ID   TUBZ_BACCE              Reviewed;         435 AA.
AC   Q4MKK8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Tubulin-like protein TubZ {ECO:0000305};
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:Q74P24};
DE   AltName: Full=FtsZ/tubulin-like protein TubZ {ECO:0000305};
DE   AltName: Full=Plasmid replication protein RepX {ECO:0000305};
GN   Name=tubZ; Synonyms=repX; ORFNames=BCE_G9241_pBCXO1_0052;
OS   Bacillus cereus.
OG   Plasmid pBCXO1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G9241;
RX   PubMed=15155910; DOI=10.1073/pnas.0402414101;
RA   Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D.,
RA   Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W.,
RA   Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J.,
RA   Peterson S.N., Weyant R.S., Galloway D.R., Read T.D., Popovic T.,
RA   Fraser C.M.;
RT   "Identification of anthrax toxin genes in a Bacillus cereus associated with
RT   an illness resembling inhalation anthrax.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
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 pBCXO1 plasmid. It is essential for plasmid
CC       replication (By similarity). Binds GTP and forms filaments. The
CC       filaments seed from a DNA centromere-like site (tubC)-TubR complex
CC       which extends to surround the TubZ filaments. Highly dynamic filaments
CC       grow at the plus end and depolymerize at the minus end, a process
CC       called treadmilling. TubR-tubC complexes track the depolymerizing minus
CC       end of the filament, probably pulling plasmid within the cell (By
CC       similarity). {ECO:0000250|UniProtKB:Q74P24,
CC       ECO:0000250|UniProtKB:Q8KNP3}.
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:0000250|UniProtKB:Q74P24};
CC   -!- SUBUNIT: Forms filaments. Binds to the TubR-tubC protein DNA complex.
CC       {ECO:0000250|UniProtKB:Q8KNP3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Forms long, dynamic
CC       filaments. {ECO:0000250|UniProtKB:Q8KNP3}.
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 (By similarity).
CC       Interactions between the C-terminus and the following monomer drive
CC       polymerization (By similarity). {ECO:0000250|UniProtKB:B3FK34,
CC       ECO:0000250|UniProtKB:Q74P24}.
CC   -!- SIMILARITY: Belongs to the FtsZ family. TubZ subfamily. {ECO:0000305}.
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DR   EMBL; AAEK01000038; EAL12705.1; -; Genomic_DNA.
DR   RefSeq; WP_000918303.1; NZ_MUBB01000028.1.
DR   AlphaFoldDB; Q4MKK8; -.
DR   SMR; Q4MKK8; -.
DR   STRING; 1396.DJ87_5687; -.
DR   PATRIC; fig|1396.419.peg.790; -.
DR   eggNOG; COG0206; Bacteria.
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   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Plasmid;
KW   Plasmid partition.
FT   CHAIN           1..435
FT                   /note="Tubulin-like protein TubZ"
FT                   /id="PRO_0000233627"
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:0000250|UniProtKB:Q8KNP3"
FT   BINDING         124..126
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KNP3"
FT   BINDING         185
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KNP3"
FT   BINDING         209
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KNP3"
SQ   SEQUENCE   435 AA;  48735 MW;  B0C0F533FC236065 CRC64;
     MAGNFSEIES QGNISLKFGF LGLGMGGCAI AAECANKETQ IKNNKYPYRA ILVNTNSQDF
     NKIEIKNAGN VRKIQLEGYE QGAARNPQVG EEAFVKHETK IFETVKQEFE DRDFIWITCG
     LGGGTGTGAL LKAIEMLYEH DYNFGLLLTL PRDAEALKVL ENATSRIRSI AMNQEAFGSI
     VLIDNAKLYR KFEEENPSAL ANEYTSYSNK YIADALHEIN LVTSSFTPFS DTHFDASEFA
     QVINTPGVLS LAKLELKSNQ LDTENPLGYL TQLGNALEKG VLYDTEREEL ESAKKSALSI
     VTSPLRASRL YNFSFLNQME NFLKDRTPYV DERPIAPYVN KHTAKKEEDI VKFYSVVAGL
     PLPKRVSDII DEITRIKEER EQANSKKSNA VLNKLFAFDD SVQEEKPKKK KLNFGAEPEV
     EVADDSQPTK KKLSF