ID A0A0A2M011_9FLAO Unreviewed; 630 AA.
AC A0A0A2M011;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Peptidase M1 {ECO:0000313|EMBL:KGO84803.1};
GN ORFNames=Q765_19665 {ECO:0000313|EMBL:KGO84803.1};
OS Flavobacterium rivuli WB 3.3-2 = DSM 21788.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121895 {ECO:0000313|EMBL:KGO84803.1, ECO:0000313|Proteomes:UP000030152};
RN [1] {ECO:0000313|EMBL:KGO84803.1, ECO:0000313|Proteomes:UP000030152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 3.3-2 {ECO:0000313|EMBL:KGO84803.1,
RC ECO:0000313|Proteomes:UP000030152};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO84803.1}.
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DR EMBL; JRLX01000036; KGO84803.1; -; Genomic_DNA.
DR RefSeq; WP_020213905.1; NZ_KB899971.1.
DR AlphaFoldDB; A0A0A2M011; -.
DR STRING; 1121895.GCA_000378485_02737; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 9814383at2; -.
DR Proteomes; UP000030152; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09604; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR Pfam; PF01433; Peptidase_M1; 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:UP000030152};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..630
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001991481"
FT DOMAIN 360..514
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 455
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 630 AA; 71440 MW; EE93D10747845EE8 CRC64;
MRTILAVALL SASGLFAQKS PNAGYWQQHV NYKMDVSVDV KTFKYTGKQQ LVYTNNSPDT
LRRVFYHLYN NAFQPNSEMD ARLQAIADPD SRMVITTKVG DKTTKTSRIA PLKPNETGYL
NITNFKQDNV AAKTIVSGTI LEVTLAKPIL PHSSTTFTLD FDAQVPLQIR RSGRNSADGI
ALSMTQWYPK MAEYDFEGWH ADPYIGREFH GVWGDFDVNI TIDKTYTIGG SGYLQNKNEI
GKGYEDAGVT VEIPKKAKTL TWHFFAPNVH DFAWGADPEY IHDKIIGENS VELHFFYKNK
PEFLDNWKRL QPKTAEILAY YDKNVGPYPY KQYSVVQGGD GGMEYAMCTL ITGGRSFGSL
VGTTAHEFAH SWFQHILATN ESKHYWMDEG FTSYISDLAM DAVLPPKVKE DEAPESPFKG
AYDNYFYLVK SGKEQPLTTH ADRYNSNTAY SIAAYSKGEI FLAQLGYVIG EEKLAQTLKR
YFADYKFTHP TPNDIKRTAE KVSGAELDWY LTDWCQTTNT IDYSIKEVKE AGANTTITLE
RIGLMPMPID IIVAYSDGTQ ESFYVPLNLM HYTKDNPFPK LKRTVLKEWD WAHPTFTFTI
NKPKDAIRIM AIDPSETMAD VNKANNLYSK
//