TUBZ_CBCP
ID TUBZ_CBCP Reviewed; 358 AA.
AC Q331T7;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Tubulin-like protein TubZ {ECO:0000303|PubMed:22538818};
DE EC=3.6.5.- {ECO:0000269|PubMed:22538818};
DE AltName: Full=Tubulin/FtsZ-like protein TubZ {ECO:0000303|PubMed:22538818};
GN Name=tubZ {ECO:0000303|PubMed:22538818}; ORFNames=CST189;
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] {ECO:0007744|PDB:3V3T}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, FILAMENT FORMATION, AND MUTAGENESIS OF THR-100 AND GLU-200.
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] {ECO:0007744|PDB:4XCQ}
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 1-316 IN COMPLEX WITH GDP,
RP FUNCTION, SUBUNIT, FILAMENT FORMATION, AND MUTAGENESIS OF THR-100; GLU-200;
RP 317-ILE--MET-358 AND 350-ILE--MET-358.
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 tubulin-like, filament forming GTPase; the motor component
CC of the type III partition system presumably used to ensure correct
CC segregation of this bacteriophage. In the presence of Mg(2+) and GTP
CC (or GTP-gamma-S) assembles into filaments which upon polymerization are
CC almost exclusively bound to GDP. Filament formation is cooperative,
CC requiring a critical concentration. Formation occurs very quickly and
CC is followed by disassembly as GTP is consumed. Unlike its plasmid
CC homolog in B.thuringiensis (AC Q8KNP3) GTP-gamma-S does not alter
CC filament formation (PubMed:22538818, PubMed:28230082). When forced to
CC assemble with GDP instead of GTP it makes much stiffer, thicker
CC filaments (PubMed:28230082). The filaments bind a DNA centromere-like
CC site (tubC)-TubR complex which extends to surround the TubZ filaments
CC (PubMed:22538818). Highly dynamic filaments grow at the plus end and
CC depolymerize at the minus end, a process called treadmilling. TubR-tubC
CC complexes track the depolymerizing minus end of the filament, probably
CC pulling phage DNA within the cell (By similarity).
CC {ECO:0000250|UniProtKB:Q8KNP3, ECO:0000269|PubMed:22538818,
CC ECO:0000269|PubMed:28230082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:22538818, ECO:0000269|PubMed:28230082};
CC -!- SUBUNIT: Monomer. In the presence of Mg(2+) and GTP assembles into 2-
CC stranded filaments which coalesce into bundles. Binds a centromere-like
CC site (tubC)-TubR complex. The TubZ-TubR-tubC complex bind to TubY which
CC reshapes the filament bundles into rings (PubMed:22538818). A later
CC paper by the same group shows 4-stranded filament formation and
CC suggests the 2-stranded form is a short-lived intermediate
CC (PubMed:28230082). {ECO:0000269|PubMed:22538818,
CC ECO:0000269|PubMed:28230082}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Note=Forms long
CC dynamic filaments. {ECO:0000269|PubMed:22538818,
CC ECO:0000269|PubMed:28230082}.
CC -!- DOMAIN: Consists of two domains: a nucleotide-binding N-terminus that
CC hydrolyzes GTP and a C-terminus domain necessary for polymerization.
CC The domains are bridged by a long, central helix (PubMed:28230082). The
CC C-terminus is thought to insert into the most distant monomer of the
CC plus end of the filament, forming the complete active site and
CC modulating filament assembly (Probable). {ECO:0000269|PubMed:28230082,
CC ECO:0000305|PubMed:28230082}.
CC -!- MISCELLANEOUS: This bacteriophage also exists as a circular plasmid
CC prophage in its host. {ECO:0000269|PubMed:16287978}.
CC -!- SIMILARITY: Belongs to the FtsZ family. TubZ subfamily. {ECO:0000305}.
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DR EMBL; AP008983; BAE47887.1; -; Genomic_DNA.
DR RefSeq; YP_398619.1; NC_007581.1.
DR PDB; 3V3T; X-ray; 2.30 A; A=1-358.
DR PDB; 4XCQ; X-ray; 2.39 A; A=1-316.
DR PDBsum; 3V3T; -.
DR PDBsum; 4XCQ; -.
DR SMR; Q331T7; -.
DR GeneID; 3772975; -.
DR KEGG; vg:3772975; -.
DR Proteomes; UP000001240; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 1.
DR Pfam; PF00091; Tubulin; 1.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Host cytoplasm; Hydrolase; Nucleotide-binding;
KW Plasmid partition; Reference proteome.
FT CHAIN 1..358
FT /note="Tubulin-like protein TubZ"
FT /id="PRO_0000448564"
FT BINDING 12..16
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:4XCQ"
FT BINDING 95
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:4XCQ"
FT BINDING 99..101
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:4XCQ"
FT BINDING 132
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:4XCQ"
FT BINDING 164
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:4XCQ"
FT BINDING 170
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:4XCQ"
FT BINDING 174
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:4XCQ"
FT BINDING 182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8KNP3"
FT MUTAGEN 100
FT /note="T->A: Reduced GTPase activity, lower critical
FT concentration value, filaments are more stable, forms more
FT stable crystals. More 2-stranded filaments are seen than
FT with wild-type, interacts normally with TubY."
FT /evidence="ECO:0000269|PubMed:22538818,
FT ECO:0000269|PubMed:28230082"
FT MUTAGEN 200
FT /note="E->A: Reduced GTPase activity, lower critical
FT concentration value, filaments are much more stable. More
FT 2-stranded filaments are seen than with wild-type."
FT /evidence="ECO:0000269|PubMed:22538818,
FT ECO:0000269|PubMed:28230082"
FT MUTAGEN 317..358
FT /note="Missing: Polymerizes at higher cricital
FT concentration, binds GTP normally, has no GTPase activity,
FT interacts with TubY."
FT /evidence="ECO:0000269|PubMed:28230082"
FT MUTAGEN 350..358
FT /note="Missing: Polymerizes at higher cricital
FT concentration, binds GTP normally, has almost no GTPase
FT activity, interacts with TubY. In the presence of GDP and
FT TubY forms rings."
FT /evidence="ECO:0000269|PubMed:28230082"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:3V3T"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:3V3T"
FT TURN 151..155
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:3V3T"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3V3T"
FT HELIX 289..304
FT /evidence="ECO:0007829|PDB:3V3T"
SQ SEQUENCE 358 AA; 40209 MW; 4E80DFCC8AECF5A8 CRC64;
MKNKIVFAPI GQGGGNIVDT LLGICGDYNA LFINTSKKDL DSLKHAKHTY HIPYAEGCGK
ERKKAVGYAQ TYYKQIIAQI MEKFSSCDIV IFVATMAGGT GSGITPPILG LAKQMYPNKH
FGFVGVLPKA TEDIDEHMNA IACWNDIMRS TNEGKDISIY LLDNNKREKE SDINKEFATL
FNDFMNMSES HAEGVVDEDE ISKLLTMKKS NVILEFDDKE DIQVALAKSL KESIFAEYTT
NTCEFMGIST TRVVDVEAIK SIVGYPRRTF KGYNSKKNIV VATGIEPQKT TVQMMNEIIE
DKMKQRREVT SKSENMIIEP IALDDEDNKS VISSNEKEIS IDNVEKEIDI NDFFSKYM
