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Database: UniProt
Entry: A0A1H9AVV2_9BACT
LinkDB: A0A1H9AVV2_9BACT
Original site: A0A1H9AVV2_9BACT 
ID   A0A1H9AVV2_9BACT        Unreviewed;       373 AA.
AC   A0A1H9AVV2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Putative aminopeptidase FrvX {ECO:0000313|EMBL:SEP80914.1};
GN   ORFNames=SAMN05444359_102247 {ECO:0000313|EMBL:SEP80914.1};
OS   Neolewinella agarilytica.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC   Neolewinella.
OX   NCBI_TaxID=478744 {ECO:0000313|EMBL:SEP80914.1, ECO:0000313|Proteomes:UP000199021};
RN   [1] {ECO:0000313|Proteomes:UP000199021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24740 {ECO:0000313|Proteomes:UP000199021};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOFB01000002; SEP80914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9AVV2; -.
DR   STRING; 478744.SAMN05444359_102247; -.
DR   InParanoid; A0A1H9AVV2; -.
DR   Proteomes; UP000199021; 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; cd05656; M42_Frv; 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: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   ECO:0000313|EMBL:SEP80914.1}; 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:UP000199021}.
FT   ACT_SITE        227
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   373 AA;  41385 MW;  4D49F87BDD448094 CRC64;
     MLFRLEQISN YFMATLTKQS EQFLNNYLNN ASPTGFESAG QKLWLEYIRP YVDEVGLDNY
     GTAYGVINPG KDYRVVIEGH ADEISWFVHY ISDNGYINVI RNGGSDHQIA PSKRVNIHGT
     KGIVRGVFGW PAIHTRRGDE AKLQAQIHNI FIDVGAKDKA EVLEMGIHVG SVITYPDELE
     VMNDRFYCGR ALDNRMGGFC IAEVARLLKK NKIELDYTLY IVNSVQEEVG LRGAQMIADS
     IKPDVAIVTD VTHDTGTPLL NKKKVGDVQA GKGPSVTYAP AVHNKLLQMI IDTAEANSID
     IQREASSRAT GTDTDAFAYS NGGVPSALIS LPLRYMHTTV EMAHKDDVEG VIQLIYETLQ
     VIKGGMSFKY FEV
//
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