ID A0A1R4KET5_9ACTN Unreviewed; 854 AA.
AC A0A1R4KET5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=FM114_13765 {ECO:0000313|EMBL:SJN42797.1};
OS Luteococcus japonicus LSP_Lj1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Luteococcus.
OX NCBI_TaxID=1255658 {ECO:0000313|EMBL:SJN42797.1, ECO:0000313|Proteomes:UP000188342};
RN [1] {ECO:0000313|EMBL:SJN42797.1, ECO:0000313|Proteomes:UP000188342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSP_Lj1 {ECO:0000313|EMBL:SJN42797.1,
RC ECO:0000313|Proteomes:UP000188342};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUKQ01000049; SJN42797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4KET5; -.
DR STRING; 1255658.FM114_13765; -.
DR OrthoDB; 3885507at2; -.
DR Proteomes; UP000188342; 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; 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:SJN42797.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SJN42797.1};
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:UP000188342};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 97..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 238..451
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 536..844
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 854 AA; 93649 MW; 119790805142740A CRC64;
MSTGNISRAE ARVRSTGITV ESYHSTIDVR RATDQSHDTF GVHCVIVLDT SLDSTTLDFL
DAIVHRVVVN GEVQAVDYDG ARFPVQLTPG RNVVEVSAAG RYSRSGQGLH RFLDPVDKQT
YLYTQYEPAD ARRVFPNFEQ PDLKAVHHIT VLAPEGWQVR SNQPRVAGGP IKGDDDQFDG
VRHAFGPTPP LSTYLTCIIA GPWHEQTSSW TSDDGLEVPL GALCRQSLAP HFDAEKIFEV
TRQGMDFYHR AFGFPYPWGK YDQVFVPEYN LGAMENPGLV TFTEAYIHRS TATRAQYQGR
ANTILHEMAH MWFGDLVTPQ WWDDLWLKES FAEFMGAHVS VQATEFTDAW VAFAGRRKAW
AYAQDQLPTT HPIVADIADV EAAKQNFDGI TYAKGAAVLK QLVAHVGVDV FFAGARAYFQ
QHAFSSATLA DLLASLQEAS GRDLDEWAAC WLQTAGPDTL TPVIETADGR ITRLAIRQES
LDARDGTVVG RPHTLVVGLY RVVDGTLRRT DRLEVDLAGG PSTDLPQAVG LASPDLVLVN
DEDLTYAKVV LDPASLETVR AHLSGVDDAL ARALVWAALW NMTRDAVLPA RDYLAIAMDH
ALAETDAATL TDVLARVDSC LNLYLPPEAR EEAAGPVAER IWQELVAARP GSDAQVVLAR
SIARLGLRVD ILSPRITTLL DGSLVLDGLE LGPELRWMFA RALTAQQIWG MAELDEELRR
DPSADGVTAR LEALASRPSA EVKAQVWQDL HTPDALSNDH VDALVSGFGT PGQEELAAPA
AGGYFEGLTE VWQQHSIEIA QRLVGGLFPK TADGREGAQR WLDQTDDVPA ALRRMVVEGA
DDAARIQRVL AFNS
//
