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
//