ID   A0A327Q2G0_9BACT        Unreviewed;       544 AA.
AC   A0A327Q2G0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Peptidase M1-like protein {ECO:0000313|EMBL:RAI97901.1};
GN   ORFNames=LX64_04951 {ECO:0000313|EMBL:RAI97901.1};
OS   Chitinophaga skermanii.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=331697 {ECO:0000313|EMBL:RAI97901.1, ECO:0000313|Proteomes:UP000249547};
RN   [1] {ECO:0000313|EMBL:RAI97901.1, ECO:0000313|Proteomes:UP000249547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23857 {ECO:0000313|EMBL:RAI97901.1,
RC   ECO:0000313|Proteomes:UP000249547};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-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:RAI97901.1}.
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DR   EMBL; QLLL01000013; RAI97901.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327Q2G0; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000249547; Unassembled WGS sequence.
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; IPR042097; Aminopeptidase_N-like_N_sf.
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; 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:UP000249547};
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..544
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016418705"
FT   DOMAIN          262..467
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        333
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        407
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
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         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   544 AA;  62699 MW;  715257DA8C6D5D88 CRC64;
     MRRIFLLLMG IVGTSSVFAQ HQTTFTKADT LRGTLNADRI WWDVTFYDLH VNVHPADSSL
     QGHNTIRYKV LKPHNKMQID LQVPMQIDSV VQNNRSLKFT RDGNAFLVQL EATQTKGSTQ
     AITVHYSGKP RVAIRAPWDG GLVWSKDSLG RPWIATACQG LGASVWWPNK DHQSEEPDSM
     SITVTVPKGL IDVSNGRLRS KQENENTTTF NWYVQNPINN YDVALNIAHY SNFTDVYDGE
     KGKLDLSYWV IDYNLEKAKK HFEVVKPMMQ CFEHWFGPYP WYEDSYKLVE TPHLGMEHQS
     AVAYGNKYKM GYNGRDLSGS KWGIKWDFII IHESGHEWFG NNITTKDIAD MWVHESFTNY
     SETIFTECQY GKEAGNEYNQ GARRNIQNDI PVIGHYGVNS EGSGDMYYKG SAMIHTIRQV
     IDNDEKFRSI LRGLNKTFYH QTVTTKQVEE YINKMAGRNF NKVFDQYLRT TGVPVLEYKV
     EGNKLSYRWK ADVKGFDLPV KVKINGSTNF QFLYPTTESW KTMVVDNFTS LEADKNFYIK
     VSKH
//