ID A4BVX3_9FLAO Unreviewed; 549 AA.
AC A4BVX3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Aminopeptidase M1 family protein {ECO:0000313|EMBL:EAR13114.1};
GN ORFNames=PI23P_01432 {ECO:0000313|EMBL:EAR13114.1};
OS Polaribacter irgensii 23-P.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR13114.1, ECO:0000313|Proteomes:UP000003053};
RN [1] {ECO:0000313|EMBL:EAR13114.1, ECO:0000313|Proteomes:UP000003053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23-P {ECO:0000313|EMBL:EAR13114.1,
RC ECO:0000313|Proteomes:UP000003053};
RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR13114.1}.
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DR EMBL; AAOG01000001; EAR13114.1; -; Genomic_DNA.
DR RefSeq; WP_004568906.1; NZ_CH724148.1.
DR AlphaFoldDB; A4BVX3; -.
DR STRING; 313594.PI23P_01432; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_014298_1_1_10; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000003053; Unassembled WGS sequence.
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; 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 Aminopeptidase {ECO:0000313|EMBL:EAR13114.1};
KW Hydrolase {ECO:0000313|EMBL:EAR13114.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW Protease {ECO:0000313|EMBL:EAR13114.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003053};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..549
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002665630"
FT DOMAIN 52..219
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 271..473
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 413
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 549 AA; 63440 MW; 35827A501156AEBF CRC64;
MKHPFYLHLF FIVICSLNLQ AQGLLTEKDI FSRQDTLRGS ITPERVWWDL TYYHLEVTVA
PDKKYISGKN TIKYTVLNVY QTMQIDLQTP LQMTKVTQDG KELAIIHEGN AHFIKLTKAQ
VIGNTESIIV HYESNPKEAV NAPWDGGFSW KKDKNGNHFI ATSCQGLGAS VWWPCKDHMY
DEVKSMRISV TVPSHLMDVS NGRLESIEDH GTTKTYNWFV NNPINNYGVN VNIGDYTHFS
ETFDGEKGPL DMDYYVLKYN LAKAKKQFTD APKMMKAFEH WFGPYPFYKD GYKLVEVPYL
GMEHQSSVTY GNEFKQGYLG SDLSGTGWGL KFDFIIIHES GHEWFANNIT DIDAADMWIH
ESFTNYSESL FLDYYYGKKA ASEYVIGLRK SIANKTPIIG TYNVNKSGSS DMYNKGGNLL
HTLRQLIDND KKWRLILRKM NAQFYHQTVK TKQIEDFLST ETGFDLNPFF NQYLRTIKIP
TLAHKIENDT LKYRWTNTVP NFEMPLKTTI NGKEKWIYPA SNWKSLALKS AGTSFLIDEN
FYVFNKKVD
//