ID   A0A0U4BNP6_9BACT        Unreviewed;       862 AA.
AC   A0A0U4BNP6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=AUC43_07865 {ECO:0000313|EMBL:ALW85015.1};
OS   Hymenobacter sedentarius.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW85015.1, ECO:0000313|Proteomes:UP000059542};
RN   [1] {ECO:0000313|EMBL:ALW85015.1, ECO:0000313|Proteomes:UP000059542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5B {ECO:0000313|EMBL:ALW85015.1,
RC   ECO:0000313|Proteomes:UP000059542};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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; CP013909; ALW85015.1; -; Genomic_DNA.
DR   RefSeq; WP_068191694.1; NZ_CP013909.1.
DR   AlphaFoldDB; A0A0U4BNP6; -.
DR   STRING; 1411621.AUC43_07865; -.
DR   KEGG; hyg:AUC43_07865; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000059542; Chromosome.
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:ALW85015.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059542};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..862
FT                   /note="Aminopeptidase N"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006847344"
FT   DOMAIN          80..267
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          304..513
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   862 AA;  97326 MW;  9277ADDEC52908C8 CRC64;
     MKYLVPGFTS LLLFIHLLAV AQSSGAGARK PATKASASKK TVPAVAPAPA PAGLVVPSWL
     PAEAPLQPAA TVLTDVVDTK LDVRFDYKKQ QLLGTAVLTL RSHFYPQAEV ALDAKGFEIQ
     KVELVGDKKN KGLNYNYNRR KLVIALDHPY PRTTAYQVRI VYVAKPNELP QGGSAAITSD
     KGLYFINPLG LEKNKPRQIW TQGETESNSC WFPTIDKPNQ RMTQEIRMTV EKQFKTLSNG
     LLVSSKANAD GTRTDTWKLN EPHAPYLATM VVGDFAVVND SWHGKPVDYY VEPQYAATAR
     AVFGHTPQML DFFSKKLGVE YPWEKYAQVA VRDYVSGAME NTTATTHGAS IQATRRDLID
     ANYQSGESTI AHELFHHWFG DYVTSESWAN LPLNESFADY SEFLWAEYKF GADEAGLVQE
     IKLNNYLEEA QSKREPLIRY RYTNREDMFD RHSYDKGGRV LHMLRKYLGD DAFFTSLNHY
     LVQNKQTPVE ISKLRTAFEE TTGEDLMWFF NQWFLQRGHP ELRITHSYTN GQVTLRVQQV
     QDTLFQPVFR LPVTVAVWTN NNQPTEHRIT VTKANQTFTL PASQKPNLVK FDNESQLLAQ
     FDEERTQDEL IFQFYHAQGY QQKAEAMELL HNKTTELSVS SLLRNALNDK FWAVRQAALS
     HLRRYRGPEP EGMRKDIQRL ANADANPRVR AKAINTLATL PDGTFGPIFS AAIGDSSALV
     AAAAVEALAK KPDVNTSQQV AALDNTSSSP LMLALANYYA TNGGLDQYAW FLRRLPDVAE
     SDLYAYFQSF GTLMTHIPSV ERDKGLKVLE DYARNAPQYY VRLGAYRGLA LLVPTTPELK
     AKLQNIREKE MDDRLKAFYN LM
//