GenomeNet

Database: UniProt
Entry: A5FFX2_FLAJ1
LinkDB: A5FFX2_FLAJ1
Original site: A5FFX2_FLAJ1 
ID   A5FFX2_FLAJ1            Unreviewed;       551 AA.
AC   A5FFX2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   SubName: Full=Peptidase family M1, membrane alanine aminopeptidase {ECO:0000313|EMBL:ABQ05889.1};
GN   OrderedLocusNames=Fjoh_2868 {ECO:0000313|EMBL:ABQ05889.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ05889.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ05889.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000685; ABQ05889.1; -; Genomic_DNA.
DR   RefSeq; WP_012024927.1; NZ_MUGZ01000033.1.
DR   AlphaFoldDB; A5FFX2; -.
DR   STRING; 376686.Fjoh_2868; -.
DR   KEGG; fjo:Fjoh_2868; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_014298_1_1_10; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000006694; 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; 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:ABQ05889.1};
KW   Hydrolase {ECO:0000313|EMBL:ABQ05889.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW   Protease {ECO:0000313|EMBL:ABQ05889.1}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..551
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030164407"
FT   DOMAIN          51..225
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          270..474
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        414
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
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         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   551 AA;  63484 MW;  ECC31B128EA7390A CRC64;
     MKKYFGSVIT AFLIGFAANA QGLLNKSETV FTHQDSLRGS ITKERAWWDL KYYHLDIKVN
     PTDRTISGTN TVRYTVLNEY NRMQIDLQEP MNITKVTQNG KDLKFERDGN AFFITLSENQ
     KAGETKEIIV SFGGVPKEAV RPPWDGGITW QKDKNGKDFI ASSCQGLGAS VWWPCKDHMY
     DEVENMLISV NVPGNLTDVS NGRLQSVKKQ KDGTKTFNWY VANPINNYGV NINIGDYVNF
     SEKFKGEKGD LDCNYYVLRD NLAKAKEQFK DAPKMLKAFE SWFGPYPFYE DSYKLVEVPY
     LGMEHQSSVT YGNNYQNGHN GHDISGTGWG LKFDYIIIHE SGHEWFANNI TYKDIADMWI
     HESFTTYSEV LFIEYYYGKD AANEYARGIR KMIANKEPII GHYDVNREGS GDMYPKGANM
     IHTIRQVIND DAKFKAILRG MNKTFYHQTV TTKQIEDYIS KESGIDFSAV FNQYLRTPQV
     PVFEYYFKNQ KLAYHWINCQ ENFDLPLKVI LNGVETWLKP TSDWQAKDLN SEKTVLTVDK
     NFYVIESNIT N
//
DBGET integrated database retrieval system