ID A0A1B1M9Y6_STRLN Unreviewed; 859 AA.
AC A0A1B1M9Y6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 Name=pepN {ECO:0000313|EMBL:QMV07048.1};
GN ORFNames=GJU35_16085 {ECO:0000313|EMBL:QMV07048.1}, SLCG_5360
GN {ECO:0000313|EMBL:AXG56515.1}, SLINC_3053
GN {ECO:0000313|EMBL:ANS65277.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS65277.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS65277.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS65277.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG56515.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG56515.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV07048.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV07048.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
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; CP016438; ANS65277.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG56515.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV07048.1; -; Genomic_DNA.
DR RefSeq; WP_067432739.1; NZ_CP046024.1.
DR AlphaFoldDB; A0A1B1M9Y6; -.
DR STRING; 1915.SLINC_3053; -.
DR KEGG; sls:SLINC_3053; -.
DR PATRIC; fig|1915.4.peg.3357; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; 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:ANS65277.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:QMV07048.1};
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:UP000092598};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 117..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 242..452
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 535..845
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 859 AA; 95055 MW; 8DAF1E78574F479A CRC64;
MPGENLSRDE ARERAALLSV DSYDVSLDVR SAVGDDTGDG PRTFRSVTTI RFRCAEPGAT
SFADLIAPGV TAVSLNGKDL DPSEVFDGSR IALEDLAAEN ELVVDARCAY SRTGEGLHRF
VDPEDGEVYL YTQYEPADSR RVFANFEQPD LKAPFRFEVR APEGWTVWSN GVGAESDGVW
RFAETKPIST YITCVVAGPY HYVTDSYERE FKDGTRLEIP LGALCRKGLA PHFDADDVFL
VTKQGLDFFH DHFDYPYPFG KYDQAFVPEY NLGAMENPGL VTFREEFIFR GKVTQASYEG
RANVILHEMA HMWFGDLVTM RWWDDLWLKE SFADFMGAFA LVGATRFEDG WITFANRRKA
WAYRADQLPS THPVTADIRD LQDAKLNFDG ITYAKGASVL KQLVAYVGQD AFLEGARRYF
KRHAYGNTRL GDLLSVLEET SGRDMGTWAR AWLQTAGVNS LTPQVLLDAE GRVDELAVVQ
EAAESHPELR PHRVAVGLYR RTPEGALERY ARAEADVEGP RTVVAELAGA EAPELVLVND
DDLTYCKIRF DANSLETLKA GLGDLTDPLA RALCWSALWN MTRDALLPAR DFVDLVLRFA
GRESGIGVLQ MLHAWANAAL VNYLAPEYRQ TGGRLLAEGA LRELRAAEPG SEHQLAWARF
FASTAALPDD LELLKGLLAG TEQIDGLVVD QELRWVFLEP LAAHGAADEK ALAAELARDD
TASGKRHQVR CLAARPSAAV KAQAWAQLVE SDALSNALVE ATIAGFDRSS QRELLAPYAE
KYFAVIERVW RERSIQIAMH VVQGLFPSLQ QSPATLDAAD AWLAAHEDAA PALRRLVLEG
RDDLARALRG QACDAESAA
//
