YDIR_BACSU
ID YDIR_BACSU Reviewed; 313 AA.
AC O35025;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Type II restriction enzyme BsuMI component YdiR {ECO:0000303|PubMed:12654995};
DE Short=R.BsuM;
DE Short=R.BsuMI;
DE EC=3.1.21.4 {ECO:0000269|PubMed:2830465};
DE AltName: Full=Endonuclease BsuMI component YdiR;
DE AltName: Full=Type-2 restriction enzyme BsuMI component YdiR;
GN Name=ydiR; OrderedLocusNames=BSU06090;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=9455482; DOI=10.1093/dnares/4.5.335;
RA Kasahara Y., Nakai S., Ogasawara N., Yata K., Sadaie Y.;
RT "Sequence analysis of the groESL-cotA region of the Bacillus subtilis
RT genome, containing the restriction/modification system genes.";
RL DNA Res. 4:335-339(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, AND DNA TARGET SEQUENCE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=2830465; DOI=10.1007/bf00338412;
RA Bron S., Janniere L., Ehrlich S.D.;
RT "Restriction and modification in Bacillus subtilis Marburg 168: target
RT sites and effects on plasmid transformation.";
RL Mol. Gen. Genet. 211:186-189(1988).
RN [4]
RP SUBUNIT, DEVELOPMENTAL STAGE, INDUCTION, OPERON STRUCTURE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=11751814; DOI=10.1128/jb.184.2.381-389.2002;
RA Ohshima H., Matsuoka S., Asai K., Sadaie Y.;
RT "Molecular organization of intrinsic restriction and modification genes
RT BsuM of Bacillus subtilis Marburg.";
RL J. Bacteriol. 184:381-389(2002).
RN [5]
RP NOMENCLATURE, AND SUBTYPE.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=32324221; DOI=10.1093/nar/gkaa266;
RA Nye T.M., van Gijtenbeek L.A., Stevens A.G., Schroeder J.W., Randall J.R.,
RA Matthews L.A., Simmons L.A.;
RT "Methyltransferase DnmA is responsible for genome-wide N6-methyladenosine
RT modifications at non-palindromic recognition sites in Bacillus subtilis.";
RL Nucleic Acids Res. 48:5332-5348(2020).
CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC stranded sequence 5'-CTCGAG-3'; the cleavage site is unknown.
CC {ECO:0000269|PubMed:2830465, ECO:0000269|PubMed:32324221,
CC ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC Evidence={ECO:0000269|PubMed:2830465};
CC -!- SUBUNIT: BsuMI restriction activity requires YdiR, YdiS and YdjA.
CC {ECO:0000269|PubMed:11751814}.
CC -!- DEVELOPMENTAL STAGE: Not expressed during sporulation.
CC {ECO:0000269|PubMed:11751814}.
CC -!- INDUCTION: Constitutively expressed during exponential growth. Encoded
CC in an operon with ydiS and ydjA. {ECO:0000269|PubMed:11751814}.
CC -!- DISRUPTION PHENOTYPE: Not essential; its disruption results in
CC increased transformation by plasmid DNA carrying multiple BsuMI target
CC sequences (PubMed:11751814). Triple deletion ydiO-ydiP-ydiS leads to
CC loss of susceptibility to MspJI, which only digests C-methylated DNA
CC (PubMed:32324221). {ECO:0000269|PubMed:11751814,
CC ECO:0000269|PubMed:32324221}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB007637; BAA22753.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12428.1; -; Genomic_DNA.
DR PIR; C69788; C69788.
DR RefSeq; NP_388490.1; NC_000964.3.
DR RefSeq; WP_003244216.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O35025; -.
DR STRING; 224308.BSU06090; -.
DR REBASE; 156235; Bsu16045ORF661P.
DR REBASE; 619; BsuMI.
DR jPOST; O35025; -.
DR PaxDb; O35025; -.
DR PRIDE; O35025; -.
DR EnsemblBacteria; CAB12428; CAB12428; BSU_06090.
DR GeneID; 938002; -.
DR KEGG; bsu:BSU06090; -.
DR PATRIC; fig|224308.179.peg.660; -.
DR BioCyc; BSUB:BSU06090-MON; -.
DR PRO; PR:O35025; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Nuclease; Reference proteome; Restriction system.
FT CHAIN 1..313
FT /note="Type II restriction enzyme BsuMI component YdiR"
FT /id="PRO_0000049509"
FT REGION 289..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 35311 MW; 5825E8C93A8141AE CRC64;
MTFIKRLEDA YETLLGNYPA GVSSTSTSKY NEIRKIVSEA FLIGENEVYV TGTSRRISNL
DTRFAQGNQR NKHTRMAVAF ISIPSVDDSE LDELIIRTRN SAITTSSKFC NGEERGTIFD
GILLFLVFEG ETKVYPLAFL VFENDFELKE KAEELIPGIE LKEYPRANQS PAQENNKSAK
NEDEESAKSY VVFLDIEEDG SIVEFVEDKD KTYRIGDMIW TASHTNGSSA ITRRLEVIEV
VENLVVCKIK HKYNEPVDKN SLLKFVNIEQ DLISFLDLHP NVQNGSEGFV SGDIVDENAT
TSSDDLPEDF ENN
