ID   Q6A7A1_CUTAK            Unreviewed;       864 AA.
AC   Q6A7A1;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE   AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE   AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN   OrderedLocusNames=PPA1627 {ECO:0000313|EMBL:AAT83364.1};
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT83364.1, ECO:0000313|Proteomes:UP000000603};
RN   [1] {ECO:0000313|EMBL:AAT83364.1, ECO:0000313|Proteomes:UP000000603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT83364.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6A7A1; -.
DR   MEROPS; M01.009; -.
DR   EnsemblBacteria; AAT83364; AAT83364; PPA1627.
DR   KEGG; pac:PPA1627; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_007335_1_1_11; -.
DR   Proteomes; UP000000603; 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; cd09602; M1_APN; 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; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR012778; Pept_M1_aminopeptidase.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR   PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 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   Aminopeptidase {ECO:0000313|EMBL:AAT83364.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAT83364.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          108..198
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          242..456
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          538..854
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   REGION          728..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   864 AA;  96136 MW;  C7375E6EA6906D53 CRC64;
     MSSVNITREE AQQRSQVITA HSSKVLVDLS GRDPNGDPLG EPTETFVSSS TIQFSSTGGQ
     SHLDLIADGV YAADLDGTPL DPAAFSHNRF PFTTEPGTHE ITVTALCRYS HSGEGLHRFV
     DPADGKVYLY TQFEIADARR MYADFEQPDQ KMTFELQVIA PTGWTIVSNS PAPEPTEGPW
     EGMSRWSFEP TLPISTYLTA LVAGEYHVDH GTIHTASGEI DADILCRQSI TEYLDADRIR
     TTTQRGFEVY EAEFGYPYPF GKYTQSFVPE FNAGAMENAA CITHRDDLLF RSRVTSAAYE
     NRDNTILHEL AHMWFGDLVT MKWWDDLWLN ESFAEWASHY CQEKIVEKHG GIDPWVSFAN
     QRKTWGYTQD QLPTTHPIAA DMIDLDTVEQ NFDGITYAKG ASTLKQLVAF VGEDKFLAGV
     RTYFAQNAFS NTELKDLLHQ LQVASGRDLS SFTEQWLRTP GVNTVRPDYD VDEKGNFTRF
     DIVQTATEKY PTLRTHRLGV GIYTLTDDHL TRTELLDVDI HDERTPIAAL VGHSRGDLVL
     LNDSDLTYAK VRLDDHSMAT LIDRIDALSD PLARALCWSS AWDMCRDAEM RAQDYVTLVG
     KGLPSETDLT AVTALIRQAT TAAISYSNAE DRQEVRDRLV AILATGLRDA MPGSDHQVAY
     ANGLATAATT DAADLLKGWL SGEEVPEGLS IDQGMRWRLV TALARVGRVG EDEIAAELQR
     DNTISGSEQA AGARAAMPTA QAKQAAWQRA TTDDSVPNET YRQLVMQFIQ PDQTEVLSPY
     VDPYLELCKA IDSHEGQWAK AGHAQVQNAL MWLFPSTEVI DAAWLNKLEG WVSDNDPGST
     VRRVLAERAD NARRILRCQE ASRG
//