ID A0A2X4U006_9NOCA Unreviewed; 449 AA.
AC A0A2X4U006;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN_3 {ECO:0000313|EMBL:SQI32513.1};
GN ORFNames=NCTC10994_02222 {ECO:0000313|EMBL:SQI32513.1};
OS Rhodococcus coprophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI32513.1, ECO:0000313|Proteomes:UP000249091};
RN [1] {ECO:0000313|EMBL:SQI32513.1, ECO:0000313|Proteomes:UP000249091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI32513.1,
RC ECO:0000313|Proteomes:UP000249091};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; LS483468; SQI32513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X4U006; -.
DR STRING; 1219011.GCA_001895045_03314; -.
DR KEGG; rcr:NCTC10994_02222; -.
DR Proteomes; UP000249091; Chromosome 1.
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 Aminopeptidase {ECO:0000313|EMBL:SQI32513.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SQI32513.1};
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:UP000249091};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 36..206
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 245..437
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 50180 MW; F802B23A4F6B517E CRC64;
MKPIKAAKPV PPVAADRPLD PYLPTSGNRG YRVSRYELEL GYRVMANRLE GRAVIIATTT
DVRGKFALDL AASMRVSKVT VNGRRPAKYV HRNGKLTVTP ADVIPAGAVL TISVQYAGTP
TPLRTMWGEV GWEELEEGSL VASQPNGAPS WFPCDDHPGS KATYRISITT DAPFQAIANG
TLVHRTTKSS RTTWVYEQPE PMATYLATVQ IGHYEIRQIA SSPVPQYAVH PPRLRDAFDK
DFGRQAEMLE LFTRLFGPYP FAHYTALVTD DDLEIPIEAQ GLSTFGANFC DGHRTEERLV
AHELAHQWFG NSLTLSRWCD IWLHEGFACY AEWLWSENSG GPSAQALAAD AYRGLSRKPQ
DILLENPGAK DMFDDRIYKR GALTLHALRL ALGDDSFFTL LRTWTSEHRH SNVTTTQFKD
LAARFSDTSL RPLWDAWLGQ RELPAPPRI
//
