ID   A0A1E3SYY5_9MYCO        Unreviewed;       440 AA.
AC   A0A1E3SYY5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=BHQ21_09380 {ECO:0000313|EMBL:ODR07315.1};
OS   Mycobacterium sherrisii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=243061 {ECO:0000313|EMBL:ODR07315.1, ECO:0000313|Proteomes:UP000094224};
RN   [1] {ECO:0000313|Proteomes:UP000094224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC1_M4 {ECO:0000313|Proteomes:UP000094224};
RA   Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL   Submitted (SEP-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}.
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:ODR07315.1}.
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DR   EMBL; MIHC01000013; ODR07315.1; -; Genomic_DNA.
DR   RefSeq; WP_069400080.1; NZ_MIHC01000013.1.
DR   AlphaFoldDB; A0A1E3SYY5; -.
DR   STRING; 243061.AWC25_08465; -.
DR   Proteomes; UP000094224; 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; 1.10.390.10; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094224};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          29..201
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          289..433
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  48754 MW;  46E5CF3A3ABEA8B2 CRC64;
     MKASANKAAP PEVLDEYLPK NGDPGYQVSR YELDLDYRVA LNRLSGVATI TAVALTELRQ
     LTLDLSNALT VSKVSVNGKR VDQFSCRAGK LRIRLGSTVP IGAALSIVVH YGGSPRPIRS
     LWGNVGFEEL TEGALVAGQP NGAASWFPCN DHPSAKAAFH IQVSTESRYR VIANGELLSR
     RARASRTVWT YEQREPTSTY LITLQIGSYE MHRLTRTPVA ITAALPARLR GNFDHDFARQ
     PEMMRLFIEL FGPYPLGSGY TVVVTDDVLE IPVEAQGISI FGANHCDGTR ASERLIAHEL
     AHQWFGNSVT AGQWRDIWLH EGFACYAEWL WSEHSGGPDA DELAAAHHAQ LRAQPQDLLL
     ADPGARDMFD DRVYKRGALT LHALRRHLGD DNFVALLNDW TTRHRHSTAV TGDFTGLAAN
     YASDSLRPLW DQWLYATKVP
//