ID A0A2A3Y0W9_9MICC Unreviewed; 881 AA.
AC A0A2A3Y0W9;
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:PCC29593.1};
GN ORFNames=CIK76_05630 {ECO:0000313|EMBL:PCC29593.1};
OS Glutamicibacter sp. BW80.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=2024404 {ECO:0000313|EMBL:PCC29593.1, ECO:0000313|Proteomes:UP000218725};
RN [1] {ECO:0000313|EMBL:PCC29593.1, ECO:0000313|Proteomes:UP000218725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BW80 {ECO:0000313|EMBL:PCC29593.1,
RC ECO:0000313|Proteomes:UP000218725};
RX PubMed=28644126;
RA Bonham K.S., Wolfe B.E., Dutton R.J.;
RT "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL Elife 6:e22144-e22144(2017).
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:PCC29593.1}.
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DR EMBL; NRGV01000020; PCC29593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3Y0W9; -.
DR Proteomes; UP000218725; 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:PCC29593.1};
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 110..201
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 249..461
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 547..868
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 881 AA; 97149 MW; 554856AF8D05D83C CRC64;
MDTLERYAPN ENLRRDEAAW RAANIGWHFA EVELDLRNAT DAAETSFAAV TTLNFSAASP
ETFIDYIHES IQSIVLNGSE IPVADAVLDA RIYLRGLRTD APNTVRIAGR SSYSRSGEGL
HRFVDPQDGQ TYLYTQFEPS EARRVFACFE QPDLKTSYRF TLTGPEGWHL ASNQQVLDEV
NNGDGSKTVS CAPTAPISSY ITAVLAGPYH VVRGTHLQKL ADGEELSIEM AATCRASLAE
HFDGEEILKL TSQGLEYFHE LFDFPYPWGK YDSAFVPEYN LGAMENPGLV TFTERYVFTS
QATEAQHEQR ANTLMHEMAH MWFGDLVTMK WWDDLWLKES FADYIGTLAN DEATDFTTAW
TTFAARRKAW AYVADQMPTT HPIVADIPDL LAADQNFDGI TYAKGASVLK QLAAFVGAEA
FRDAARAYFR QHAYANTSLE DFLQALEKAS GRDMRGWADA WLKTSGVPKL AAHYTVDESG
LITAAQLEQR GIDPISGEQI IRPHVLSVAA YTLRAGILER TESQRVELLG ASVELDFLVG
QRAPDLLLPN DGDETYALIE FDERSLRTLL EHLGALRDSL PRATCWASLW DAVRQGKLDG
QSYVAAILEH AHTIEDSGVF SVLLDQLATS ISKYVAPELR AALREQAARV LTGWLADFAS
GSDQQTTTAR MLARLARSGV APEIIDAFLA EEPNPYRVTV DEQLRWASYI ALAASGRMDS
AAQARMHEAA KANPTSVAQN SVRTALAARP DAAVKEAAFD TVLMGHDDNG PLSNDALSAI
AQGFAMGSPS LLADCQRRYW AAILPVFETM SMEFATRVIE GLYPGIQDLT GDPAQNPTLL
AANAWLEANQ TAPAALQRIL IEERAELQRS LQAQSFSRIS R
//
