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
//