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DMA_ECOLI
ID   DMA_ECOLI               Reviewed;         278 AA.
AC   P0AEE8; P00475; Q2M752;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=DNA adenine methylase {ECO:0000303|PubMed:6300769};
DE            EC=2.1.1.72;
DE   AltName: Full=DNA adenine methyltransferase;
DE   AltName: Full=Deoxyadenosyl-methyltransferase;
DE   AltName: Full=Orphan methyltransferase M.EcoKDam {ECO:0000303|PubMed:12654995};
DE            Short=M.EcoKDam {ECO:0000303|PubMed:12654995};
GN   Name=dam {ECO:0000303|PubMed:6300769}; OrderedLocusNames=b3387, JW3350;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=K12 / CS520;
RX   PubMed=6300769; DOI=10.1093/nar/11.3.837;
RA   Brooks J.E., Blumenthal R.M., Gingeras T.R.;
RT   "The isolation and characterization of the Escherichia coli DNA adenine
RT   methylase (dam) gene.";
RL   Nucleic Acids Res. 11:837-851(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7603433; DOI=10.1007/bf00290345;
RA   Lyngstadaas A., Lobner-Olesen A., Boye E.;
RT   "Characterization of three genes in the dam-containing operon of
RT   Escherichia coli.";
RL   Mol. Gen. Genet. 247:546-554(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC   STRAIN=K12;
RX   PubMed=2549371; DOI=10.1007/bf00330946;
RA   Jonczyk P., Hines R., Smith D.W.;
RT   "The Escherichia coli dam gene is expressed as a distal gene of a new
RT   operon.";
RL   Mol. Gen. Genet. 217:85-96(1989).
RN   [6]
RP   MUTAGENESIS, MUTAGENESIS OF PRO-134; GLY-136; ARG-137; LYS-139; ASP-181;
RP   PRO-182 AND PRO-183, AND DNA-BINDING.
RX   PubMed=8341592; DOI=10.1093/nar/21.14.3183;
RA   Guyot J.-B., Grassi J., Hahn U., Guschlbauer W.;
RT   "The role of the preserved sequences of Dam methylase.";
RL   Nucleic Acids Res. 21:3183-3190(1993).
RN   [7]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: An alpha subtype methylase that recognizes the double-
CC       stranded sequence 5'-GATC-3' and methylates A-2 on both strands
CC       (Probable) (PubMed:12654995). Although it shares sequence specificity
CC       with a number of type II restriction endonucleases and methylases, it
CC       is thought to act in methyl-directed mismatch repair, initiation of
CC       chromosome replication and gene expression.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:6300769}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC   -!- INTERACTION:
CC       P0AEE8; P13035: glpD; NbExp=3; IntAct=EBI-548491, EBI-548509;
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; J01600; AAA23664.1; -; Genomic_DNA.
DR   EMBL; V00272; CAA23530.1; -; Genomic_DNA.
DR   EMBL; Z19601; CAA79668.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58184.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76412.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77904.1; -; Genomic_DNA.
DR   EMBL; X15162; CAA33254.1; -; Genomic_DNA.
DR   PIR; A00555; XYECDA.
DR   RefSeq; NP_417846.1; NC_000913.3.
DR   RefSeq; WP_000742143.1; NZ_STEB01000004.1.
DR   PDB; 2G1P; X-ray; 1.89 A; A/B=1-278.
DR   PDB; 2ORE; X-ray; 2.99 A; D/E/F=1-278.
DR   PDB; 4GBE; X-ray; 2.66 A; D/E/F=1-278.
DR   PDB; 4GOL; X-ray; 2.57 A; D/E/F=1-278.
DR   PDB; 4GOM; X-ray; 2.45 A; D/E/F=1-278.
DR   PDB; 4GON; X-ray; 2.72 A; D/E/F=1-278.
DR   PDB; 4GOO; X-ray; 2.70 A; D/E/F=1-278.
DR   PDB; 4RTJ; X-ray; 1.99 A; A=1-278.
DR   PDB; 4RTK; X-ray; 1.96 A; A=1-278.
DR   PDB; 4RTL; X-ray; 2.19 A; A=1-278.
DR   PDB; 4RTM; X-ray; 2.50 A; A=1-278.
DR   PDB; 4RTN; X-ray; 2.59 A; A=1-278.
DR   PDB; 4RTO; X-ray; 2.69 A; A=1-278.
DR   PDB; 4RTP; X-ray; 2.39 A; A=1-278.
DR   PDB; 4RTQ; X-ray; 2.00 A; A=1-278.
DR   PDB; 4RTR; X-ray; 2.39 A; A=1-278.
DR   PDB; 4RTS; X-ray; 2.49 A; A=1-278.
DR   PDBsum; 2G1P; -.
DR   PDBsum; 2ORE; -.
DR   PDBsum; 4GBE; -.
DR   PDBsum; 4GOL; -.
DR   PDBsum; 4GOM; -.
DR   PDBsum; 4GON; -.
DR   PDBsum; 4GOO; -.
DR   PDBsum; 4RTJ; -.
DR   PDBsum; 4RTK; -.
DR   PDBsum; 4RTL; -.
DR   PDBsum; 4RTM; -.
DR   PDBsum; 4RTN; -.
DR   PDBsum; 4RTO; -.
DR   PDBsum; 4RTP; -.
DR   PDBsum; 4RTQ; -.
DR   PDBsum; 4RTR; -.
DR   PDBsum; 4RTS; -.
DR   AlphaFoldDB; P0AEE8; -.
DR   SMR; P0AEE8; -.
DR   BioGRID; 4261860; 125.
DR   DIP; DIP-47948N; -.
DR   IntAct; P0AEE8; 24.
DR   STRING; 511145.b3387; -.
DR   ChEMBL; CHEMBL1075075; -.
DR   REBASE; 13376; M.EcoW3110DamP.
DR   REBASE; 2396; M.EcoKDam.
DR   REBASE; 441639; M.EcoBL21FDamP.
DR   jPOST; P0AEE8; -.
DR   PaxDb; P0AEE8; -.
DR   PRIDE; P0AEE8; -.
DR   EnsemblBacteria; AAC76412; AAC76412; b3387.
DR   EnsemblBacteria; BAE77904; BAE77904; BAE77904.
DR   GeneID; 66672733; -.
DR   GeneID; 947893; -.
DR   KEGG; ecj:JW3350; -.
DR   KEGG; eco:b3387; -.
DR   PATRIC; fig|1411691.4.peg.3343; -.
DR   EchoBASE; EB0200; -.
DR   eggNOG; COG0338; Bacteria.
DR   HOGENOM; CLU_063430_0_1_6; -.
DR   InParanoid; P0AEE8; -.
DR   OMA; MNRHGFN; -.
DR   PhylomeDB; P0AEE8; -.
DR   BioCyc; EcoCyc:EG10204-MON; -.
DR   BioCyc; MetaCyc:EG10204-MON; -.
DR   BRENDA; 2.1.1.72; 2026.
DR   EvolutionaryTrace; P0AEE8; -.
DR   PRO; PR:P0AEE8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:EcoCyc.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IDA:EcoCyc.
DR   GO; GO:1902328; P:bacterial-type DNA replication initiation; IMP:EcoCyc.
DR   GO; GO:0032775; P:DNA methylation on adenine; IMP:EcoCyc.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IMP:EcoliWiki.
DR   GO; GO:0006298; P:mismatch repair; IDA:EcoliWiki.
DR   GO; GO:0009411; P:response to UV; IMP:EcoCyc.
DR   Gene3D; 1.10.1020.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR30481; PTHR30481; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00571; dam; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..278
FT                   /note="DNA adenine methylase"
FT                   /id="PRO_0000087991"
FT   BINDING         10
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         134
FT                   /note="P->S: About 63% methylase activity, binds S-
FT                   adenosyl-methionine (SAM) normally."
FT                   /evidence="ECO:0000269|PubMed:8341592"
FT   MUTAGEN         136
FT                   /note="G->A: About 33% methylase activity, binds SAM
FT                   normally."
FT                   /evidence="ECO:0000269|PubMed:8341592"
FT   MUTAGEN         137
FT                   /note="R->L: No methylase activity, binds SAM normally."
FT                   /evidence="ECO:0000269|PubMed:8341592"
FT   MUTAGEN         139
FT                   /note="K->S,T: 75% methylase activity, binds SAM normally."
FT                   /evidence="ECO:0000269|PubMed:8341592"
FT   MUTAGEN         181
FT                   /note="D->G,N,S: Protein stable, no methylase activity, no
FT                   binding to S-adenosyl-methionine."
FT                   /evidence="ECO:0000269|PubMed:8341592"
FT   MUTAGEN         183
FT                   /note="P->E,G: Low amounts of protein, no methyase
FT                   activity, no binding to S-adenosyl-methionine."
FT                   /evidence="ECO:0000269|PubMed:8341592"
FT   MUTAGEN         183
FT                   /note="P->R: Protein stable, no methylase activity, no
FT                   binding to S-adenosyl-methionine."
FT                   /evidence="ECO:0000269|PubMed:8341592"
FT   TURN            11..13
FT                   /evidence="ECO:0007829|PDB:4GOM"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           18..24
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           57..68
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:4GOM"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           88..100
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           104..117
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           145..154
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   STRAND          158..162
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           165..169
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   STRAND          176..180
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           203..218
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   STRAND          223..228
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   HELIX           231..236
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   TURN            237..239
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   STRAND          240..245
FT                   /evidence="ECO:0007829|PDB:2G1P"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:2G1P"
SQ   SEQUENCE   278 AA;  32100 MW;  B2FA5D1FDC863CB9 CRC64;
     MKKNRAFLKW AGGKYPLLDD IKRHLPKGEC LVEPFVGAGS VFLNTDFSRY ILADINSDLI
     SLYNIVKMRT DEYVQAAREL FVPETNCAEV YYQFREEFNK SQDPFRRAVL FLYLNRYGYN
     GLCRYNLRGE FNVPFGRYKK PYFPEAELYH FAEKAQNAFF YCESYADSMA RADDASVVYC
     DPPYAPLSAT ANFTAYHTNS FTLEQQAHLA EIAEGLVERH IPVLISNHDT MLTREWYQRA
     KLHVVKVRRS ISSNGGTRKK VDELLALYKP GVVSPAKK
 
 
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