ID   A0A1B1AVZ6_9ACTN        Unreviewed;       497 AA.
AC   A0A1B1AVZ6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=AVL59_15015 {ECO:0000313|EMBL:ANP50756.1};
OS   Streptomyces griseochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP50756.1, ECO:0000313|Proteomes:UP000092659};
RN   [1] {ECO:0000313|EMBL:ANP50756.1, ECO:0000313|Proteomes:UP000092659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP50756.1,
RC   ECO:0000313|Proteomes:UP000092659};
RA   Wu L.;
RT   "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT   Blasticidin S producer.";
RL   Submitted (JUN-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; CP016279; ANP50756.1; -; Genomic_DNA.
DR   RefSeq; WP_067304026.1; NZ_JAGGLP010000008.1.
DR   AlphaFoldDB; A0A1B1AVZ6; -.
DR   KEGG; sgs:AVL59_15015; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000092659; 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; 1.10.390.10; 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; 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; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..497
FT                   /note="Aminopeptidase N"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008519265"
FT   DOMAIN          50..219
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          309..455
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   497 AA;  53759 MW;  BB2A8C7695091994 CRC64;
     MHRRIIAPGA LVAASLLLAI PASAASYAPG APGIGDPYYP SYGNGGYDVS HYDLRLRYQP
     KTDELQGTAT ILARTTEDLS SFDLDFLLDV SEVRVNGAKA SFTTSDQHEL VITPKTPLAK
     GTPVTVVVRY SGVPSKKSAY GFNTWHRTPD GAVAADEPEA AWWWFPSNDH PSDKATYDVS
     VAVPDGTQAI SNGTLQSTGS KLGWTTYNWR QNKPQATYLA TLAVGKFDIT TSTSDGGVPV
     VNAYSKDLGD NDGAARASVE RTGEIVDWLS GYFGPYPFSS AGGYVPNTTT GYALETQTRV
     YYSPKQFANG SNTSVVVHEL AHQWYGDDVS LKGWKDIWIN EGFARYAQWL WSEHEGEGTT
     QELADYVYAS HPSGDAFWTV KPGDPGPDGQ FDLAVYDRGA LAIQALRDEI GDDAFFALLK
     GWPKDHAYGN ASVADFQRYA EQVSGKPLAA LFDTWLFQPS KPAAAAARAA SLTKAGTAVV
     QPKSWKKIEA TNDVHGH
//