ID A0A1R1A5E7_9BACL Unreviewed; 349 AA.
AC A0A1R1A5E7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:OME80794.1};
GN ORFNames=BK120_19175 {ECO:0000313|EMBL:OME80794.1};
OS Paenibacillus sp. FSL A5-0031.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920420 {ECO:0000313|EMBL:OME80794.1, ECO:0000313|Proteomes:UP000187447};
RN [1] {ECO:0000313|EMBL:OME80794.1, ECO:0000313|Proteomes:UP000187447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0031 {ECO:0000313|EMBL:OME80794.1,
RC ECO:0000313|Proteomes:UP000187447};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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:OME80794.1}.
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DR EMBL; MRTD01000010; OME80794.1; -; Genomic_DNA.
DR RefSeq; WP_076269105.1; NZ_MRTD01000010.1.
DR AlphaFoldDB; A0A1R1A5E7; -.
DR OrthoDB; 361940at2; -.
DR Proteomes; UP000187447; 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 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:OME80794.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 349 AA; 38152 MW; C3E9FA3C415558C5 CRC64;
MSLPLSKQLN RDFILSQLEA LLNIPSPSGY CMDIVKHLGV EAEKLGYSLE ITPKGNGMIT
IPGVNSEKVI GITAHLDTLG AMVRSIKSDG KLRFTSIGGY NMQTVEGEYC VIHTRDGRKY
EGTVLSTKAS VHVYSDSREW KREEANMEIR IDELVKTKAD TEGLGISVGD IISWEPRVRI
FPNGWVKSRH LDDKASVAAL LGLMEWFKRE GNTPAHTLKL IFSTYEEVGH GSSYIPEDIT
EMIAVDMGAL GDDLSATEQD ISICAKDSTG PYDYNMTTKL IELAKRENLA YAVDIYPHYG
SDASAALRGG SNIRAALIGP GVHASHGMER THADAIVGTS ALLLAYVME
//
