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Database: UniProt
Entry: A0A226HJZ7_9FLAO
LinkDB: A0A226HJZ7_9FLAO
Original site: A0A226HJZ7_9FLAO 
ID   A0A226HJZ7_9FLAO        Unreviewed;       551 AA.
AC   A0A226HJZ7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase M1 {ECO:0000313|EMBL:OXA94472.1};
GN   ORFNames=B0A75_19740 {ECO:0000313|EMBL:OXA94472.1};
OS   Flavobacterium oncorhynchi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=728056 {ECO:0000313|EMBL:OXA94472.1, ECO:0000313|Proteomes:UP000198336};
RN   [1] {ECO:0000313|EMBL:OXA94472.1, ECO:0000313|Proteomes:UP000198336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 59446 {ECO:0000313|EMBL:OXA94472.1,
RC   ECO:0000313|Proteomes:UP000198336};
RA   Stine C., Li C., Tadesse D.;
RT   "Whole genomes of Flavobacteriaceae.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
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:OXA94472.1}.
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DR   EMBL; MUHA01000036; OXA94472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226HJZ7; -.
DR   Proteomes; UP000198336; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..551
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012307938"
FT   DOMAIN          51..227
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          271..474
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        414
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   551 AA;  63641 MW;  76BE3651FEA4EC58 CRC64;
     MKKIFSGVFI AFLIGFTANA QGLLKKSETV FTHQDTLRGS ITKERAWWDL KYYHLDVKIN
     PKEKTITGSN TVRYTVLSEY NKMQIDLQEP MQIYKVTQGG KDLKFKRDGN AFFIDLIEKQ
     KVGEVKEIVI SFGGKPREAV NAPWDGGISW KKDKNGKDFI ASSCQGLGAS VWWPNKDHMY
     DEVENMLISM NVPGDLTGVS NGRLQSVKKQ KDGTKTFNWY VSNPINNYGV NINVADYVNF
     SEKFKGEKGD LDCSYYVLRD NLALAKEHFK DAPRMLKAFE NWFGPYPFYE DSYKLVEVPY
     LGMEHQSSIT YGNDYKMGYR GKDLSGTGWG LKFDFIIIHE SGHEWFANNI TYKDIADMWV
     HESFTNYSES LFIEYYYGKD AAAEYVIGCR RNIQNDKPII GHYDVNNEGS GDMYPKGANM
     LHMIRQVIND DAKWKSILRG MNKTFYHQTV TGKQIQDYIN EKSGINFNRV FAQYLTTTQI
     PVFEYMFKNG TFGYHWTNCV ANFDMPVRVK LNGVETWLKP TTEWKSEKTT NENRTIEVDK
     DFYVTSSNII E
//
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