ID A0A0B4S1V1_9FIRM Unreviewed; 341 AA.
AC A0A0B4S1V1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:AIZ36805.1};
DE SubName: Full=M42 family peptidase {ECO:0000313|EMBL:AXU10639.1};
GN ORFNames=DYJ31_04895 {ECO:0000313|EMBL:AXU10639.1}, NW74_05370
GN {ECO:0000313|EMBL:AIZ36805.1};
OS Parvimonas micra.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Parvimonas.
OX NCBI_TaxID=33033 {ECO:0000313|EMBL:AIZ36805.1, ECO:0000313|Proteomes:UP000031386};
RN [1] {ECO:0000313|EMBL:AIZ36805.1, ECO:0000313|Proteomes:UP000031386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCOM 1535 {ECO:0000313|EMBL:AIZ36805.1}, and KCOM 1535 / ChDC
RC B708 {ECO:0000313|Proteomes:UP000031386};
RA Kook J.-K., Park S.-N., Lim Y.K., Roh H.;
RT "Complete genome sequence of Parvimonas micra KCOM 1535 (= ChDC B708).";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXU10639.1, ECO:0000313|Proteomes:UP000258329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCOM 1037 {ECO:0000313|EMBL:AXU10639.1,
RC ECO:0000313|Proteomes:UP000258329};
RA Kook J.-K., Park S.-N., Lim Y.K.;
RT "Genome sequencing of Parvimonas micra KCOM 1037.";
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}.
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DR EMBL; CP009761; AIZ36805.1; -; Genomic_DNA.
DR EMBL; CP031971; AXU10639.1; -; Genomic_DNA.
DR RefSeq; WP_004833113.1; NZ_RKIS01000001.1.
DR AlphaFoldDB; A0A0B4S1V1; -.
DR GeneID; 71955366; -.
DR KEGG; pmic:NW74_05370; -.
DR OrthoDB; 361940at2; -.
DR Proteomes; UP000031386; Chromosome.
DR Proteomes; UP000258329; Chromosome.
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 CDD; cd05657; M42_glucanase_like; 1.
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:SF7; AMINOPEPTIDASE YHFE-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 ECO:0000313|EMBL:AIZ36805.1}; 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:UP000031386}.
FT ACT_SITE 217
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 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 341 AA; 38142 MW; 958E0A87F7F05293 CRC64;
MDRNYVKNLL EELLNIYSPT GDTENAICFM EKKFKELNIP CRRTNKNALI ATIEGEEKEA
ITFSGHVDTL GLMVKEIKAN GRLAFSLVGG FSPTSVETEN VFIKTYNGKL IPGTALYNEA
SVHVYDTTTT GQRSIKNMEI RIDEDVKTAE DVRKLGISVG DFICLDPRCR IYDSGFIKSR
HLDDKACIAA MMGLAKYLVE NKIKPKNTIN FFISNYEEIG HGSSFVPENT VEFFAVDMAA
PGVGQESDEK AVTICAMDST TPYDLGMRNK LRKIAEEKKI DYRIDIYPHY GSDATAALRA
GHDIRCALIG PGVDASHSYE RTHILGIENT YKLMLEYLLD K
//
