ID   TUBR_CBCP               Reviewed;          81 AA.
AC   Q331T6;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   02-JUN-2021, entry version 39.
DE   RecName: Full=DNA-binding protein TubR {ECO:0000305};
DE   AltName: Full=Centromere-binding protein {ECO:0000303|PubMed:29762781};
DE            Short=CBP {ECO:0000303|PubMed:29762781};
GN   Name=tubR {ECO:0000303|PubMed:22538818}; ORFNames=CST190;
OS   Clostridium botulinum C phage (Clostridium botulinum C bacteriophage).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=12336;
OH   NCBI_TaxID=36828; Clostridium botulinum C.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Clostridium phage c-st;
RX   PubMed=16287978; DOI=10.1073/pnas.0505503102;
RA   Sakaguchi Y., Hayashi T., Kurokawa K., Nakayama K., Oshima K., Fujinaga Y.,
RA   Ohnishi M., Ohtsubo E., Hattori M., Oguma K.;
RT   "The genome sequence of Clostridium botulinum type C neurotoxin-converting
RT   phage and the molecular mechanisms of unstable lysogeny.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:17472-17477(2005).
RN   [2]
RP   FUNCTION, SUBUNIT, AND DNA-BINDING.
RC   STRAIN=Clostridium phage c-st;
RX   PubMed=22538818; DOI=10.1073/pnas.1121546109;
RA   Oliva M.A., Martin-Galiano A.J., Sakaguchi Y., Andreu J.M.;
RT   "Tubulin homolog TubZ in a phage-encoded partition system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:7711-7716(2012).
RN   [3]
RP   FUNCTION, SUBUNIT, AND DNA-BINDING.
RC   STRAIN=Clostridium phage c-st;
RX   PubMed=29762781; DOI=10.1093/nar/gky370;
RA   Martin-Garcia B., Martin-Gonzalez A., Carrasco C., Hernandez-Arriaga A.M.,
RA   Ruiz-Quero R., Diaz-Orejas R., Aicart-Ramos C., Moreno-Herrero F.,
RA   Oliva M.A.;
RT   "The TubR-centromere complex adopts a double-ring segrosome structure in
RT   Type III partition systems.";
RL   Nucleic Acids Res. 46:5704-5716(2018).
CC   -!- FUNCTION: A DNA-binding protein that is part of the type III partition
CC       system presumably used to ensure correct segregation of this
CC       bacteriophage. Binds to tubC (centromere-like site) DNA upstream of its
CC       own gene in a sequence-specific fashion (consensus TTGAC); binds to
CC       multiple sites in the tubC region, probably spreading from an initial
CC       site (PubMed:22538818, PubMed:29762781). Upon binding to tubC forms
CC       flexible loops over about 1 kb of DNA that forms 2 rings, covering tubC
CC       and the promoter region. This probably shuts off transcription of the
CC       operon. DNA is both bent and untwisted by TubR (PubMed:29762781). The
CC       TubR-tubC DNA complex binds to TubZ forming large bundles and
CC       decreasing TubZ's GTPase activity (PubMed:22538818).
CC       {ECO:0000269|PubMed:22538818, ECO:0000269|PubMed:29762781}.
CC   -!- SUBUNIT: Monomer; probably dimerizes when bound to DNA
CC       (PubMed:29762781). Binds to TubZ when associated with tubC DNA
CC       (PubMed:22538818). {ECO:0000269|PubMed:22538818,
CC       ECO:0000269|PubMed:29762781}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: This bacteriophage also exists as a circular plasmid
CC       prophage in its host. {ECO:0000269|PubMed:16287978}.
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; AP008983; BAE47888.1; -; Genomic_DNA.
DR   RefSeq; YP_398620.1; NC_007581.1.
DR   PDB; 6TEY; NMR; -; A=1-81.
DR   PDBsum; 6TEY; -.
DR   BMRB; Q331T6; -.
DR   SMR; Q331T6; -.
DR   GeneID; 3772976; -.
DR   KEGG; vg:3772976; -.
DR   Proteomes; UP000001240; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Host cytoplasm; Plasmid partition;
KW   Reference proteome.
FT   CHAIN           1..81
FT                   /note="DNA-binding protein TubR"
FT                   /id="PRO_0000448568"
FT   HELIX           5..17
FT                   /evidence="ECO:0007829|PDB:6TEY"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:6TEY"
FT   HELIX           28..34
FT                   /evidence="ECO:0007829|PDB:6TEY"
FT   HELIX           39..51
FT                   /evidence="ECO:0007829|PDB:6TEY"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:6TEY"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:6TEY"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:6TEY"
FT   HELIX           71..79
FT                   /evidence="ECO:0007829|PDB:6TEY"
SQ   SEQUENCE   81 AA;  9419 MW;  B425653BC328E1C3 CRC64;
     MAVNKNEYKI LIMLKENQCT TELKSFTYTK LCNISKLSMS TVRRSIKKFL ELQYVKEGCK
     QGISKTFYIT PNGIEKLKSI M