MTB1_BACP9
ID MTB1_BACP9 Reviewed; 445 AA.
AC P0DW08;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 1.
DT 03-AUG-2022, entry version 1.
DE RecName: Full=Type II methyltransferase M.Bpa9945I {ECO:0000303|PubMed:12654995};
DE Short=M.Bpa9945I {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37 {ECO:0000255|PROSITE-ProRule:PRU01016, ECO:0000269|PubMed:29085076};
DE AltName: Full=DISARM protein DrmMII {ECO:0000303|PubMed:29085076};
GN Name=drmMII {ECO:0000303|PubMed:29085076};
GN OrderedLocusNames=BaLi_c08350 {ECO:0000312|EMBL:AGN35230.1};
OS Bacillus paralicheniformis (strain ATCC 9945a / NCIMB 11709 / CD-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=766760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9945a / NCIMB 11709 / CD-2;
RX PubMed=23908277; DOI=10.1128/genomea.00525-13;
RA Rachinger M., Volland S., Meinhardt F., Daniel R., Liesegang H.;
RT "First Insights into the Completely Annotated Genome Sequence of Bacillus
RT licheniformis Strain 9945A.";
RL Genome Announc. 1:0-0(2013).
RN [2]
RP NOMENCLATURE.
RC STRAIN=ATCC 9945a / NCIMB 11709 / CD-2;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND EXPRESSION IN
RP B.SUBTILIS.
RC STRAIN=ATCC 9945a / NCIMB 11709 / CD-2;
RX PubMed=29085076; DOI=10.1038/s41564-017-0051-0;
RA Ofir G., Melamed S., Sberro H., Mukamel Z., Silverman S., Yaakov G.,
RA Doron S., Sorek R.;
RT "DISARM is a widespread bacterial defence system with broad anti-phage
RT activities.";
RL Nat. Microbiol. 3:90-98(2018).
CC -!- FUNCTION: Component of antiviral defense system DISARM (defense island
CC system associated with restriction-modification), composed of DrmE,
CC DrmA, DrmB, DrmC and DrmMII. DISARM is probably a multi-gene
CC restriction module, this subunit is a DNA methylase. Expression of
CC DISARM in B.subtilis (strain BEST7003) confers resistance to phages Nf,
CC phi29, phi105, phi3T, SPO1, SPR and SPP1. Protection is over 10(7)-fold
CC against phi3T, 10(4)-10(5)-fold against Nf, phi29, phi105 and SPR, 100-
CC fold against SPO1 and 10-fold against SPP1. DISARM does not interfere
CC with phage adsorption, but instead interferes with (phi3T) DNA
CC replication early in its cycle, preventing replication, circularization
CC and lysogeny and probably causes phage DNA degradation (DNA is degraded
CC in SPP1-infected cells). Expression of this methylase alone leads to
CC highly methylated phage, however they are still susceptible to the
CC DISARM system. {ECO:0000269|PubMed:29085076}.
CC -!- FUNCTION: A methylase, recognizes the double-stranded sequence 5'-
CC CCWGG-3', methylates C-2 on both strands. Phage Nf does not have any
CC 5'-CCWGG-3' motifs but is still targeted by the DISARM system.
CC {ECO:0000269|PubMed:29085076}.
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:0000269|PubMed:29085076};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13682;
CC Evidence={ECO:0000269|PubMed:29085076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cannot be deleted in a DISARM-containing strain
CC of B.subtilis. {ECO:0000269|PubMed:29085076}.
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; CP005965; AGN35230.1; -; Genomic_DNA.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..445
FT /note="Type II methyltransferase M.Bpa9945I"
FT /id="PRO_0000456313"
FT DOMAIN 1..444
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 445 AA; 51787 MW; F6432E1302F16245 CRC64;
MIVIDLFSGA GGLSEGFHKH DFKIAAHVEK EYWACETIKT RLFYHFLKAQ NDLELYHEYL
RVSDNYRNIE QSRAFVFQRY PELREKLEME VLNRKFGNPH NDPTATSSTQ MIQLIQNSLQ
YSRATSVDLI IGGPPCQAYS LVGRSRMKDS VGKDSRNYLF QYYKRIVDEF KPKAFVFENV
PGILTAKQGK VYQEIKESFD QIGYTVLSGT SQEDRSNVID FADFGVPQRR KRVILFGFQK
KLNYEYPNFE RHKLSWNSPL TTRDVISDLP VLKPKQGHDL RLFEYDTTQG VDQLSPYELM
MREDSIGFTN HFARPIKERD AEIYQIAIEH ATQGRQIKYN ELPERLKTHK NEKAFLDRFK
VHWWDIIPHT VVAHISKDGH YNIHPDIEQC RSLTVREAAR IQGFPDNYKF EGPRTAQYTQ
VGNAVPPLMS GIIARAVKDV INGHH
