ID A0A0C1IFI8_9BACT Unreviewed; 553 AA.
AC A0A0C1IFI8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Peptidase M1 {ECO:0000313|EMBL:KIC92915.1};
GN ORFNames=OI18_20225 {ECO:0000313|EMBL:KIC92915.1};
OS Flavihumibacter solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC92915.1, ECO:0000313|Proteomes:UP000031408};
RN [1] {ECO:0000313|EMBL:KIC92915.1, ECO:0000313|Proteomes:UP000031408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-3 {ECO:0000313|EMBL:KIC92915.1,
RC ECO:0000313|Proteomes:UP000031408};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL Submitted (NOV-2014) 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:KIC92915.1}.
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DR EMBL; JSVC01000026; KIC92915.1; -; Genomic_DNA.
DR RefSeq; WP_039143302.1; NZ_JSVC01000026.1.
DR AlphaFoldDB; A0A0C1IFI8; -.
DR STRING; 1349421.OI18_20225; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000031408; 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; IPR045357; Aminopeptidase_N-like_N.
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 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:UP000031408};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..553
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002133472"
FT DOMAIN 56..232
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 274..478
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 418
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 553 AA; 62564 MW; 1BC5924AF25F3BED CRC64;
MQLTSITRGF IGSLLTISLS LSATAQQPLS KTEVLTKQDT LRGTLNAERS WWDVTRYDIS
VTPDYETKTI KGTVTMSFKV TGKGNAMQVD LQEPMMLDKA EINGKSLKIT REGNAFHIAI
NKALPVNSTQ KILLSYSGKP TEAVRPPWDG GWIWKKDKAG NPWMSVACQG LGASVWYPCK
DHQSDEPDNG ASLSMTVPSD LVAVGNGRLI KKTPAGDKTT YVWEVKNPIN NYNIIPYIGK
YASWKETYKG EKGNLDCEYW VLEEDLDKAK QQFQQVKPMM ECFEHWFGPY PFYEDGYKLV
QSPHLGMEHQ SAVAYGNRFM NGYLGKDLSG TGHGLKWDFI IIHETGHEWF GNNITTKDIA
DMWVHEGFTN YSETIYTTCQ SGVTAGNEYL AGIRRNIQNN IPIIGQYGVN KEGSGDMYAK
GANMIHIIRQ LIGDDEKFRQ LLRGLNKDFY HKTVTSAEVE KYINQFAGKD FSKIFDQYLR
TVKIPQLQYQ FLAGTLSYRW RNSVDGFDMP VKVKLDGTDT WLEPTPEWKT LTTPATSLEA
DKNFYIETKQ QGS
//
