TUBZ_BACAN
ID TUBZ_BACAN Reviewed; 435 AA.
AC Q9X315; Q7CMH8;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Tubulin-like protein TubZ {ECO:0000305};
DE EC=3.6.5.- {ECO:0000269|PubMed:18179418};
DE AltName: Full=FtsZ-like protein TubZ-Ba {ECO:0000303|PubMed:16585744};
DE AltName: Full=FtsZ/tubulin-like protein TubZ {ECO:0000303|PubMed:18198178};
DE AltName: Full=Plasmid replication protein RepX {ECO:0000303|PubMed:18952800};
GN Name=tubZ {ECO:0000303|PubMed:18198178};
GN Synonyms=repX {ECO:0000303|PubMed:16585744};
GN OrderedLocusNames=pXO1-45 {ECO:0000303|PubMed:10515943},
GN BXA0067 {ECO:0000303|PubMed:12004073},
GN GBAA_pXO1_0067 {ECO:0000303|PubMed:18952800};
OS Bacillus anthracis.
OG Plasmid pXO1.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne; PLASMID=pXO1;
RX PubMed=10515943; DOI=10.1128/jb.181.20.6509-6515.1999;
RA Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., Keim P.,
RA Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., Martinez Y.,
RA Ricke D., Svensson R., Jackson P.J.;
RT "Sequence and organization of pXO1, the large Bacillus anthracis plasmid
RT harboring the anthrax toxin genes.";
RL J. Bacteriol. 181:6509-6515(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ames / isolate Florida / A2012; PLASMID=pXO1;
RX PubMed=12004073; DOI=10.1126/science.1071837;
RA Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L.,
RA Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P.,
RA Fraser C.M.;
RT "Comparative genome sequencing for discovery of novel polymorphisms in
RT Bacillus anthracis.";
RL Science 296:2028-2033(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor; PLASMID=pXO1;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-125.
RC STRAIN=Sterne; PLASMID=pXO1;
RX PubMed=16585744; DOI=10.1128/jb.188.8.2829-2835.2006;
RA Tinsley E., Khan S.A.;
RT "A novel FtsZ-like protein is involved in replication of the anthrax toxin-
RT encoding pXO1 plasmid in Bacillus anthracis.";
RL J. Bacteriol. 188:2829-2835(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, FILAMENT FORMATION, AND
RP SUBUNIT.
RC STRAIN=7702; PLASMID=pXO1;
RX PubMed=18198178; DOI=10.1074/jbc.m709163200;
RA Chen Y., Erickson H.P.;
RT "In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from
RT Bacillus plasmids: evidence for a capping mechanism.";
RL J. Biol. Chem. 283:8102-8109(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, FILAMENT FORMATION, SUBUNIT, MUTAGENESIS OF
RP THR-125, AND POTENTIAL DNA-BINDING.
RC PLASMID=pXO1;
RX PubMed=18179418; DOI=10.1111/j.1365-2958.2007.06100.x;
RA Anand S.P., Akhtar P., Tinsley E., Watkins S.C., Khan S.A.;
RT "GTP-dependent polymerization of the tubulin-like RepX replication protein
RT encoded by the pXO1 plasmid of Bacillus anthracis.";
RL Mol. Microbiol. 67:881-890(2008).
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 pXO1 plasmid. Essential for plasmid replication
CC (PubMed:16585744). The filaments seed from a DNA centromere-like site
CC (tubC)-TubR complex which extends to surround the TubZ filaments.
CC Highly dynamic filaments grow at the plus end and depolymerize at the
CC minus end, a process called treadmilling. TubR-tubC complexes track the
CC depolymerizing minus end of the filament, probably pulling plasmid
CC within the cell (By similarity). Has a high GTPase activity; in the
CC presence of GTP assembles into dynamic filaments which bind almost
CC exclusively GDP. Filament formation is cooperative, requiring a
CC critical concentration. Formation occurs very quickly and is followed
CC by disassembly as GTP is consumed. Small amounts of GTP-gamma-S
CC stabilize filaments (PubMed:18198178, PubMed:18179418). Has high GTP
CC and dGTPase activity, 6-fold lower ATPase activity. Forms filaments in
CC the presence of ATP that also disassemble. Weakly binds DNA in a GTP-
CC dependent, non-sequence-specific manner; GTP hydrolysis is not required
CC for DNA-binding (PubMed:18179418). {ECO:0000250|UniProtKB:Q8KNP3,
CC ECO:0000269|PubMed:16585744, ECO:0000269|PubMed:18179418,
CC ECO:0000269|PubMed:18198178}.
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:18179418, ECO:0000269|PubMed:18198178};
CC -!- ACTIVITY REGULATION: GTPase inhibited by GTP-gamma-S, which also
CC stabilizes filaments. {ECO:0000269|PubMed:18198178}.
CC -!- SUBUNIT: Polymerizes to form two-stranded filaments and bundles at
CC higher concentration in the presence of GTP (PubMed:18198178,
CC PubMed:18179418). Binds to the TubR-tubC protein DNA complex (By
CC similarity). {ECO:0000250|UniProtKB:Q8KNP3,
CC ECO:0000269|PubMed:18179418, ECO:0000269|PubMed:18198178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Forms long, dynamic
CC filaments. {ECO:0000269|PubMed:18198178}.
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 -!- DISRUPTION PHENOTYPE: Loss of plasmid replication.
CC {ECO:0000269|PubMed:16585744}.
CC -!- SIMILARITY: Belongs to the FtsZ family. TubZ subfamily. {ECO:0000305}.
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DR EMBL; AF065404; AAD32349.1; -; Genomic_DNA.
DR EMBL; AE011190; AAM26022.1; -; Genomic_DNA.
DR EMBL; AE017336; AAT28808.2; -; Genomic_DNA.
DR PIR; E59096; E59096.
DR RefSeq; NP_052741.1; NC_001496.1.
DR RefSeq; WP_000918302.1; NZ_VTZH01000011.1.
DR AlphaFoldDB; Q9X315; -.
DR SMR; Q9X315; -.
DR EnsemblBacteria; AAT28808; AAT28808; GBAA_pXO1_0067.
DR GeneID; 45025445; -.
DR KEGG; bar:GBAA_pXO1_0067; -.
DR HOGENOM; CLU_024865_1_1_9; -.
DR OMA; VYNCLAL; -.
DR Proteomes; UP000000594; Plasmid pXO1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 Cytoplasm; DNA-binding; GTP-binding; Hydrolase; Nucleotide-binding;
KW Plasmid; Plasmid partition; Reference proteome.
FT CHAIN 1..435
FT /note="Tubulin-like protein TubZ"
FT /id="PRO_0000233625"
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"
FT MUTAGEN 125
FT /note="T->A: Abolishes plasmid replication. Retains about
FT 6% GTPase activity, forms very few filaments."
FT /evidence="ECO:0000269|PubMed:16585744,
FT ECO:0000269|PubMed:18179418"
SQ SEQUENCE 435 AA; 48707 MW; 6790F533FC236077 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 KLNFGAEPEA
EVADDSQPTK KKLSF
