TUBY_CBCP
ID TUBY_CBCP Reviewed; 239 AA.
AC Q331T8;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 23-FEB-2022, entry version 50.
DE RecName: Full=Regulator protein TubY {ECO:0000305|PubMed:22538818};
GN Name=tubY {ECO:0000303|PubMed:22538818}; ORFNames=CST188;
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, DOMAIN, AND MUTAGENESIS OF 227-ASN--ARG-239.
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, AND SUBUNIT.
RC STRAIN=Clostridium phage c-st;
RX PubMed=28230082; DOI=10.1038/srep43342;
RA Fuentes-Perez M.E., Nunez-Ramirez R., Martin-Gonzalez A.,
RA Juan-Rodriguez D., Llorca O., Moreno-Herrero F., Oliva M.A.;
RT "TubZ filament assembly dynamics requires the flexible C-terminal tail.";
RL Sci. Rep. 7:43342-43342(2017).
CC -!- FUNCTION: A probable TubZ filament regulator that is part of the type
CC III partition system presumably used to ensure correct segregation of
CC this bacteriophage. Binds to TubZ in the presence of GTP and Mg(2+),
CC and to TubZ-TubR-tubC (tubC is the centromere-like site). The latter
CC complex is reshaped from large bundles to rings by TubY
CC (PubMed:22538818). Modifies TubZ filaments formed in the presence of
CC GDP to make them thinner and more flexible; in GDP and lacking the last
CC 8 residues of TubZ makes rings without TubT-tubC (PubMed:28230082).
CC {ECO:0000269|PubMed:22538818, ECO:0000269|PubMed:28230082}.
CC -!- SUBUNIT: Forms homooctamers in the absence of the last 13 residues; the
CC coiled coil domain is required for oligomerization. In the presence of
CC GTP and Mg(2+) binds to TubZ and also to TubZ-TubR-tubC DNA; the latter
CC is reshaped from large filament bundles to rings of 30-40 nm diameter.
CC {ECO:0000269|PubMed:22538818, ECO:0000269|PubMed:28230082}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The coiled coil domain is required for oligomerization and for
CC binding to TubZ, but the C-terminal 13 residues are not.
CC {ECO:0000269|PubMed:22538818}.
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; BAE47886.1; -; Genomic_DNA.
DR RefSeq; YP_398618.1; NC_007581.1.
DR SMR; Q331T8; -.
DR GeneID; 3772974; -.
DR KEGG; vg:3772974; -.
DR Proteomes; UP000001240; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR Pfam; PF13411; MerR_1; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Host cytoplasm; Plasmid partition; Reference proteome.
FT CHAIN 1..239
FT /note="Regulator protein TubY"
FT /id="PRO_0000448569"
FT REGION 138..239
FT /note="Required to bind TubZ"
FT /evidence="ECO:0000269|PubMed:22538818"
FT REGION 217..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 150..229
FT /evidence="ECO:0000255"
FT MUTAGEN 227..239
FT /note="Missing: Allows purification of soluble protein.
FT Bind TubZ."
FT /evidence="ECO:0000269|PubMed:22538818"
SQ SEQUENCE 239 AA; 28079 MW; 877C8C3AB5A79BF9 CRC64;
MNEESTRYVD VNYSDLDKEL TYTTSEVAEI LNENESTIRY WCDCFSDYIH IEREGRNRKF
TKSNIDDLAF TKELLKKERL TIKQAQKRWE HIKTQPSQNT KVISTTETTS QENVLNEQAL
LKLEEIKKQF LNDISTQINN TISQQLSTAL NAHNEALEQT KVELKDYISA TIEDKLEANI
SNLKAHIDAT TENTNKQIHQ IYDKDVELVN DLKKHMEERK QQNEEQNNKK GFFGKLFKR
