ID A0A0D3LH95_9BACT Unreviewed; 622 AA.
AC A0A0D3LH95;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Peptidase M1 membrane alanine aminopeptidase {ECO:0000313|EMBL:AHM61092.1};
GN ORFNames=D770_14190 {ECO:0000313|EMBL:AHM61092.1};
OS Flammeovirgaceae bacterium 311.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM61092.1, ECO:0000313|Proteomes:UP000064112};
RN [1] {ECO:0000313|EMBL:AHM61092.1, ECO:0000313|Proteomes:UP000064112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=311 {ECO:0000313|EMBL:AHM61092.1,
RC ECO:0000313|Proteomes:UP000064112};
RA Fang C.;
RT "Complete bacteria genome obtained just from illumina data.";
RL Submitted (NOV-2012) 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; CP004371; AHM61092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D3LH95; -.
DR STRING; 1257021.D770_14190; -.
DR KEGG; fbt:D770_14190; -.
DR PATRIC; fig|1257021.3.peg.3214; -.
DR OrthoDB; 9814383at2; -.
DR Proteomes; UP000064112; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:AHM61092.1};
KW Hydrolase {ECO:0000313|EMBL:AHM61092.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW Protease {ECO:0000313|EMBL:AHM61092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064112};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..622
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002274062"
FT DOMAIN 340..494
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 599..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 435
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 622 AA; 71495 MW; 6F0141688AA955B8 CRC64;
MQKPFLITSL LCLLQVIATA QPDRWQQRAE YTMAVEMDVS TNRYTGTQKL VYHNNSPDTL
NRVFYHLYFN AFQPGSEMDW RSRTIDDPDP RVGSRINELK PNEIGYLRAQ SLEQDGNKVE
FTEEGTILVV NLARPLLPGT STTLDMRFEG QVPLQIRRSG RDSNEGIRYT MTQWYPKLAE
YDYEGWHPNA YIGREFYGVW GDFDVKITLD GSYTVGATGY LQNPQNIGHG YAPGTKQPKL
KKGQKLTWHF VAPNVHDFAW AADPDYVHDM VQVPNGPMLH FFYQNDPAYA GIWKQMQPYA
VEAFQVMNRD FGVYPYEQYS FIQGGDGGME YPMATMITGN RNLNSLVGVA VHEAVHSWYQ
MVLGTNESLY AWMDEGFTSY ASSHVMNIIF DQNKENPHLA SIQSYIGLAR SNQQEPLTTH
ADRYKRNRTY SINSYSKGAV LLSQLSYVMG HEQMMEGMRR YYNTWKFKHP NPTDFKRVME
KTADLELDWL FLEWVGTTNT IDYAIRAVEA AEDGNTRIRL QRIGELPMPV DLVVTYADGS
KELIYIPLRM MWGEKEEDLG LKRTLAADWP WVYNTYDLSI SKPVNEIRQL EIDPSGRLAD
IDQSNNKWSV PANSSPQQPK AP
//
