ID A0A3S0MCU1_9FLAO Unreviewed; 624 AA.
AC A0A3S0MCU1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE SubName: Full=M1 family peptidase {ECO:0000313|EMBL:RTY97913.1};
GN ORFNames=EKM02_12965 {ECO:0000313|EMBL:RTY97913.1};
OS Flavobacterium sp. RSP49.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2497487 {ECO:0000313|EMBL:RTY97913.1, ECO:0000313|Proteomes:UP000272024};
RN [1] {ECO:0000313|EMBL:RTY97913.1, ECO:0000313|Proteomes:UP000272024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSP49 {ECO:0000313|EMBL:RTY97913.1,
RC ECO:0000313|Proteomes:UP000272024};
RA Liu Q., Xin Y.-H.;
RT "Flavobacterium sp. nov., isolated from glacier ice.";
RL Submitted (DEC-2018) 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:RTY97913.1}.
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DR EMBL; RYDN01000034; RTY97913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0MCU1; -.
DR Proteomes; UP000272024; 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 Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..624
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018531038"
FT DOMAIN 360..507
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 448
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 624 AA; 71435 MW; 086B58E794072E73 CRC64;
MKKLLLFSFV VFGLGTVFAQ NTSYWQQHVD YKMDVTLDVK THQYTGKQEL VYTNNSSDTL
RKVYYHLFNN AFQPGSEMDA RIQSIKDPDG RMVTKIKVDG KEVKESRIKN LKPNEIGFLR
ISNFKQDGAV ATAKEVGTIL EVTLAKEILP NTKTTFTLDF EGQVPIQIRR SGRNNAEGVA
LSMSQWYPKM AEFDFEGWHA DPYIAREFHG VWGNFDVNIT IDKDYVLGGT GYLQNKNEIG
HGYQDQGVVV SVPKKTKMLT WHFNAPMVHD FTWAADPDYI HDVVKGPNGV DLHFLYKNNP
KYIQNWKNLQ PKTVQLMEIY NKTVGDYPYK QYSVIQGGDG GMEYAMCTLI LGQGSFEGLL
GVTAHEMAHS WFQHVLASNE SKHGWMDEGF TSFLEDFGLN EIADKKVENP FAGAYTSYFS
MVNSGKELPQ GTHADRFDEN RVYSITSYSK GEIFLTQLMY LIGKDNVMKT LKRYYSDFKF
KHPTPNDIKR SAERVSGANL DWYLVDWTQT TNTIDYGIKD VKENADKTTV TLERIGRMPM
PIDLLVEYTD GKTESFYIPL RMMSFEKENP NPAIKRTVLN DWAWAYPTFE FDISKSKASI
KKITIDSSGL MADLKKENNT YEIK
//
