ID F8JRG3_STREN Unreviewed; 476 AA.
AC F8JRG3; G8WSV9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN OrderedLocusNames=SCATT_42940 {ECO:0000313|EMBL:AEW96665.1};
OS Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptantibioticus.
OX NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW96665.1, ECO:0000313|Proteomes:UP000007842};
RN [1] {ECO:0000313|Proteomes:UP000007842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC {ECO:0000313|Proteomes:UP000007842};
RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL Submitted (DEC-2011) 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; CP003219; AEW96665.1; -; Genomic_DNA.
DR RefSeq; WP_014145021.1; NC_017586.1.
DR AlphaFoldDB; F8JRG3; -.
DR STRING; 1003195.SCATT_42940; -.
DR MEROPS; M01.032; -.
DR KEGG; scy:SCATT_42940; -.
DR PATRIC; fig|1003195.11.peg.5747; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_014298_2_0_11; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000007842; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000007842};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..476
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003378933"
FT DOMAIN 64..236
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 321..466
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 476 AA; 52586 MW; C617E145C6810F24 CRC64;
MALSRPARLV ALAVATASAC MVAVGTSPAS AASSVRPGVP TPGAPGIGDS YFPDLGNGGF
DVRHYGLGIS YDPASGRLDG RAAVTSRATQ DLSRFDLDLQ RLTVDKVTVD GRRARFTRRG
DELVITPARP LRRGRTFTTD VTYHGIPQPL GGPIVFGSKY GWMKTKTGVF VACEPNAAST
WFPSSDHPSD KATFDITMDA PKGLTGVSNG RLVSTWTKGD RTWSHWRETR PMATYLATAT
IDRFHVRTGR TPGGIPMYVA IDPDLEASSK VDVYQVTSDA TDYWSKVFGP YPFEETGAIV
DDMPLAGFSL EVQSKPVYSA VRSESTIVHE LAHQWFGDSV SVRRWKDIWL NEGFATYAQW
LWAEHKGTRS AHDSFLAAYN SYPADNPFWK IKVDDPQRDT MFSDAVYDRG AMTLQMLRER
IGDQAFFRLL KVWTSEHRYG NAQTSDFVRT AERVSGKPLG DLFRTWLETP ARPSLG
//
