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Database: UniProt
Entry: A0A1Y3WG54_9FIRM
LinkDB: A0A1Y3WG54_9FIRM
Original site: A0A1Y3WG54_9FIRM 
ID   A0A1Y3WG54_9FIRM        Unreviewed;       338 AA.
AC   A0A1Y3WG54;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Peptidase M42 family protein {ECO:0000313|EMBL:OUN72216.1};
GN   ORFNames=B5G11_00640 {ECO:0000313|EMBL:OUN72216.1};
OS   Drancourtella sp. An57.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Drancourtella.
OX   NCBI_TaxID=1965647 {ECO:0000313|EMBL:OUN72216.1, ECO:0000313|Proteomes:UP000196207};
RN   [1] {ECO:0000313|Proteomes:UP000196207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An57 {ECO:0000313|Proteomes:UP000196207};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000256|PIRSR:PIRSR001123-2};
CC   -!- SIMILARITY: Belongs to the peptidase M42 family.
CC       {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUN72216.1}.
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DR   EMBL; NFHY01000001; OUN72216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3WG54; -.
DR   Proteomes; UP000196207; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008007; Peptidase_M42.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR32481:SF9; ENDOGLUCANASE; 1.
DR   Pfam; PF05343; Peptidase_M42; 1.
DR   PIRSF; PIRSF001123; PepA_GA; 1.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196207}.
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   338 AA;  36673 MW;  D49DA6055FFA1711 CRC64;
     MIKDYTQTWG VSGLEKNVSD LIIREVMDYA DEITRDAMGN LIVLKRGSGA DKKKIMCAAH
     MDEIGLCVVK ILDNGLLKVK QIGGVSALCS FMNRVRFENG TVGTVGVTDP IDTVKPKEID
     KLYIDIGAMS KEEAGKYVKP GDCAVFCGDY AELAGRNVMS KAFDDRIACY IQTEALKRIK
     NCYHDLYFVY TVQEEVGLFG STTSAETVKP DLGIAVDITG SFDVPGDENG NPVLGKGAAI
     KINDSSVICD CEMTKGLIDC AERNRIPYQR DALVAGGTDA GAINKSGGGV KVLGISIPTR
     YGHTPNSIVN LDDVEACIRL MECYLQEEIP IITQEKIK
//
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