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Database: UniProt
Entry: A0A1B1MKG5_STRLN
LinkDB: A0A1B1MKG5_STRLN
Original site: A0A1B1MKG5_STRLN 
ID   A0A1B1MKG5_STRLN        Unreviewed;       161 AA.
AC   A0A1B1MKG5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
DE            EC=2.1.1.63 {ECO:0000256|HAMAP-Rule:MF_00772};
DE   AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
DE            Short=MGMT {ECO:0000256|HAMAP-Rule:MF_00772};
DE   AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
GN   ORFNames=GJU35_35725 {ECO:0000313|EMBL:QMV10491.1}, SLCG_1747
GN   {ECO:0000313|EMBL:AXG52902.1}, SLINC_6668
GN   {ECO:0000313|EMBL:ANS68892.1};
OS   Streptomyces lincolnensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS68892.1, ECO:0000313|Proteomes:UP000092598};
RN   [1] {ECO:0000313|EMBL:ANS68892.1, ECO:0000313|Proteomes:UP000092598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS68892.1,
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:AXG52902.1, ECO:0000313|Proteomes:UP000253884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC-G {ECO:0000313|EMBL:AXG52902.1,
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:QMV10491.1, ECO:0000313|Proteomes:UP000515335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B48 {ECO:0000313|EMBL:QMV10491.1,
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   -!- FUNCTION: Involved in the cellular defense against the biological
CC       effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in
CC       DNA. Repairs the methylated nucleobase in DNA by stoichiometrically
CC       transferring the methyl group to a cysteine residue in the enzyme. This
CC       is a suicide reaction: the enzyme is irreversibly inactivated.
CC       {ECO:0000256|HAMAP-Rule:MF_00772}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a
CC         thymidine in DNA + S-methyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC         Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387;
CC         EC=2.1.1.63; Evidence={ECO:0000256|HAMAP-Rule:MF_00772};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein]
CC         = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC         Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00772};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00772}.
CC   -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and therefore is
CC       not strictly catalytic. According to one definition, an enzyme is a
CC       biocatalyst that acts repeatedly and over many reaction cycles.
CC       {ECO:0000256|HAMAP-Rule:MF_00772}.
CC   -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000256|HAMAP-
CC       Rule:MF_00772}.
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DR   EMBL; CP016438; ANS68892.1; -; Genomic_DNA.
DR   EMBL; CP022744; AXG52902.1; -; Genomic_DNA.
DR   EMBL; CP046024; QMV10491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B1MKG5; -.
DR   STRING; 1915.SLINC_6668; -.
DR   KEGG; sls:SLINC_6668; -.
DR   PATRIC; fig|1915.4.peg.7359; -.
DR   OMA; ILRPCHR; -.
DR   OrthoDB; 9802228at2; -.
DR   Proteomes; UP000092598; Chromosome.
DR   Proteomes; UP000253884; Chromosome.
DR   Proteomes; UP000515335; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd06445; ATase; 1.
DR   Gene3D; 3.30.160.70; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_00772; OGT; 1.
DR   InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR   InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR   InterPro; IPR008332; MethylG_MeTrfase_N.
DR   InterPro; IPR023546; MGMT.
DR   InterPro; IPR036631; MGMT_N_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00589; ogt; 1.
DR   PANTHER; PTHR10815; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10815:SF5; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF02870; Methyltransf_1N; 1.
DR   SUPFAM; SSF53155; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR   SUPFAM; SSF46767; Methylated DNA-protein cysteine methyltransferase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00772};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00772};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00772};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772,
KW   ECO:0000313|EMBL:ANS68892.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092598};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00772, ECO:0000313|EMBL:ANS68892.1}.
FT   DOMAIN          3..73
FT                   /note="Methylguanine DNA methyltransferase ribonuclease-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF02870"
FT   DOMAIN          79..160
FT                   /note="Methylated-DNA-[protein]-cysteine S-
FT                   methyltransferase DNA binding"
FT                   /evidence="ECO:0000259|Pfam:PF01035"
FT   ACT_SITE        131
FT                   /note="Nucleophile; methyl group acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00772"
SQ   SEQUENCE   161 AA;  17258 MW;  2C4EACD934BD9AAC CRC64;
     MMTMRWTHLD SPVGRLLLTA DDEGALTSLS VPEQKNGRTV QEGWRHDPGP FRAAEEQLAA
     YFAGELKDFD LELSSAGSEF RERVWTALDT VPYGATTSYG EIAARIGAPR AAVRAVGGAI
     GANPLLILRP CHRVIGANGA LTGYAGGLER KTHLLTLEGV L
//
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