ID A0A3S4SLK6_9ACTO Unreviewed; 890 AA.
AC A0A3S4SLK6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=pepN_1 {ECO:0000313|EMBL:VEG26168.1};
GN ORFNames=NCTC11636_00384 {ECO:0000313|EMBL:VEG26168.1};
OS Actinomyces howellii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=52771 {ECO:0000313|EMBL:VEG26168.1, ECO:0000313|Proteomes:UP000266895};
RN [1] {ECO:0000313|EMBL:VEG26168.1, ECO:0000313|Proteomes:UP000266895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11636 {ECO:0000313|EMBL:VEG26168.1,
RC ECO:0000313|Proteomes:UP000266895};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LR134350; VEG26168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4SLK6; -.
DR KEGG; ahw:NCTC11636_00384; -.
DR Proteomes; UP000266895; Chromosome 1.
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:VEG26168.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:VEG26168.1};
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:UP000266895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 108..211
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 257..471
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 558..879
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 890 AA; 96059 MW; C7ED5C397047B41F CRC64;
MGLTAVPLSH APARASGRGN IGREEAAWRS GVLRLEALEV VVDLCDTRSP GCSVFDVRST
LTLVVEEPGA AGLWVDFVGE HVRETAVDGV IVPVAWDGAR LALPELAPGR HTVDVGARGR
LSNSGQGLNR FVDPVDSATY LYTHFEPSDA RRAWPCLDQP DLKAPFTLTV LHPASWTVLA
NGVVESTRPA DHREGCTVTR MSTTPPLPSY LTALAAGPWH RVTSSWSSPL RPEDPAVELS
WSCRASVARH LDDEPMAITA AGLDLFDRVY GFPYPWGSYD SVLVPEYNLG AMENPGCVTF
NEDTYLLSDR ATRAQRAERA GTILHEMCHM WFGDLVTPRW WEDTWLKESF AEHQGVWAQA
EATAYTEAWV SFASRRKAWA YREDARPSTT HPIVAQVDDV EAARQAFDGI TYAKGAAVLK
QLVAHLGQEV FLTAARRWFT EHAYGNADLT DFIGTLSEAS GRDMSSWAQA WLSTCGPSVI
SDEMTTAEGL LTSLVLTQEG LDPRTGEQVL RPHSLVVGLY SFEGPGGELV RTHRLPVSLT
GPRAEVPGAA GLPVPDLVTV NDEDHTYAVV RPDPASLATA RRALHRLTDP LTRSLWWSCL
DTLVRDAIMA PGDFVETVLE RATDSSETAT LTTVLDQALT AAVRLSEGQE RARLLGDLTG
TRGPEGQGAW GLLMAAAPGS DAQLVRARAW IRAAGEGLVL DPAARASCAS RLRLLADGGL
EGLVADNDLR WRVLAALACL GEVTDAELDD QRRTDPSSTG AVRHLRAVSS LPSADLKAEV
LERLLTDATL SKDQVAALVV GFAVDSHREL TAGSTGTYLG ALEELWASRP QESATRLAVG
LFPAAGEAGD LAAVETWLAD HPHAPAALRR LVLKGRDDLV QVLRVRAAAH
//
