ID A5FA98_FLAJ1 Unreviewed; 623 AA.
AC A5FA98;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Aminopeptidase N-like protein peptidase family M1 {ECO:0000313|EMBL:ABQ07867.1};
GN OrderedLocusNames=Fjoh_4868 {ECO:0000313|EMBL:ABQ07867.1};
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:ABQ07867.1, ECO:0000313|Proteomes:UP000006694};
RN [1] {ECO:0000313|EMBL:ABQ07867.1, 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 ---------------------------------------------------------------------------
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; ABQ07867.1; -; Genomic_DNA.
DR RefSeq; WP_012026833.1; NZ_MUGZ01000004.1.
DR AlphaFoldDB; A5FA98; -.
DR STRING; 376686.Fjoh_4868; -.
DR KEGG; fjo:Fjoh_4868; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_015077_0_0_10; -.
DR OrthoDB; 9814383at2; -.
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; cd09604; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:ABQ07867.1};
KW Hydrolase {ECO:0000313|EMBL:ABQ07867.1};
KW Protease {ECO:0000313|EMBL:ABQ07867.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..623
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030164148"
FT DOMAIN 374..531
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 623 AA; 71218 MW; 1E523CB8CF9C355E CRC64;
MKKLSIHLAF TAFLILAQTG FAQELYMPRN IKAAYAKGTR SADGKPGKNY WQNHGKYTMD
ITVDAKTKMV SGTETIIYEN NSNDSLRNLV IRFVNNLHKP SAPRSGDVSE DFLSNGLTLT
SLKVAGETYN ENARNWGTVG NVKLKKALAP HSKTTINIDW NYPLSKESGR EGQIDESTFF
VAYSYPRVSV FDDYNGWDRI PHTDRQEFYN DFNDYVYSVK APKNFVVYAT GDFLNPDEVL
QPEFAARLKK SYSTDEILHI ANEQEMKSGI VTKQNEWNIW KFEAKNITDV CFGLSDHYLW
DASSVLVDKK TNRRASVQAA YDIKGTDFVN SVKNNQFALD WFSNNWPGIP YPYSKMTAFQ
GFADMEYPMM CNDSQMNDPK FAQLVQDHEV AHTYFPFYMG INETRYAYMD EGWATTFEYL
IGIAEHGKEA ADKFYKEFRV EYYINDKSTE EDQPIISMST QVSGPGYGNN SYGKASLSYL
ALKDMLGDDL FKKALHHYMD TWNGKHPIPW DYFNSMNTGS GKNLNWFFNN WFFTNNYIDI
SVKNVSKNIV SIQNKGGFAI PFDVIVVYAD NSTETIHETP SVWEKNQKTA QVAVNTKKQI
KKVTVDGGIF LDATPDDNIW NSK
//
