ID   TUBR_BACC1              Reviewed;         119 AA.
AC   Q74P25;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=DNA-binding protein TubR {ECO:0000305};
DE   AltName: Full=Centromere-binding protein {ECO:0000303|PubMed:30414406};
DE   AltName: Full=TubR-Bc {ECO:0000303|PubMed:22847006};
GN   Name=tubR {ECO:0000303|PubMed:22847006}; OrderedLocusNames=BCE_A0069;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OG   Plasmid pBc10987.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248; PLASMID=pBc10987;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RC   STRAIN=ATCC 10987 / NRS 248; PLASMID=pBc10987;
RX   PubMed=22847006; DOI=10.1074/jbc.m112.373803;
RA   Hoshino S., Hayashi I.;
RT   "Filament formation of the FtsZ/tubulin-like protein TubZ from the Bacillus
RT   cereus pXO1 plasmid.";
RL   J. Biol. Chem. 287:32103-32112(2012).
RN   [3] {ECO:0007744|PDB:6AHT}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 5-114 AND 7-119, FUNCTION,
RP   SUBUNIT, PROBABLE OPERON, DISRUPTION PHENOTYPE, MUTAGENESIS OF TYR-72;
RP   GLU-82 AND ARG-94, AND DNA-BINDING.
RC   STRAIN=ATCC 10987 / NRS 248; PLASMID=pBc10987;
RX   PubMed=30414406; DOI=10.1016/j.jmb.2018.11.001;
RA   Hayashi I., Oda T., Sato M., Fuchigami S.;
RT   "Cooperative DNA Binding of the Plasmid Partitioning Protein TubR from the
RT   Bacillus cereus pXO1 Plasmid.";
RL   J. Mol. Biol. 430:5015-5028(2018).
CC   -!- FUNCTION: A DNA-binding protein that is part of the type III plasmid
CC       partition system used to ensure correct segregation of the pBc10987
CC       plasmid (Probable). Binds TubZ filaments but does not influence the
CC       GTPase activity of TubZ with or without DNA (PubMed:22847006).
CC       Cooperatively binds to multiple regions in tubC (centromere-like site)
CC       upstream of its own gene with consensus sequence
CC       N(T/A)ATTNC(C/G)GNAAT(A/T)N; probably forms an extended DNA-protein
CC       filament. Binds sites in its own promoter region and presumably
CC       represses its expression; its effect on RNA expression has not been
CC       shown. Does not specifically bind to the putative origin of replication
CC       on pBc10987 (PubMed:30414406). {ECO:0000269|PubMed:22847006,
CC       ECO:0000269|PubMed:30414406, ECO:0000305|PubMed:22847006}.
CC   -!- SUBUNIT: Homodimer (PubMed:30414406). Binds to TubZ filaments via the
CC       C-terminus of TubZ. DNA is not required for binding to TubZ
CC       (PubMed:22847006). {ECO:0000269|PubMed:22847006,
CC       ECO:0000269|PubMed:30414406}.
CC   -!- INDUCTION: Probably part of the tubR-tubZ operon.
CC       {ECO:0000269|PubMed:30414406}.
CC   -!- DOMAIN: Although this has the same function as TubR of B.thuringiensis
CC       subsp. israelensis there is little sequence homology and the
CC       dimerization interface is different. {ECO:0000269|PubMed:30414406}.
CC   -!- DISRUPTION PHENOTYPE: Increased expression of TubZ.
CC       {ECO:0000269|PubMed:30414406}.
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DR   EMBL; AE017195; AAS44919.1; -; Genomic_DNA.
DR   PDB; 6AHT; X-ray; 2.00 A; A=5-114, B=7-119.
DR   PDBsum; 6AHT; -.
DR   AlphaFoldDB; Q74P25; -.
DR   SMR; Q74P25; -.
DR   EnsemblBacteria; AAS44919; AAS44919; BCE_A0069.
DR   KEGG; bca:BCE_A0069; -.
DR   HOGENOM; CLU_168768_0_0_9; -.
DR   OMA; NESKWFL; -.
DR   Proteomes; UP000002527; Plasmid pBc10987.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Plasmid; Plasmid partition; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..119
FT                   /note="DNA-binding protein TubR"
FT                   /id="PRO_0000448565"
FT   MUTAGEN         72
FT                   /note="Y->A: No DNA binding."
FT                   /evidence="ECO:0000269|PubMed:30414406"
FT   MUTAGEN         82
FT                   /note="E->R: Decreased DNA binding."
FT                   /evidence="ECO:0000269|PubMed:30414406"
FT   MUTAGEN         94
FT                   /note="R->A: No DNA binding."
FT                   /evidence="ECO:0000269|PubMed:30414406"
SQ   SEQUENCE   119 AA;  13759 MW;  14C329E03E6CE54B CRC64;
     MKLLSNISMS SSEIIDVLCE NLNDGIWALR VLYAEGAMNK EKLWDYINQY HKDYQIENEK
     DYEGKKILPS RYALDIMTAR LEGAGLISFK AIGRVRIYDV TDLGNVLIKE LEKRVEKNN