ID V6K712_STRRC Unreviewed; 857 AA.
AC V6K712;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=M878_29920 {ECO:0000313|EMBL:EST24744.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST24744.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST24744.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST24744.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
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:EST24744.1}.
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DR EMBL; AWQX01000260; EST24744.1; -; Genomic_DNA.
DR RefSeq; WP_023550705.1; NZ_CM002285.1.
DR AlphaFoldDB; V6K712; -.
DR STRING; 1352936.M878_29920; -.
DR MEROPS; M01.009; -.
DR PATRIC; fig|1352936.5.peg.6238; -.
DR HOGENOM; CLU_007335_1_1_11; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000017984; 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; 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:EST24744.1};
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:UP000017984};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 106..188
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 536..845
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 857 AA; 94826 MW; 28BE4930421F34A9 CRC64;
MPGTNLTREE AQQRAELLTV DSYEIDLDLS GAQEGGTYRS VTTVRFDVAR AGAESFIDLV
APTVHEVALN GDALDPAEVF KDSRIALPGL LEGRNELRVV ADCAYTNTGE GLHRFIDPVD
EQAYLYTQFE VPDARRVFAS FEQPDLKATF QFTVTAPEGW TVVSNSPTPE PKDNVWAFEP
TPRISSYITA LIVGPYHSVH SVYEKDGQSV PLGIYCRPSL AEFLDSDAIF EVTRQGFDWF
QEKFDYAYPF AKYDQLFVPE FNAGAMENAG AVTIRDQYVF RSKVTDAAYE VRAETILHEL
AHMWFGDLVT MEWWNDLWLN ESFATYTSIA CQAAAPGSRW PHSWTTFANS MKTWAYRQDQ
LPSTHPIMAD IRDLDDVLVN FDGITYAKGA SVLKQLVAYV GEDEFFKGVQ AYFKRHAFGN
TRLSDLLGAL EETSGRDLKT WSKKWLETAG INILRPEIAT DADGVITSFA VRQEAPALPA
GAKGEPVLRP HRIAIGVYDL DAASGKLVRT DRIELDVDGE LTAVPQLNGK RRPAVILLND
DDLSYAKVRL DEQSLAFVTE HLGDFTESLP RALCWASAWD MTRDAELATR AYLSLVLSGI
GKESDIGVVQ SLQRQVKLAI DLYADPAGRE ALLTRWTDAT LAHLRAAQPA SDHQLAWARA
FAATARTPEQ LDLLEGLLEG THTIEGLAVD TELRWAFVER LAAVGRYDEA EISAEYERDK
TAAGERHAAT ARAARPTAEA KAEAWASVVE SDKLPNAVQE AVIGGFVQTD QRELLAPYTD
KYFEAVKGLW DSRSHEIAQQ LAIGLYPSVQ VSEETLTKTD TWLTSAGPNA ALRRLVSESR
AGVERALKAQ AADAATE
//
