ID   A0A1I2FLP1_9BACT        Unreviewed;       548 AA.
AC   A0A1I2FLP1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:SFF05426.1};
GN   ORFNames=SAMN04488541_101435 {ECO:0000313|EMBL:SFF05426.1};
OS   Thermoflexibacter ruber.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Thermoflexibacteraceae;
OC   Thermoflexibacter.
OX   NCBI_TaxID=1003 {ECO:0000313|EMBL:SFF05426.1, ECO:0000313|Proteomes:UP000199513};
RN   [1] {ECO:0000313|EMBL:SFF05426.1, ECO:0000313|Proteomes:UP000199513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GEY, DSM 9560 {ECO:0000313|Proteomes:UP000199513};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FONY01000014; SFF05426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2FLP1; -.
DR   STRING; 1003.SAMN04488541_101435; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000199513; 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; IPR042097; Aminopeptidase_N-like_N_sf.
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; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:SFF05426.1};
KW   Hydrolase {ECO:0000313|EMBL:SFF05426.1};
KW   Protease {ECO:0000313|EMBL:SFF05426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199513};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..548
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011481320"
FT   DOMAIN          265..461
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   548 AA;  64315 MW;  CC247C34F9FE5C16 CRC64;
     MRYYLLFAVF SFLSQSLFAQ ENPLSFTHQD SLRGTLFPER ACYDVTFYDL NLKIHPESQT
     IKGYNEIHYK ASQDFQVLQI DLFENLQIDR ILQGSNLLKF KREGNATFVY FPEKQKQGST
     NSIKVYYQGK PQIARRPPWE GGLTWTKDKE GNDWIAVSCE GLGASVWFPN KDHLSDEPDS
     IRLYFEVPKG LMCVANGNLI SQKAVNNLYD SYEWKVSYPI NNYNITFVVG KLAHFQDTYE
     SKDKEKLALD YYVLAYNLEK AKTHFQQVKK MLACYEEKFG KYPFWKDGYA LVETPFWGME
     HQGAIAYGNN YINNELGFDF IIVHESGHEY FGNSISVGDH AEMWIHEGFT TYSDALFVEC
     LTGSYDQYVA YLKKFKDKIQ NLDPVLAPLG VNYRYWRGSD MYYKGAWMLH TLRSLLANDA
     LWFKTLYDFH QTFKLSIVNS EQVIDFFCAK LGKQYRPILN QYLKYAKPPI LKIYKRQKGK
     RLELHYKLEA QEPNFELPIR LKISDSKEKL PSLKPQKDWQ KIKLKLNKNQ SVDFEQDLYY
     FLIEDTST
//