ID A0A255EGS8_9ACTN Unreviewed; 876 AA.
AC A0A255EGS8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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 {ECO:0000313|EMBL:OYN88632.1};
GN ORFNames=CGZ91_13580 {ECO:0000313|EMBL:OYN88632.1};
OS Parenemella sanctibonifatiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Parenemella.
OX NCBI_TaxID=2016505 {ECO:0000313|EMBL:OYN88632.1, ECO:0000313|Proteomes:UP000216300};
RN [1] {ECO:0000313|EMBL:OYN88632.1, ECO:0000313|Proteomes:UP000216300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 150081 {ECO:0000313|EMBL:OYN88632.1,
RC ECO:0000313|Proteomes:UP000216300};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-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:OYN88632.1}.
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DR EMBL; NMVJ01000011; OYN88632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255EGS8; -.
DR OrthoDB; 3885507at2; -.
DR Proteomes; UP000216300; 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:OYN88632.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000216300};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 67..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 246..459
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 555..862
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 876 AA; 96183 MW; 0C201DAF57245BEC CRC64;
MNPSNVTREK ARQRSDAVEL NEYAVELDLS QAADPAQTHF PTTSWLQLVT SEPTVEIDFI
GGDGGGLTGV SVDGELHERH YDGARLTLHD IPVGRPVVIE IRGRAAYSRT GQGLHRFVDP
TDGETYLYTH FEPADARRMY ANLEQPDLKA PFRLSVIAPS QWQVTSNQAA EATIDLGDET
RHEFGPTPEL STYLTALAAG PYHHVHRTWQ RAATTGTDEA ADHLSIEVGL WCRQSLAEHL
DPEELFEITF AGLDFFHDNF GYPYPWGKYD QVFVPEYNIG AMENPGCVTF TERYIFSSPA
TQAQRQGRAN TILHEMAHMW FGDLVTPQWW DDLWLKESFA DYMGTHASAA ATRFTDAWVP
FAGGRKLWAY VQDSLPTTHP IVADIPDLEA ARQNFDGITY AKGASVLKQL VRFVGTEEFF
AGARDYFQRY AFGSTTLPDL LDSLSRASGR DLSQWATRWL ETAGPDVLTP VVTEAASAQR
SGTIEELVIE QQSVDPTTGA WVGRPHRLQV GLYRSGADGL VRTELIETEL AAGEPTEGVR
RHPVAEAAGL PVPDLVLVND DDWTYALVRL DDRGRETVLA QLSRLGDPMA RAVIWSSLWT
AVREAELPAA RFVQAVAEHG PAETDISLLT TITRNAGTAV RRYVPAGRRS EVADGLYAAA
QAQIAGAQPG SDGWLVWHRV AGALLPLLTE LPADAVAQVP AEGGDDLRWL YWSGLAAAGD
ATPEQLDAEL ARKDTFDNRV NHLGALSARP TPEVKADVWQ RVHQPGAYSN DEVDAMIGGF
NAPAHSGLVA RYAVDYIQGL EQTWADHPME IAERLAAGLF PRPDHEPGTD PADHPVVGAT
QEWLELHPDA PGALRRIVTE ETAELQRALT AQAAGE
//
