC   -!- FUNCTION: Aminopeptidase which hydrolyzes substrates with free N-
CC       terminal amino acid residues but not N-terminal blocked ones. May be
CC       important in the nutrition and pathogenesis of the organism in the
CC       human oral cavity.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5.;
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DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Calcium; Direct protein sequencing; Hydrolase; Magnesium;
KW   Protease.
FT   CHAIN           <1..>10
FT                   /note="Aminopeptidase"
FT                   /id="PRO_0000064631"
FT   NON_TER         1
FT   NON_TER         10
SQ   SEQUENCE   10 AA;  1307 MW;  00C0A6DB43772694 CRC64;
     DVNMLWYVXR