ID A0A2A5NQA8_9MICO Unreviewed; 846 AA.
AC A0A2A5NQA8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 {ECO:0000313|EMBL:PCN47511.1};
GN ORFNames=Csp2054_11580 {ECO:0000313|EMBL:PCN47511.1};
OS Curtobacterium sp. 'Ferrero'.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2033654 {ECO:0000313|EMBL:PCN47511.1, ECO:0000313|Proteomes:UP000218649};
RN [1] {ECO:0000313|EMBL:PCN47511.1, ECO:0000313|Proteomes:UP000218649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ferrero {ECO:0000313|EMBL:PCN47511.1,
RC ECO:0000313|Proteomes:UP000218649};
RA Osdaghi E., Forero Serna N., Bolot S., Fischer-Le Saux M., Jacques M.-A.,
RA Portier P., Carrere S., Koebnik R.;
RT "High-Quality Draft Genome Sequence of the Curtobacterium sp. Strain
RT 'Ferrero'.";
RL Submitted (SEP-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}.
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:PCN47511.1}.
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DR EMBL; NXIA01000012; PCN47511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5NQA8; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000218649; 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:PCN47511.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 229..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 527..837
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 846 AA; 93165 MW; B3E7CACDC5073974 CRC64;
MPGENLTRIE AQERAAIVDV QSYDVELDLT RGAETFGSTT RVRFTATAGA STFIDAITKT
VHSVTLNGTA LDVDAVADGV RIQLDGLQEQ NELVVVADAL YTNTGEGLHR FVDPVDDEVY
LYSQFEVPDS RRMFAVFEQP DLKAEFSFTV TAPARWQVVS NAPTPEPHVD GDVATWSFAP
TARISSYITA LIAGPYEVVR DELTSRDGRT IPLGVFARKS LAEYLDPEYV FETTRKGFAY
FEEKFDVPYP FEKYDQLFVP EFNAGAMENA GAVTFTETYV FRSKVTDAIK ERRVVTILHE
LAHMWFGDLV TMKWWNDLWL NESFAEWAST IATAEATEWT EAWTTFQAME KSWAYRQDQL
PSTHPIVATI NDLEDVQVNF DGITYAKGGS VLKQLVAWVG IDAFFAGVSA YFKKHHHSNT
ELRDLLVELE STSGRDLSEW SKLWLETAGV NTLRPEFDVD ADGTITSFAV LQEAPSDYPT
LRPHRLAIGV YAAADGGKLE RTHRVEIDVD GARTDVPELV GVHRGDLVLL NDDDLAYAKI
RLDEQSRQTA IAHLADIANP LARSIVWGAI WDATRDAEAP ASDYVRLVLG NIATETESTT
IRTTLSQLLL TARNYVAPAK AEATIQQVGD ALWTLATEAE AGSDAQFQFV KFFAQIPSTP
EHVATLRGLR DGSVTLDGLE IDTDLRWELL EGLVLAGAAD GSDVDTELAA DRTASGEQAA
ARARAAIPTA EGKLAAFSSL VDSDALPNAI VRQTTVGFQH VNSPVVLEGL VPEYFDVLTR
IWAERSYHMA DTIVTGLYPA PLASAELRDA ARAWLEAHPE TPALRRIVTE NLAGTERALR
VQAADA
//
