TUBZ_BACC1
ID TUBZ_BACC1 Reviewed; 435 AA.
AC Q74P24;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Tubulin-like protein TubZ {ECO:0000305};
DE EC=3.6.5.- {ECO:0000269|PubMed:22847006};
DE AltName: Full=FtsZ-like protein TubZ-Bc {ECO:0000303|PubMed:22847006};
DE AltName: Full=FtsZ/tubulin-like protein TubZ {ECO:0000303|PubMed:22847006};
DE AltName: Full=Plasmid replication protein RepX;
GN Name=tubZ {ECO:0000303|PubMed:30414406}; Synonyms=repX;
GN OrderedLocusNames=BCE_A0070;
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 INDUCTION, AND PROBABLE OPERON.
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).
RN [3] {ECO:0007744|PDB:4EI7, ECO:0007744|PDB:4EI8, ECO:0007744|PDB:4EI9}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-389 ALONE AND IN COMPLEX WITH
RP GDP AND GTP-GAMMA-S, FUNCTION, CATALYTIC ACTIVITY, FILAMENT FORMATION,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-85; GLU-238; GLU-332; ARG-333 AND
RP 390-ALA--PHE-435.
RC STRAIN=ATCC 10987 / NRS 248;
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).
CC -!- FUNCTION: A tubulin-like, filament forming GTPase; the motor component
CC of the type III plasmid partition system which ensures correct
CC segregation of the pBc10987 plasmid (Probable). Binds GTP and forms
CC filaments (PubMed:22847006). The filaments seed from a DNA centromere-
CC like site (tubC)-TubR complex which extends to surround the TubZ
CC filaments. 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 plasmid within the cell (By similarity).
CC {ECO:0000250|UniProtKB:Q8KNP3, ECO:0000269|PubMed:22847006,
CC ECO:0000305|PubMed:22847006}.
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:22847006};
CC -!- SUBUNIT: Forms filaments. Filaments bind to TubR (PubMed:22847006).
CC Binds to the TubR-tubC protein DNA complex (By similarity).
CC {ECO:0000250|UniProtKB:Q8KNP3, ECO:0000269|PubMed:22847006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Forms filaments.
CC {ECO:0000269|PubMed:22847006}.
CC -!- INDUCTION: Expression is repressed by upstream TubR (at protein level).
CC Probably part of the tubR-tubZ operon. {ECO:0000269|PubMed:30414406}.
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. The C-terminus is
CC required for GTP hydrolysis in solution but not in crystals; it plays a
CC role in filament assembly and in binding to TubR (PubMed:22847006).
CC Interactions between the C-terminus and the following monomer drive
CC polymerization (By similarity). {ECO:0000250|UniProtKB:B3FK34,
CC ECO:0000269|PubMed:22847006}.
CC -!- SIMILARITY: Belongs to the FtsZ family. TubZ subfamily. {ECO:0000305}.
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DR EMBL; AE017195; AAS44920.1; -; Genomic_DNA.
DR RefSeq; WP_000918313.1; NC_005707.1.
DR PDB; 4EI7; X-ray; 1.90 A; A/B=1-389.
DR PDB; 4EI8; X-ray; 2.10 A; A=1-389.
DR PDB; 4EI9; X-ray; 3.30 A; A/B=1-389.
DR PDBsum; 4EI7; -.
DR PDBsum; 4EI8; -.
DR PDBsum; 4EI9; -.
DR AlphaFoldDB; Q74P24; -.
DR SMR; Q74P24; -.
DR EnsemblBacteria; AAS44920; AAS44920; BCE_A0070.
DR GeneID; 59159894; -.
DR KEGG; bca:BCE_A0070; -.
DR HOGENOM; CLU_024865_1_1_9; -.
DR OMA; VYNCLAL; -.
DR Proteomes; UP000002527; Plasmid pBc10987.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; 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; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 1.
DR Pfam; PF00091; Tubulin; 1.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW Plasmid; Plasmid partition.
FT CHAIN 1..435
FT /note="Tubulin-like protein TubZ"
FT /id="PRO_0000233626"
FT REGION 403..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:4EI7, ECO:0007744|PDB:4EI9"
FT BINDING 124..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22847006,
FT ECO:0007744|PDB:4EI7, ECO:0007744|PDB:4EI9"
FT BINDING 155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:4EI7, ECO:0007744|PDB:4EI9"
FT BINDING 185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:4EI7, ECO:0007744|PDB:4EI9"
FT BINDING 208..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:4EI7, ECO:0007744|PDB:4EI9"
FT MUTAGEN 85
FT /note="R->A: Loss of GTPase, no polymerization."
FT /evidence="ECO:0000269|PubMed:22847006"
FT MUTAGEN 238
FT /note="E->A: Loss of GTPase, forms polymers twice as
FT efficiently."
FT /evidence="ECO:0000269|PubMed:22847006"
FT MUTAGEN 332
FT /note="E->A: About 40% GTPase, decreased polymer
FT formation."
FT /evidence="ECO:0000269|PubMed:22847006"
FT MUTAGEN 333
FT /note="R->A: No change in GTPase, no change in filament
FT polymerization."
FT /evidence="ECO:0000269|PubMed:22847006"
FT MUTAGEN 390..435
FT /note="Missing: Loss of filament formation and loss of
FT GTPase activity."
FT /evidence="ECO:0000269|PubMed:22847006"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4EI9"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:4EI7"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 156..172
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4EI9"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 204..222
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 245..257
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4EI9"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 294..302
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:4EI7"
FT STRAND 350..360
FT /evidence="ECO:0007829|PDB:4EI7"
FT HELIX 364..383
FT /evidence="ECO:0007829|PDB:4EI7"
SQ SEQUENCE 435 AA; 48719 MW; 4CDB1417257507FE CRC64;
MAGNFSEIES QGNISLKFGF LGLGMGGCAI AAECANKETQ IKNNKYPYRA ILVNTNSQDF
NKIEIKNTGN VRKIQLEGYE QGAARNPQVG EEAFVKHETK IFEAVKQEFE DRDFIWITCG
LGGGTGTGAL LKAIEMLYEH DYNFGLLLTL PRDAEALKVL ENATSRIRSI AMNQEAFGSI
VLIDNAKLYR KFEEENPSAL ANEYTSYSNK YIADALHEIN LVTSSFTPFS DTHFDASEFA
QVINTPGVLS LAKLELKSNQ LDTENPLGYL TQLGNALEKG VLYDTEREEL ESAKKSALSI
VTSPLRAGRL YNFSFLNQME NFLKERTPYV DERPIAPYVN KHTTKKEEDI VKFYSVVAGL
PLPKRVSDII DEITRIKEER EQANSKKSNA VLNKLFAFDD SVQEEKPKKK KLNFGAEPEV
EVADDSQPAK KKLSF
