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Database: UniProt
Entry: A0A1Y0MKU9_9FLAO
LinkDB: A0A1Y0MKU9_9FLAO
Original site: A0A1Y0MKU9_9FLAO 
ID   A0A1Y0MKU9_9FLAO        Unreviewed;       540 AA.
AC   A0A1Y0MKU9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Peptidase M1 {ECO:0000313|EMBL:ARV10977.1};
GN   ORFNames=BTO09_00865 {ECO:0000313|EMBL:ARV10977.1};
OS   Gilvibacter sp. SZ-19.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gilvibacter.
OX   NCBI_TaxID=754429 {ECO:0000313|EMBL:ARV10977.1, ECO:0000313|Proteomes:UP000196054};
RN   [1] {ECO:0000313|EMBL:ARV10977.1, ECO:0000313|Proteomes:UP000196054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZ-19 {ECO:0000313|EMBL:ARV10977.1,
RC   ECO:0000313|Proteomes:UP000196054};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-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};
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DR   EMBL; CP019333; ARV10977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0MKU9; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000196054; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000196054};
KW   Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT   DOMAIN          40..211
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          322..463
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        329
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        403
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   540 AA;  62268 MW;  FC9CE2A5BEAC8DAD CRC64;
     MNYRFLFLLL SCSISFGQNY SRQDSLRGQI TAERAWWDLQ HYQLDVTVDI DNQSISGSNI
     ITYKVLKNGD RLQLDLQEPM RIEKVVQDGK ELEWTSEGIA HFVKLRKKMK PGKEEQIKVF
     FSGKPRIAKN PPWDGGFVFT QDSNGKAFVA NANQGIGASI WWPNKDHPYD EPDQGTVISV
     TTPKDLMDVS NGRLIKVDST ATTKTWTWQV VNPINNYGIN VNIGDYVHFR EIHEGEKGNL
     DVDYYVLREN EAKARKQFEQ TTGMLAAFEY WFGPYPFYED GFKLVEAPYL GMEHQSSVTY
     GNGYKNGYRG YDLSGSGWGM KFDFIIIHEA GHEWFANNIT TTDVADLWVH EGFTAYSENL
     YLDYHFGANA AADYVVGTRK IIMNDKPIIG TYGVREEGSS DMYYKGANML HTLRQLIEDD
     LQWRSILRGL NEDFRHQTVS SKQVEDYISK ATGKDLSAFF NQYLRTTMIP NLEVKMAGNK
     LSYRYTNIVE NFDMPVIAML NDTEKWIFPS SEWKTEELDL NLKFFAVKRD FYVDYQLIAN
//
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