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Database: UniProt
Entry: J0RXJ5_9FLAO
LinkDB: J0RXJ5_9FLAO
Original site: J0RXJ5_9FLAO 
ID   J0RXJ5_9FLAO            Unreviewed;      1195 AA.
AC   J0RXJ5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Aminopeptidase N-like protein {ECO:0000313|EMBL:EJG00470.1};
GN   ORFNames=FF52_15089 {ECO:0000313|EMBL:EJG00470.1};
OS   Flavobacterium sp. F52.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1202532 {ECO:0000313|EMBL:EJG00470.1, ECO:0000313|Proteomes:UP000002690};
RN   [1] {ECO:0000313|EMBL:EJG00470.1, ECO:0000313|Proteomes:UP000002690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F52 {ECO:0000313|EMBL:EJG00470.1,
RC   ECO:0000313|Proteomes:UP000002690};
RX   PubMed=22965088; DOI=10.1128/JB.01249-12;
RA   Kolton M., Green S.J., Harel Y.M., Sela N., Elad Y., Cytryn E.;
RT   "Draft Genome Sequence of Flavobacterium sp. Strain F52, Isolated from the
RT   Rhizosphere of Bell Pepper (Capsicum annuum L. cv. Maccabi).";
RL   J. Bacteriol. 194:5462-5463(2012).
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:EJG00470.1}.
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DR   EMBL; AKZQ01000030; EJG00470.1; -; Genomic_DNA.
DR   AlphaFoldDB; J0RXJ5; -.
DR   PATRIC; fig|1202532.3.peg.3095; -.
DR   eggNOG; COG0308; Bacteria.
DR   eggNOG; COG1277; Bacteria.
DR   Proteomes; UP000002690; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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:SF304; 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:EJG00470.1};
KW   Hydrolase {ECO:0000313|EMBL:EJG00470.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EJG00470.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        419..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        468..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        496..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        541..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        587..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          879..1077
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          765..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1195 AA;  138317 MW;  7A66D0B6F70D587D CRC64;
     MFTLIYYLKI NLKNNVMLSK LIQFEWHNNT RNWTFYAIFI IYLVLGFFVS AFANFSFSGA
     YKNSPFTLTY AIGLISLMTI FSTTLLVAQH FLKEYETKFD AIIFSTPISK FYYLGSKFIT
     AFVIAVSSFG MFIIGMIIGH QMSWIPRTEI GPFEILNYVW PYLVIVVPNI FLCLSILATL
     AWLTRSKLFV YVGGLFIYLL YIAGSIFSNS PLFANASPSS AKAMSLAAKI DPFGLAAFLE
     QTRYWTSIEK NTQLISLSGN FLFNRILWIC ISFLLIFASY KMFSFRKTKT KKVKTIKTNA
     RETKTYSAVI PKQLEFKTSK HNWAVFKSNL KMDFYLILKG IPFLLIVILL SGLLMIEISD
     EIDGGIRLAE KITDTALMIS TIMDRLPFIL ILIILFYSSE LLNRSENSRF EMLENTAPYS
     QLIVLLSKLT VLFMIPLILI GISVLIGIGF QIIHANAPIE AGLYFSMFYY IGFPLFLISI
     LVIAIQTFVK NKYLGLAVSA FIVLLFCTGI GQQLGITHTL FRFGDSFKRE YFDLNGFGSY
     TYPFHISMLY NSGLTLILLT LTGILWKRNS SILKTIRRNS FNSIQKITFV LGIILLIGFG
     SYLFYKTNIE YPYLTKDDFN NWSEQYELQF KKYTNFAQPT IIAVKSKVDM FPEENRYEVS
     GTYELINNSE KPIDSLLLYI DRNSKLTSVA IENAKNLDDS SEFQHYWYLL EKPLQPHQKM
     KMSFAFTSTW SPFKGHTAFN SIIENGSFMR ISRYFPTFGY QDSNEISSKK EREKRHLKPQ
     TPLKRLEDKS KTTNDFIDYD VVVSTSKNQT AIGIGDLVGN WKKDNRNYFH YKSNGKIPFR
     FAFSSAEYQI QKTNYKGISI EVYYDKRHSR NVAKLIQDVK NTLDYCQNNF GKYPYKTIRY
     AEVSAFADGF AATSYPSTVF MKENFGFYSN LNNRDKEDVI NQLTAHELSH EWWGNAQISP
     EQKEGSWILT ETLAQYTELM LYEKEHGLEK ALETLKIHLD LYLSSRSYEL ETPLYKTNYE
     TPHLPYDKGM LVMHHLRVLI GEEKVNLALQ NFLNHYKHPN PIPDSEDLLS EIYLVTDSKL
     YPKLDEMFKK IITYSSKISE VESVKKNGFY EVSFKADTKK YIENATGIRK QIDNDKTIDI
     GIYDENGKLF RYTFPIKNNR IEGKIKFKNK PQRIVIDPLL MNIDTFIKDN EKEID
//
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