ID A0A2M8WJ73_9MICO Unreviewed; 428 AA.
AC A0A2M8WJ73;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, 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};
GN ORFNames=CLV34_2240 {ECO:0000313|EMBL:PJI90981.1};
OS Luteimicrobium subarcticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Luteimicrobium.
OX NCBI_TaxID=620910 {ECO:0000313|EMBL:PJI90981.1, ECO:0000313|Proteomes:UP000231586};
RN [1] {ECO:0000313|EMBL:PJI90981.1, ECO:0000313|Proteomes:UP000231586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22413 {ECO:0000313|EMBL:PJI90981.1,
RC ECO:0000313|Proteomes:UP000231586};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-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:PJI90981.1}.
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DR EMBL; PGTZ01000009; PJI90981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8WJ73; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000231586; 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; cd09603; M1_APN_like; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 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:UP000231586};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 23..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 234..407
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 428 AA; 47637 MW; 966319F067E3D095 CRC64;
MSVREPALDP YVPHRGSSAY TVDHYDLDLE YKVASNRLDG AATLELRLLE DTDVVELDLV
RLRVEHVTVE RQRAPYKHSG GRVRVRLGRV RRAGTRLTLA VRYSGRPAPA MGTWGDVGWE
ELTDGSLCAN QPDGAPTWFP CNDHPSHRAT FRITVTTEAD YAVVTNGELE HVARKGSTRV
WRFGRTDPMC TYLAAVHVGR YEPLVLASSR VPQVAHAPRA QHHAVAADLV RHDQLMRTFE
DLFGPYPFTS YRLVVTADPL EIPLEAQGMS VFGAQHLDGT GSWDRLVAHE LAHQWFGNSV
SVARWSDIWL NEGFACYAEW LWSEASGGPT ADRLAREAHA RLAALPQDLV VGDPGPENMF
DDRLYKRGAL TLHALRTVLG DDAFFDAVRE WTRSHRHASA STADLRALVG HDALLDAWLL
DPALPALP
//
