ID   A0A1I0PUB6_9BACT        Unreviewed;       846 AA.
AC   A0A1I0PUB6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=SAMN05428988_2800 {ECO:0000313|EMBL:SEW18045.1};
OS   Chitinophaga sp. YR573.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW18045.1, ECO:0000313|Proteomes:UP000198758};
RN   [1] {ECO:0000313|EMBL:SEW18045.1, ECO:0000313|Proteomes:UP000198758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR573 {ECO:0000313|EMBL:SEW18045.1,
RC   ECO:0000313|Proteomes:UP000198758};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; FOJF01000001; SEW18045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0PUB6; -.
DR   STRING; 1881040.SAMN05428988_2800; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000198758; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001930; Peptidase_M1.
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; PF13646; HEAT_2; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:SEW18045.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..846
FT                   /note="Aminopeptidase N"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011646471"
FT   DOMAIN          58..245
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          283..491
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   846 AA;  95897 MW;  77A8351F4ABD4270 CRC64;
     MSKPFKQVLK SLLLGGVTGM FFLTPAVAQQ QETPPQNDPL LKIYRGTTTR INDLVNTKLD
     VRFDYPKRYL YGKAWITLKP HFYATDSLLL DAKGMEIKQI AVVKNGKNTP LKYEYDGSQL
     HIKLDKSYQR TESYIIYADY TARPEEVKAE GSAAITDAKG LYFINHDGTE PNKPIQIWTQ
     GETESNSVWF PTIDRTAQKM TDEISMTVEK KYVTLSNGKL VSQKDNADGT RTDTWKMELP
     HSPYLVMMAV GDFSIVKDQW RGKEVNYYVE KPYAPYAKAI FGNTPEMLSF YSDILGYEYP
     WAKYSQIVVR DYVSGAMENT TATLHGDFLQ KTDRELLDNN HYDEAVVAHE LFHHWFGDLA
     TAESWSNLTL NESFADYSEY LWLSHKYGKD MADDHAYKAA KNYIQFTEYA GDRDLVRFHY
     HDKEDMFDAV SYQKGGRILN MLRNVVGDSA FFKSLNLYLK TNAFKSAEAH QLRLAFEEVS
     GQDLNWFFNQ WYFGQGYPIL DISYNYDDAG KKVSVIIQQK QPGDKVFELP IAIDVYAGGK
     KTRHLVTIND KSETFTFPYT TRPDFVNVDA EKVILDDKDD HRDINTYIFE YANAPEYGDR
     REAIEACLKE QTTNPAARKT VIAALKDKFY GLRSLTVAGL EMEDESVKTA ALPVLQQLAQ
     NDENSSVRAA ALRQLGKLKD KQLIPLFEKA TKDRSYAAAG AGLAGLAQLD LEKSYALAKQ
     LEAESKGALS NAIATVYAQK GNDADVAFFA KAFDEANGQE KFEAAMQYIG ILANVDNTET
     VIKGLDQIQN MAKLFNNKMV NSYLVKMLQP LAKKKQDKAS LATPEIKAEL NKQSDYILKI
     VNSLNK
//