ID A0A1W6MJU7_9FLAO Unreviewed; 545 AA.
AC A0A1W6MJU7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidase M1 {ECO:0000313|EMBL:ARN77870.1};
GN ORFNames=BST97_07565 {ECO:0000313|EMBL:ARN77870.1};
OS Nonlabens spongiae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=331648 {ECO:0000313|EMBL:ARN77870.1, ECO:0000313|Proteomes:UP000193431};
RN [1] {ECO:0000313|EMBL:ARN77870.1, ECO:0000313|Proteomes:UP000193431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13191 {ECO:0000313|EMBL:ARN77870.1,
RC ECO:0000313|Proteomes:UP000193431};
RA Kumagai Y.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
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};
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DR EMBL; CP019344; ARN77870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6MJU7; -.
DR STRING; 331648.BST97_07565; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000193431; 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:UP000193431};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..545
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010867848"
FT DOMAIN 50..226
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 269..472
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 412
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 545 AA; 63183 MW; B3E67C1789233C01 CRC64;
MKNIKIIVAI ILLMGIQQVS AQLLQDKNQF TRQDTLRGSI TQERAWWDLK YYDLEVEVFP
DRKFIKGQNT ITYTVNEPYQ LMQVDLQAPM KITKVTQNGK NLLVTDEGNT HFIKLINNQK
TGKEYEVVVH FEGEPREARN APWDGGFSWK KDKNGKHFIA TSNQGLGASV WWPCKDHMYQ
EPEGMTITAT VPEDLICVSN GRLIKEKNKG GKTAYTWQVK NPINNYGVNL NIGDYVNFSE
VYDGEKGDLD MDYWVLKDNL EKAKEHFKDA PKMMKAFEHW FGPYPFYEDS FKLVEVPYLG
MEHQSSVTYG NKYVKGYLGQ DLSRTGWGLK FDFIIIHEAG HEWFANNITN KDIADMWIHE
GFTAYSESLF LDYHYGTDAA NAYVIGTRRS IQNDRPLIGV YGVNNEGSGD MYYKGANLLH
TLRQIVSNDE KWRSILRGMN ETFYHRTVTT QEIEDYLNKN IDLDLKPIFD QYLRTTDIPL
FKYEIKDGKL YYHYDNVVTG FSMPLQVAIN GTLHMLQPQE EEQVFSLDQL IEKVEVNPNF
YVGVQ
//