ID A9I8R5_BORPD Unreviewed; 636 AA.
AC A9I8R5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=DNA (Cytosine-5-)-methyltransferase, putative {ECO:0000313|EMBL:CAP41279.1};
GN OrderedLocusNames=Bpet0947 {ECO:0000313|EMBL:CAP41279.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP41279.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP41279.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000256|ARBA:ARBA00000743};
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DR EMBL; AM902716; CAP41279.1; -; Genomic_DNA.
DR AlphaFoldDB; A9I8R5; -.
DR STRING; 94624.Bpet0947; -.
DR REBASE; 28805; M.Bpe12804ORF947P.
DR KEGG; bpt:Bpet0947; -.
DR eggNOG; COG0270; Bacteria.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 636 AA; 68770 MW; D3F4EFBEF1FA32D6 CRC64;
MITDINHFHL FFGLGGGAAG FQEARPEIPG MQGRMVCIGG MDVDPAGAED FHRFTGVRGT
VRDLFDRSQY LDFHGREPGP GWIEAMPADV RTAANGRRPS IVFLSAPCKG FSGLLSETRS
TTAKYQALNR LTLRGVWLML EAWADDPPEV ILFENVPRIA TRGRHLLDQI TGMLRHYGYV
VRETTHDCGE LGGLAQSRRR FLLIARHAEK VPPFIYEPPK RALRSVGEVL SRYGRPGDPA
MGPMHRIPSL NWKTWVRLAF VEAGKDWRSL NRLAVENGHL RDYLIVPEAH HGFLGVQRWE
TASGTISSRC GPTNGAYSVA DPRQEVYSAG YGVNAWEAPT GAVAGESLPS NGRFSVADPR
AAAGASQYQQ YGVLRMDDTA GAVIGVKSPG QGSFSVADPR HSGPAKHSNE FRIVPFDGQA
RAVTGAHGTG QCVADPLGGR QAADQHGKYP VSAWTEAARA VIAGNANGAY AVADPRPNME
RGRGDNYLTA GHYGVVDPAE PAGAVSASAC HDNGRWSVAD WRLPEATDKL VCVIRALDGT
WHRPFTTLDL AALQSLYDPD DYAEAAEQFV LHGSSDQAWR ERIGNAVPKK AAKAMAEEIG
RAILLARAGE SFQLSSTPIW VRPIATALAV RGGDSA
//
