ID A0A444PVT7_9MICO Unreviewed; 848 AA.
AC A0A444PVT7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:RWZ51911.1};
GN ORFNames=ELQ90_07465 {ECO:0000313|EMBL:RWZ51911.1};
OS Labedella phragmitis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Labedella.
OX NCBI_TaxID=2498849 {ECO:0000313|EMBL:RWZ51911.1, ECO:0000313|Proteomes:UP000288547};
RN [1] {ECO:0000313|EMBL:RWZ51911.1, ECO:0000313|Proteomes:UP000288547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11W25H-1 {ECO:0000313|EMBL:RWZ51911.1,
RC ECO:0000313|Proteomes:UP000288547};
RA Li F.;
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}.
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:RWZ51911.1}.
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DR EMBL; RZNB01000002; RWZ51911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444PVT7; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000288547; 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:RWZ51911.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RWZ51911.1};
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 21..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 527..838
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 848 AA; 92897 MW; CD5074043254E6F1 CRC64;
MPGENLTRAE AIERAAIVST SSYDVTLDLT TGPETFLSTT TVRFTATPGA STFIDAITAA
VRSVTLNGRE LDPAVVSDGV RIQLDDLAAE NELTIVADAR YTNTGEGLHR FVDPVDDEVY
LYSQFEVPDS RRMFAVFEQP DLKATFAFTV TAPSYWSVVS NSPTPEPVEV RDGVSTWSFS
PTPVLSSYVT ALVAGPYVST HSELTSSDGR TIPLGIYARK SLSEFVDSDY IFEKTRQGFA
FFENAFGLAY PFEKYDQLFV PEFNAGAMEN AGAITFTETY VFRSKVTDAV KERRVVTILH
ELAHMWFGDL VTMKWWNDLW LNESFAEYAS TLAVAEATEW TEAWTTFTAM EKSWAYKQDQ
LPSTHPIVAE IRDLEDVQVN FDGITYAKGA SVLKQLVAWV GQEDFLAGVS AYFAKHAFGN
TELTDLLDEL ERTSGRELRS WSKLWLETAG VNTLRAAIET DDDGVIASFV VEQSAPADYP
TIRPHRLAIG FYSLEGSSLV RTHRVEIDID GPASPVPELI GLTRPDLVLL NDDDLAYAKI
RLDETSLATA IAHLSDIESP LARSLVWGSA WDATRDAETP ASDYVALVLG NIASETESTT
IRTTLNQLLL AVSAYVAPEK RDAVNATAAA ALWELAKNAD AGSDAQFQFV KFFAALASSD
EHLDIIETLR DRSETLEGLD IDTDLGWELL IALAAGGRAD ESVIDAELAA DNTATGQQSA
AHARAAIPTA EGKAAAWSSV FDSDRLPNTI VRSTGLGFQR ATDTDVLRPF VERYFSALEG
IWETRSYKIA EYLVAGMYPS ALADRELADA TRAWLDANPE QPAALRRLVL ENLAGVERAI
AAQERDAS
//
