ID A0A069JXV0_9ACTN Unreviewed; 496 AA.
AC A0A069JXV0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=DT87_22710 {ECO:0000313|EMBL:KDQ69899.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69899.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ69899.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69899.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) 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:KDQ69899.1}.
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DR EMBL; JJOB01000001; KDQ69899.1; -; Genomic_DNA.
DR RefSeq; WP_037879919.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069JXV0; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000027475; 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; 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 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 ECO:0000313|EMBL:KDQ69899.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KDQ69899.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..496
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038784409"
FT DOMAIN 254..460
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 466..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 54799 MW; 3838DE6FD0575552 CRC64;
MPHTSRRLRA ALLVTASAAL VAATLPAPEP LGIGDRLFPH LGNPGYDVLA YDISLTYRGK
NTEPLDAVTT IDARTTHPLE RVNLDFAVGT VEAVEVDGRA AEFATRDEDL VIRPPDRLPA
GVPVRITVRH TSDPSGDPSR GGWVRTADGL AMANQADAAH RVFPGNDHPA DKAYFTFRVT
APNDLTVVAG GLPAGRRRHG DTTTWTYRTA HPMATELAQV SIGRSTVPHR TGPHGLPVRD
VVPSADRDIL EPWLDRTPKH LAWMEEQVGP YPFETYGLLV ADTETGFELE TQTLSLFERS
LFTEPAHPAW YIESVMVHEL AHQWFGDSVS PRVWSDLWLN EGHATWYEAR YAEEHADKPL
EQRMREAYTH SDAWRAAGGP PAHPDAPSPD HKISLFRPVV YDGSALVLYA LRQEIGADAF
DRLERTWVRE HRDRSATTAD FTRLAARIAG RDLTAFFDGW LFGEKTPPMP GHPDWRSAKP
RTTAGPRGAV PAPKPG
//
