ID A0A1D3DVB1_9ACTN Unreviewed; 854 AA.
AC A0A1D3DVB1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=J116_019150 {ECO:0000313|EMBL:OEJ96260.1};
OS Streptomyces thermolilacinus SPC6.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1306406 {ECO:0000313|EMBL:OEJ96260.1, ECO:0000313|Proteomes:UP000095329};
RN [1] {ECO:0000313|EMBL:OEJ96260.1, ECO:0000313|Proteomes:UP000095329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPC6 {ECO:0000313|EMBL:OEJ96260.1,
RC ECO:0000313|Proteomes:UP000095329};
RX PubMed=23868127;
RA Chen X., Zhang B., Zhang W., Wu X., Zhang M., Chen T., Liu G., Dyson P.;
RT "Genome Sequence of Streptomyces violaceusniger Strain SPC6, a Halotolerant
RT Streptomycete That Exhibits Rapid Growth and Development.";
RL Genome Announc. 1:0-0(2013).
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:OEJ96260.1}.
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DR EMBL; ASHX02000001; OEJ96260.1; -; Genomic_DNA.
DR RefSeq; WP_023588687.1; NZ_ASHX02000001.1.
DR AlphaFoldDB; A0A1D3DVB1; -.
DR STRING; 1306406.J116_019150; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000095329; 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; 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:OEJ96260.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 43..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 231..446
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 854 AA; 94746 MW; 4C919AFB861B8D85 CRC64;
MPGTNLTREE ARRRAALLTV DAYEIDLDLS GAQEGGTYRS ETSVRFECAE EGAETFIDLV
APAVHEVVLN GRHLDVASVF RESRITLKHL ERGVNELKVV ADCSYTNTGE GLHRFVDPVD
GQAYLYTQFE VPDARRVFAS FEQPDLKATF QFTVKAPAGW KVISNSPTPE PKDDVWVFEP
TPRISTYVTA LIVGPYHAVH STYEGPGGQV VPLGVYCRPS LAEFLDADAI FEVTRQGFDW
FQEKFDYAYP FAKYDQLFVP EFNAGAMENA GAVTIRDQYV FRSKVTDAAY EVRAATILHE
LAHMWFGDLV TMEWWDDLWL NESFATYAEA ACQAYAPGSK WPHSWTTFAN QMKTWAYRQD
QLPSTHPIMA EIRDLDDVLV NFDGITYAKG ASVLKQLVAY VGMDAFFQGV QAYFKRHAFG
NTRLSDLLGA LEETSGRDLR TWSKKWLETA GINILRPVVD TDSTGVITSF AVKQEAPALP
AGAKGEAILR PHRIAVGFYD LDDAGKLVRT ERVELDVDGE LTGVEALVGK RRPAVVLLND
DDLSYAKVRL DEESLRNVVA HLGDFTESLP RALCWASAWD MTRDGELATR AYLDLVLSGV
AKESDIGVVQ SLHRQVKLAL DLYAAPDWRE TGLARWTEAT LEHLRAAEPG SDHQLAWARA
FAATARTDEQ LDLLAALLDG SETVEGLVVD TELRWAFVER LAATGRFGAD EIAAEHERDR
TAAGERHAAT AMAARPTAEA KAEAWASVVE SDTLPNAVQE AVIAGFVQTD QRELLEPYTE
KFFAAVKGVW ESRSHEMAQQ IAVGLYPSLQ VSRATLDRTD AWLESAEPNA ALRRLVSESR
SGVERALKAQ AADR
//
