ID T5D9F2_HELPX Unreviewed; 593 AA.
AC T5D9F2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=N407_00525 {ECO:0000313|EMBL:EQL70302.1};
OS Helicobacter pylori FD662.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191284 {ECO:0000313|EMBL:EQL70302.1, ECO:0000313|Proteomes:UP000015970};
RN [1] {ECO:0000313|EMBL:EQL70302.1, ECO:0000313|Proteomes:UP000015970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD662 {ECO:0000313|EMBL:EQL70302.1,
RC ECO:0000313|Proteomes:UP000015970};
RX PubMed=23012278; DOI=10.1128/JB.01278-12;
RA Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT cultured from patients with functional dyspepsia and gastric cancer.";
RL J. Bacteriol. 194:5695-5696(2012).
RN [2] {ECO:0000313|EMBL:EQL70302.1, ECO:0000313|Proteomes:UP000015970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD662 {ECO:0000313|EMBL:EQL70302.1,
RC ECO:0000313|Proteomes:UP000015970};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(2013).
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:0000256|ARBA:ARBA00001279};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQL70302.1}.
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DR EMBL; AKHT02000012; EQL70302.1; -; Genomic_DNA.
DR AlphaFoldDB; T5D9F2; -.
DR PATRIC; fig|1191284.5.peg.1124; -.
DR Proteomes; UP000015970; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..230
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 421..451
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 482..512
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 593 AA; 68374 MW; 25D65660A7FECAF5 CRC64;
MNMILHHSAD AEIAKGGFST LSNPLFINEE TGMLKTFDYV VANPPFSLKN WTDGLSIDYK
SKQVINDRFN RFEDGTPPEK NGDFAFLLHI IKSLKDTGKG AVILPHGVLF RGNAESAIRK
NLLTKGYIKS VIGLAPNLFY GTSIPACVVV LDKENARARK GVFLIDASKD FKKDGNKNRL
REQDVQKMID TFNALKEIPY YSKMVSLEEI SANDYNLNIA RYISAKQESE KDLFALINSH
KASYLPKNEI ETHDPYFQVF KELKNTLFKK SDKEGYYALK TECQNIKDLI TQSQEFQAFH
ASVLNAFERL ELLETFDHLE PGFNPKTLIE SVCSKVLKEF EKGEILDKYG VYQLFKDYYN
EVLQDDWFLL SFNGFLSAKE LRKLNPLKDK NKKANYLEEP DFVIQKTYYK SDLIPKNLIK
QRFFKKEAKE LEELENALNE KEANFEEFIE EHSNEEGLFD ESKINESVLK KELKNATDSE
DKKILKTALE LLEAKNKALK MKNKAHEELE SKAFHQYKNL KLSEIKDLII QDKWLKSLKN
ALENKIFKRI NAFSSALNEI ISNYSNSLLE IDKEVKESEL KVLEHLKDLG LMG
//