DAM_BPT1
ID DAM_BPT1 Reviewed; 238 AA.
AC Q38156;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=DNA N-6-adenine-methyltransferase {ECO:0000303|PubMed:2180941};
DE Short=DAM {ECO:0000305};
DE EC=2.1.1.72 {ECO:0000269|PubMed:3312202};
DE AltName: Full=Orphan methyltransferase M.EcoT1Dam {ECO:0000303|PubMed:12654995};
DE Short=M.EcoT1Dam {ECO:0000303|PubMed:12654995};
GN Name=M.T1 {ECO:0000303|PubMed:3312202};
OS Escherichia phage T1 (Bacteriophage T1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Drexlerviridae; Tunavirinae; Tunavirus.
OX NCBI_TaxID=1921008;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, AND FUNCTION.
RX PubMed=2180941; DOI=10.1016/s0021-9258(19)39295-6;
RA Schneider-Scherzer E., Auer B., de Groot E.J., Schweiger M.;
RT "Primary structure of a DNA (N6-adenine)-methyltransferase from Escherichia
RT coli virus T1. DNA sequence, genomic organization, and comparative
RT analysis.";
RL J. Biol. Chem. 265:6086-6091(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14972552; DOI=10.1016/j.virol.2003.09.020;
RA Roberts M.D., Martin N.L., Kropinski A.M.;
RT "The genome and proteome of coliphage T1.";
RL Virology 318:245-266(2004).
RN [3]
RP FUNCTION.
RX PubMed=376871; DOI=10.1128/jvi.29.3.1229-1231.1979;
RA Wagner E.F., Auer B., Schweiger M.;
RT "Development of Escherichia coli virus T1: escape from host restriction.";
RL J. Virol. 29:1229-1231(1979).
RN [4]
RP IDENTIFICATION, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, INDUCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=3312202; DOI=10.1016/s0021-9258(18)48162-8;
RA Scherzer E., Auer B., Schweiger M.;
RT "Identification, purification, and characterization of Escherichia coli
RT virus T1 DNA methyltransferase.";
RL J. Biol. Chem. 262:15225-15231(1987).
RN [5]
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).
CC -!- FUNCTION: Methyltransferase that methylates adenine residues in the
CC dsDNA sequence 5'-GATC-3' (PubMed:2180941, PubMed:3312202). May prevent
CC degradation of viral DNA by the host restriction-modification antiviral
CC defense system (PubMed:376871). {ECO:0000269|PubMed:2180941,
CC ECO:0000269|PubMed:3312202, ECO:0000269|PubMed:376871}.
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:3312202};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.9 uM for S-adenosylmethionine {ECO:0000269|PubMed:3312202};
CC pH dependence:
CC Optimum pH is 6.9. {ECO:0000269|PubMed:3312202};
CC Temperature dependence:
CC Optimum temperature is between 40 and 43 degrees Celsius.
CC {ECO:0000269|PubMed:3312202};
CC -!- INDUCTION: Expressed early in the viral replication cycle.
CC {ECO:0000269|PubMed:3312202}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87390.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; J05393; AAA87390.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY216660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Proteomes; UP000001156; Genome.
DR GO; GO:0003677; F:DNA 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 InterPro; IPR008593; Dam_MeTrfase.
DR Pfam; PF05869; Dam; 1.
DR TIGRFAMs; TIGR01712; phage_N6A_met; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Host-virus interaction; Methyltransferase;
KW Reference proteome; Restriction-modification system evasion by virus;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..238
FT /note="DNA N-6-adenine-methyltransferase"
FT /id="PRO_0000454836"
SQ SEQUENCE 238 AA; 27122 MW; FF21A20A059A9B8F CRC64;
MKDFNDIETI DFAETGCSFT REAIASGGYY QALKTPTCKE ISGRRYKGTN TPDAVRDLWS
TPREVIAYLE GRYGKYDLDA AASEENKVCE KFYSQETNCL KRWWGKNKHV WLNPPYSRPD
IFVKKAIEQM EHNNQIDMLL PADNSTAWFT EARQNAAEII WIEADLTEDI DGNEYARSGR
LAFISGETGK AVDGNNKGSV IFIMRELKEG EVQQTHYIPI TSICPSVKNK RAKVRKVD
