DAM_BPP1
ID DAM_BPP1 Reviewed; 754 AA.
AC Q71TL0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA N-6-adenine-methyltransferase {ECO:0000305};
DE Short=DAM {ECO:0000305};
DE EC=2.1.1.72 {ECO:0000269|PubMed:14715260};
DE AltName: Full=EcoP1I DNA MTase {ECO:0000303|PubMed:14715260};
DE Short=M.EcoP1I {ECO:0000303|PubMed:14715260};
DE AltName: Full=Type II methyltransferase M.EphP1ORF2P {ECO:0000303|PubMed:12654995};
DE Short=M.EphP1ORF2P {ECO:0000303|PubMed:12654995};
GN Name=dmt;
OS Escherichia phage P1 (Bacteriophage P1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Punavirus.
OX NCBI_TaxID=2886926;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Mod749::IS5 c1.100 mutant;
RX PubMed=15489417; DOI=10.1128/jb.186.21.7032-7068.2004;
RA Lobocka M.B., Rose D.J., Plunkett G. III, Rusin M., Samojedny A.,
RA Lehnherr H., Yarmolinsky M.B., Blattner F.R.;
RT "Genome of bacteriophage P1.";
RL J. Bacteriol. 186:7032-7068(2004).
RN [2]
RP FUNCTION.
RX PubMed=2236019; DOI=10.1073/pnas.87.20.8070;
RA Sternberg N., Coulby J.;
RT "Cleavage of the bacteriophage P1 packaging site (pac) is regulated by
RT adenine methylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8070-8074(1990).
RN [3]
RP NOMENCLATURE.
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).
RN [4]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14715260; DOI=10.1016/j.bbrc.2003.12.070;
RA Sistla S., Krishnamurthy V., Rao D.N.;
RT "Single-stranded DNA binding and methylation by EcoP1I DNA
RT methyltransferase.";
RL Biochem. Biophys. Res. Commun. 314:159-165(2004).
RN [5]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=21048863; DOI=10.4061/2010/302731;
RA Bheemanaik S., Sistla S., Krishnamurthy V., Arathi S., Desirazu N.R.;
RT "Kinetics of Methylation by EcoP1I DNA Methyltransferase.";
RL Enzyme Res. 2010:302731-302731(2010).
CC -!- FUNCTION: Methyltransferase that methylates adenine residues in the
CC ssDNA and dsDNA sequence 5'-AGACC-3' (PubMed:14715260,
CC PubMed:21048863). Essential for genome packaging because methylation
CC within the pac site makes the latter cleavable (PubMed:2236019). May
CC prevent degradation of viral DNA by the host restriction-modification
CC antiviral defense system (Probable). {ECO:0000269|PubMed:14715260,
CC ECO:0000269|PubMed:21048863, ECO:0000269|PubMed:2236019, ECO:0000305}.
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 Evidence={ECO:0000269|PubMed:14715260, ECO:0000269|PubMed:21048863};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14715260, ECO:0000269|PubMed:21048863};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:21048863};
CC Note=Presence of Mg(2+) enhances the ssDNA binding ability of the
CC enzyme. {ECO:0000269|PubMed:14715260};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.78 uM for ssDNA {ECO:0000269|PubMed:14715260,
CC ECO:0000269|PubMed:21048863};
CC KM=0.68 uM for dsDNA {ECO:0000269|PubMed:14715260,
CC ECO:0000269|PubMed:21048863};
CC KM=0.27 uM for a 31mer duplex DNA {ECO:0000269|PubMed:21048863};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:14715260};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21048863}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; AF234172; AAQ14041.1; -; Genomic_DNA.
DR RefSeq; YP_006537.1; NC_005856.1.
DR SMR; Q71TL0; -.
DR REBASE; 7756; M.EphP1ORF2P.
DR PRIDE; Q71TL0; -.
DR GeneID; 2777403; -.
DR KEGG; vg:2777403; -.
DR Proteomes; UP000008091; Genome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IDA:UniProtKB.
DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1020.10; -; 1.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30481; PTHR30481; 1.
DR Pfam; PF00145; DNA_methylase; 2.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 2.
DR TIGRFAMs; TIGR00571; dam; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 1: Evidence at protein level;
KW Host-virus interaction; Methyltransferase; Reference proteome;
KW Restriction-modification system evasion by virus; S-adenosyl-L-methionine;
KW Transferase; Viral genome packaging; Viral release from host cell.
FT CHAIN 1..754
FT /note="DNA N-6-adenine-methyltransferase"
FT /id="PRO_0000433211"
FT DOMAIN 4..469
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 754 AA; 83628 MW; 4201FA805A3EFBC1 CRC64;
MKELCYGSVC SGIEAASIAW EPLGMRPAWF AEIEPFPSAV LAHRWPHVAN LGDMTKLAKK
VLAGEIESPD VLVWGTPCQA FSIAGLRGGL DDERGALTLK YVELANAIDD KRSESFLKPT
VIVWENVPGV LSSADNAFGC FLAGLAGEDA PFEPGDRPES GKSNAFWRWD GKTGCHAPKW
PQCGCIYGPQ RKVAWRILDA QYFGVAQRRR RVFVVASART DLDPATVLFE FEGVRRNIAP
RRKKKEIASA IIANGAAISG ESLNPCLHAD MPPSMKSTKA VNAFRMAAFG EYIDDETAST
VKARDFKDAT DLAVFSSTGA GFWSEGHGTL RAREQESHEH LVTLAFPERM SGTQHAATKN
TSPSLMAKNP TAVCYEVRNA EVAVRRLTPV ECERLQGFPD GHTLIPTEKR KKVNSDELAY
LRNHYPDLSE EEAAMLAADG PRYKAIGNSM AIPVMRWIGD RITKAVCRQK EGSETKERKV
KPAAEFERSI FKWAGGKFGV LEQIFRYLPE GKRLIEPFVG GGAVFTNAGY QENLLNDVNA
DLINFYKTLQ REAHSLITLA HRFFQDYNTQ EGYLAVRNAF NKQVYDDLHR AAAFLFLNRH
CFNGLTRYNQ AGEFNVGYGK YKTPYFPLQE MEAFLGAEGR SEFVCGDFAA VIEAAGEGDV
IFCDPPYEPL PNTEGFTNYS GHDFKFEEQK RLVSLLTDAH RRGAKVLITN SGAPNIRELY
HDSGFRVEPL FARRSVSCKG DTRGVAHDVL GILL
