MTBB_BPSPB
ID MTBB_BPSPB Reviewed; 443 AA.
AC P09389; Q77YW9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Orphan methyltransferase M.SPBetaI {ECO:0000303|PubMed:12654995};
DE Short=M.SPBetaI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37 {ECO:0000255|PROSITE-ProRule:PRU01016};
DE AltName: Full=Cytosine-specific methyltransferase SPBetaI;
DE AltName: Full=Modification methylase SPBetaI;
GN Name=mtbP {ECO:0000303|PubMed:9465078};
OS Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Spbetavirus.
OX NCBI_TaxID=66797;
OH NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9465078; DOI=10.1073/pnas.95.4.1692;
RA Lazarevic V., Soldo B., Duesterhoeft A., Hilbert H., Maueel C.,
RA Karamata D.;
RT "Introns and intein coding sequence in the ribonucleotide reductase genes
RT of Bacillus subtilis temperate bacteriophage SPbeta.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1692-1697(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143 AND 476-589.
RX PubMed=3087819; DOI=10.1016/0378-1119(86)90153-8;
RA Tran-Betcke A., Behrens B., Noyer-Weidner M., Trautner T.A.;
RT "DNA methyltransferase genes of Bacillus subtilis phages: comparison of
RT their nucleotide sequences.";
RL Gene 42:89-96(1986).
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).
CC -!- FUNCTION: A methyltransferase that methylates C-1 within the sequences
CC 5'-GGCC-3' and 5'-GCNGC-3' (PubMed:12654995). Modification confers
CC resistance against restriction enzymes that recognize these sequences
CC (Probable). {ECO:0000303|PubMed:12654995, ECO:0000305}.
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:0000255|PROSITE-ProRule:PRU10018};
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; AF020713; AAC13115.1; -; Genomic_DNA.
DR EMBL; M19513; AAA32601.1; -; Genomic_DNA.
DR EMBL; M19514; AAA32602.1; -; Genomic_DNA.
DR RefSeq; NP_046694.1; NC_001884.1.
DR SMR; P09389; -.
DR REBASE; 156252; M.Bsu16045ORF2153P.
DR REBASE; 2833; M.SPBetaI.
DR GeneID; 1261493; -.
DR KEGG; vg:1261493; -.
DR Proteomes; UP000009091; Genome.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 2.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW Host-virus interaction; Methyltransferase; Reference proteome;
KW Restriction-modification system evasion by virus; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..443
FT /note="Orphan methyltransferase M.SPBetaI"
FT /id="PRO_0000087867"
FT DOMAIN 4..440
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 443 AA; 50510 MW; 2BF02005159E9879 CRC64;
MSKLRVMSLF SGIGAFEAAL RNIGVDYELI GFSEIDKYAI KSYCAIHNVS ETLNVGDISK
AKKDNIPYFD LLTSGFPCPT FSVAGGRDGM EYKCSNCSHE HLITYEDYKK GVKCPKCEAV
SKAKDERGTL FFETALLAEE KKPKFVILEN VKGLINSGNG QVLRIISETM NNIGYRIDLE
LLNSKFFNVP QNRERVYIIG IREDLVENEQ WVVGQKRNDV LSKGKKRLQE INIKSFNFKW
PLQDTVTKRL REILEDFVDE KYYLNEEKTK KLVEQLGTAP LQKQEVREPL MVGHVDLKGH
DAIKRVYSPE GLSPTLTTMG GGHREPKIAE KQKEVRAVLT PEREEKRQNG RRFKENGEPA
FTVNTIDRHG VAIGEYPKYK IRKLSPLECW RLQAFDDEDF EKAFAAGISN SQLYKQAGNS
ITVSVLESIF QELIHTYVNK ESE
