ID   ACLY_ACHLY              Reviewed;         119 AA.
AC   P81730;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Achromolysin;
DE            EC=3.4.24.-;
DE   Flags: Fragments;
OS   Achromobacter lyticus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=224;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=M497-1;
RA   Li S.L.;
RT   "Achromolysin, a metalloproteinase from Achromobacter lyticus.";
RL   Submitted (MAR-1999) to UniProtKB.
CC   -!- FUNCTION: Has staphylolytic activity.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC       Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   AlphaFoldDB; P81730; -.
DR   SMR; P81730; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Metalloprotease; Protease;
KW   Secreted; Zinc.
FT   CHAIN           1..>119
FT                   /note="Achromolysin"
FT                   /id="PRO_0000078174"
FT   NON_CONS        42..43
FT                   /evidence="ECO:0000305"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000305"
FT   NON_CONS        80..81
FT                   /evidence="ECO:0000305"
FT   NON_TER         119
SQ   SEQUENCE   119 AA;  12555 MW;  738F492DDB14F18D CRC64;
     AQVGTGPGGN QKIGQYEYGS GGRPFLDVAQ SGSTYTFNTT NLTVNLNHGT SGSTAYSYTG
     PRNTINGAYS PLNDAHYFGR DYWTPSTNFN QGGQGVRQAA ADLGYSTADV IDAFRQVGV