ID   A0A413I1X5_9FIRM        Unreviewed;       337 AA.
AC   A0A413I1X5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 12.
DE   SubName: Full=M42 family peptidase {ECO:0000313|EMBL:RGY01301.1};
GN   ORFNames=DXA57_07550 {ECO:0000313|EMBL:RGY01301.1};
OS   Blautia sp. OF03-15BH.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=2292287 {ECO:0000313|EMBL:RGY01301.1, ECO:0000313|Proteomes:UP000285119};
RN   [1] {ECO:0000313|EMBL:RGY01301.1, ECO:0000313|Proteomes:UP000285119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OF03-15BH {ECO:0000313|EMBL:RGY01301.1,
RC   ECO:0000313|Proteomes:UP000285119};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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:RGY01301.1}.
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DR   EMBL; QSCM01000005; RGY01301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A413I1X5; -.
DR   OrthoDB; 9772053at2; -.
DR   Proteomes; UP000285119; 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:SF0; AMINOPEPTIDASE YPDE-RELATED; 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:UP000285119}.
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         223
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   337 AA;  36747 MW;  B9AAFDC1D485CF45 CRC64;
     MREEGLLKKL VAAHGVSGFE KAVRKIIEEE AAPYADEMTV DAIGNLIVLK KGRDGADKKK
     LMFAAHMDEI GFMVKKIESD GRLKVCNMGW NWAGSAYNER VEFQNGISGV VGCEGWIEDA
     KNDVGKLFID IGATSAEDAA KYVKLGDVCG YFGPWIDLQN DRISSRSLDN RIGCYQLLEA
     LKENDGNCPN DVYYVFTVQE EVGCRGSQVT AERIRPDFGI AVDITPAHDY PCDLQGSNTV
     DGGTGIKICD PSVICDEDLV AAMEECCKNN SIKYQREVID KGGTDASSMN LSHQGVKAGG
     IVTVVRYPHA QCSVASKNDI EAGVDLMKAI SAYRFKD
//