ID   AMP_ACETH               Reviewed;         330 AA.
AC   P55742;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Putative aminopeptidase;
DE            EC=3.4.11.-;
GN   Name=celM;
OS   Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS   thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=1515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gerngross U.T., Demain A.L., Kobayashi T.T.;
RT   "Nucleotide sequence of a gene celM encoding a new endoglucanase (CelM) of
RT   Clostridium thermocellum and purification of the enzyme.";
RL   Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
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DR   EMBL; L13461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P55742; -.
DR   SMR; P55742; -.
DR   MEROPS; M42.010; -.
DR   PRIDE; P55742; -.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.40; -; 1.
DR   InterPro; IPR008007; Peptidase_M42.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF05343; Peptidase_M42; 1.
DR   PIRSF; PIRSF001123; PepA_GA; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease.
FT   CHAIN           1..330
FT                   /note="Putative aminopeptidase"
FT                   /id="PRO_0000071654"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   330 AA;  35814 MW;  C01E765E18AEA57C CRC64;
     MEEEDMFDLL KKFTGIVGVS GNEEEIREAI IEEIKECVDE IKVDTLGNLI AVKKGKGKKI
     MVAAHMDEIG VMVTYIDDKG FLRFSAVGGV SRYDCIGQRV KFKNGVVGAV YYEEKLEDMK
     NLQLSKMYID IGARSREEAL KMVNIGDVAC FVGDAVLQGD TVISKALDNR SGCAVVVKAI
     KELKKTDNEI YFVFTVQEEV GLRGAKTAAF SIKPDIAIAV DVTMTGDTPE SHPMEVKCGG
     GPAIKVKDRS VICHPEVRKL LEESAKRNNI PYQLEILEAG GSDPGSIHLT AGGIPSGAIS
     IPVRYVHSPV ETASMSDINN AVKLLVEAIC