ID A0A0C2J694_9ACTN Unreviewed; 848 AA.
AC A0A0C2J694;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=LP52_22140 {ECO:0000313|EMBL:KIH96956.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH96956.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
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:KIH96956.1}.
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DR EMBL; JROO01000045; KIH96956.1; -; Genomic_DNA.
DR RefSeq; WP_040276283.1; NZ_JROO01000045.1.
DR AlphaFoldDB; A0A0C2J694; -.
DR STRING; 183763.LP52_22140; -.
DR MEROPS; M01.009; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000031675; 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:KIH96956.1};
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:UP000031675};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 117..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 231..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 526..835
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 848 AA; 94238 MW; CEFFF83F22DDB646 CRC64;
MAGNLTREEA QERARILSVS SYTVELDLTG SDQTFESRTV VRFDCAEPGA ETFVDLTAPS
VTSVVLNGAE LDPAEVFDGG RIRLRGLQAR NELRVLAEAA FMRTGEGLHR FVDPVDGRTY
LYTQFETADA QRMYACFDQP DLKASFELTV FAPADFEVVS NSAPEVAGEA VEDPAGPKAR
WHFPATEPVS TYITALIAGP YHVVRDEHDG IPLGVYCRAS LAEHLDADAI LEVTKQGFDF
YHGLFGLRYP FGKYDQLFVP EFNAGAMENA GAVTFLEDYV FRSRVTDARY ERRAETILHE
MAHMWFGDLV TMRWWDDLWL NESFATFASV YCQVNATKWT EAWTTFANIE KAWALRQDQL
PSTHPIAADM ADMQAVEVNF DGITYAKGAS VLKQLVAYVG EDAFFAGVRA YFAEHAWGNT
ELSDLLRHLE QASGRDLSTW SREWLETAGV NTMRPEFEVG SDGAFTSFAV RQEAAEEHPT
LRSHRLAVGL YDRTEQGVVR RDRVELDVSG ERTEVPELVG KARPDLVLVN DDDLTFTKIR
LDDLSLRTVV EGAGDIAESL PRALSFGAAW DMTRDAEMAA RDYVRLVASG LSGVSDVMVV
QSLLRQAVTA LHTYTDPAWR DSGFDLLAAR LRDLLTSAEP GGDLQLAYAN GFAEAAVGGE
HLSLLQGLLD GAITVEGLTI DTDLRWTLLR RLVAAGRAGE KEIAAELVLD PTATGERQAA
GCRAAIPTSE AKAQAWDRIR SGEMANAEFR ATLSGFTEPS QRELYRPYVD RYFDLLEQAW
REWTGEFAQT FAEMAYPRHL VEEETVRRTE EYIEKHSPAP ALRRLLVEGQ AGVRRALEAQ
RCDARAAG
//