ID A9IPD0_BART1 Unreviewed; 1451 AA.
AC A9IPD0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=BT_0455 {ECO:0000313|EMBL:CAK00910.1};
OS Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=382640 {ECO:0000313|EMBL:CAK00910.1, ECO:0000313|Proteomes:UP000001592};
RN [1] {ECO:0000313|EMBL:CAK00910.1, ECO:0000313|Proteomes:UP000001592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105476 / IBS 506 {ECO:0000313|Proteomes:UP000001592};
RX PubMed=18037886; DOI=10.1038/ng.2007.38;
RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT "Genomic analysis of Bartonella identifies type IV secretion systems as
RT host adaptability factors.";
RL Nat. Genet. 39:1469-1476(2007).
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};
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DR EMBL; AM260525; CAK00910.1; -; Genomic_DNA.
DR KEGG; btr:BT_0455; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_002151_1_0_5; -.
DR Proteomes; UP000001592; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR041635; Type_ISP_LLaBIII_C.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF18135; Type_ISP_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:CAK00910.1};
KW Helicase {ECO:0000313|EMBL:CAK00910.1};
KW Hydrolase {ECO:0000313|EMBL:CAK00910.1};
KW Nucleotide-binding {ECO:0000313|EMBL:CAK00910.1}.
FT DOMAIN 1..191
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 262..437
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1451 AA; 165417 MW; D8059EC952CD26E1 CRC64;
MACGTGKTFT SLKIAETLAG KGKRVLFLVP SLALVSQTIR EWTADAQVPL RSFAVCSDTK
VGKRRKNQED IVGMETSDLV LPATTDAQTL AKEACENLAD AMTVVFSTYH SIQVISDAQK
EHGLPEFDLI ICDEAHRTTG AVLGTDKRES EFIKVHDNRI IRGKKRLYMT ATPKIFSDKL
KRNAFLSNNV LVSMDNEKLY GKQLYTYSFS RALEDKLLSP CKVIILVVNE KEVSQSIQHL
ITDKNYELIL DDRTKINGCY RALTKMDLKL DLEDDPKPMR RALAFCKDIE TSKRICKEFK
KEKVQESLCA LHKNYKDTPP LNCTLAHIDG TFSAKERTKQ LDWLKEDAGE NTCRALTNVR
CLSEGVDVPA LDAVLFLHPR KSQIEIIQAI GRVMRRAEGK KRGYIILPIG IPADIPPEIA
LENNKKYNVI WQVLNALRAH DDNFNKIIHH MHKKQDVSDT LEIVAASQEL ALEDTTTVID
DLPIRSKLEY SGLNIGLATY ESSHTCEEQG ELSLFSKSED AIRTAIVNRY YDPSYWKKWA
INVGDLAQTH ITRLTEVLTK SETETRQVFN DFMTELRSNL NTTISEQNAI EMLAQHLVTR
PVFNALFEGH KFVQENPVSC ALQRVLNTLD QVTPEESQAL KNISRSVQFY TRGFTTLEAQ
QSLIVELYNE FFRYAFPRTV EKLGIVYTPI EVVDFIIHSV DDVLRNEFGK SLGSRGVSIL
DPFTGTGTFI TRLLQSDLIK PEDMEYKYRY DIHANEIVLL AYYIAAINIE ATYHGLMKGN
YIPFKHIGLT DTFRMIEKQD LMEGILKENS EYLEHQKKLD IKVIFGNPPY STGQKSANDN
AKNTPYPILD NRISETYAAQ SESINMQALY DSYIRAIRWA SDRIKDCGII GFVTNAGFIN
ACSLNGLRKC LVEEFSSLYI FHLRGNQRTS GELSRKEGGK IFGSGSRAPI AISILVKNPN
AQQHGKIYFR DIGDYLNREE KLTIIEKFRS IDGITRSKKG WQIITPDKHG DWLGQRDDSF
NAFLAIGDKK PHSKKLFEIY SCGLKTNRDA WAYNASNETL AKNMSNMITF YNSEVERFNG
VYTHDNGKTR TKTVDNFVNA DESKISWSIN LKKHLTKGKI FEFEDTCLIQ SLYRPFTQQW
LYYNRAFNEM VAQIPCIFPM EQAVENRVIQ ITGTGAMKGF SVLMGKDIPN FDSIEKSQCF
PRYFYESVES LKNEKQTHLF ANSTEKNTTA GLQRRDAITD EGLAHFKAAY PHETITKDDL
FYYVYGILHS EDYRARYADN LSKELPRIPC VKSSDDFWKF VTAGRELGHL HVNYEDVEPY
PVTFKKGNPK LTDISNPEKF YYVTEMKFAG NSKEKDKSTV FYNSNITITD IPLEAYEYIV
NGKPALEWVM GRQCVKTDKK SGIVNDANRY AVETIGNPAY PLELFQRVIT VSLETMKIVK
NLPKLEIRET E
//
