CBTA_ECOLI
ID CBTA_ECOLI Reviewed; 124 AA.
AC P64524; P76365; Q2MAZ1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytoskeleton-binding toxin CbtA {ECO:0000303|PubMed:21166897};
DE AltName: Full=Toxin CbtA {ECO:0000303|PubMed:21166897};
DE AltName: Full=Toxin YeeV {ECO:0000303|PubMed:14594833};
GN Name=cbtA {ECO:0000303|PubMed:21166897}; Synonyms=yeeV;
GN OrderedLocusNames=b2005, JW1987;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION AS A TOXIN.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14594833; DOI=10.1128/jb.185.22.6600-6608.2003;
RA Brown J.M., Shaw K.J.;
RT "A novel family of Escherichia coli toxin-antitoxin gene pairs.";
RL J. Bacteriol. 185:6600-6608(2003).
RN [4]
RP FUNCTION AS A TOXIN, INTERACTION WITH FTSZ AND MREB, SUBUNIT, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 1-MET--ARG-15.
RC STRAIN=K12 / BW25113;
RX PubMed=21166897; DOI=10.1111/j.1365-2958.2010.07433.x;
RA Tan Q., Awano N., Inouye M.;
RT "YeeV is an Escherichia coli toxin that inhibits cell division by targeting
RT the cytoskeleton proteins, FtsZ and MreB.";
RL Mol. Microbiol. 79:109-118(2011).
RN [5]
RP FUNCTION AS AN TOXIN.
RC STRAIN=K12 / BW25113;
RX PubMed=22515815; DOI=10.1111/j.1365-2958.2012.08068.x;
RA Masuda H., Tan Q., Awano N., Wu K.P., Inouye M.;
RT "YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ,
RT antagonizing the CbtA (YeeV) toxicity in Escherichia coli.";
RL Mol. Microbiol. 84:979-989(2012).
RN [6]
RP FUNCTION AS A TOXIN, SUBCELLULAR LOCATION, INTERACTION WITH FTSZ AND MREB,
RP AND MUTAGENESIS OF ARG-15 AND PHE-65.
RX PubMed=28931012; DOI=10.1371/journal.pgen.1007007;
RA Heller D.M., Tavag M., Hochschild A.;
RT "CbtA toxin of Escherichia coli inhibits cell division and cell elongation
RT via direct and independent interactions with FtsZ and MreB.";
RL PLoS Genet. 13:E1007007-E1007007(2017).
RN [7]
RP FUNCTION AS A TOXIN, INTERACTION WITH FTSZ, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=28257056; DOI=10.3390/toxins9030077;
RA Wen Z., Wang P., Sun C., Guo Y., Wang X.;
RT "Interaction of type IV toxin/antitoxin systems in cryptic prophages of
RT Escherichia coli K-12.";
RL Toxins 9:0-0(2017).
CC -!- FUNCTION: Toxic component of a type IV toxin-antitoxin (TA) system
CC (PubMed:14594833, PubMed:21166897, PubMed:22515815, PubMed:28931012,
CC PubMed:28257056). Acts as a dual toxin inhibitor that blocks cell
CC division and cell elongation in genetically separable interactions with
CC FtsZ and MreB (PubMed:28931012). Interacts with cytoskeletal proteins
CC FtsZ and MreB; inhibits FtsZ GTP-dependent polymerization and GTPase
CC activity as well as MreB ATP-dependent polymerization (PubMed:21166897,
CC PubMed:28931012). Binds to both the N- and C-terminus of FtsZ, likely
CC blocking its polymerization and localization, leading to blockage of
CC cell division (PubMed:21166897, PubMed:28931012). Overexpression
CC results in inhibition of growth in liquid cultures and decrease in
CC colony formation; these effects are overcome by concomitant expression
CC of antitoxin CbeA (YeeU) (PubMed:14594833). In other experiments cells
CC swell, by 6 hours are lemon-shaped and by 24 hours those that have not
CC lysed are spherical with diminished polar regions (PubMed:21166897,
CC PubMed:28931012). Toxic effects are neutralized by cognate antitoxin
CC CbeA, although there is no direct interaction between the 2 proteins
CC (PubMed:14594833, PubMed:22515815). Toxic effects are also neutralized
CC by overexpression of noncogate antitoxins YafW and YpjF
CC (PubMed:28257056). {ECO:0000269|PubMed:14594833,
CC ECO:0000269|PubMed:21166897, ECO:0000269|PubMed:22515815,
CC ECO:0000269|PubMed:28257056, ECO:0000269|PubMed:28931012}.
CC -!- SUBUNIT: Interacts with FtsZ (PubMed:21166897, PubMed:22515815,
CC PubMed:28931012). Interacts with MreB (PubMed:21166897,
CC PubMed:28931012). {ECO:0000269|PubMed:21166897,
CC ECO:0000269|PubMed:22515815, ECO:0000269|PubMed:28931012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28931012}.
CC -!- INDUCTION: Expressed in mid-log phase at lower levels than toxin relE.
CC {ECO:0000269|PubMed:28257056}.
CC -!- DOMAIN: The N-terminal 15 residues are required for interaction with
CC both FtsZ and MreB, while the C-terminal 63 residues are required for
CC interaction with MreB. {ECO:0000269|PubMed:21166897}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21166897). Deletion
CC of 3 type IV toxin genes (cbtA, ykfI, ypfJ) leads to a slight reduction
CC in resistance to oxidative stress, has no effect on cell growth
CC (PubMed:28257056). {ECO:0000269|PubMed:21166897,
CC ECO:0000269|PubMed:28257056}.
CC -!- MISCELLANEOUS: Encoded in prophage CP4-44. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbtA/YkfI/YpjF toxin family. {ECO:0000305}.
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DR EMBL; U00096; AAC75066.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76565.1; -; Genomic_DNA.
DR PIR; D64965; D64965.
DR RefSeq; NP_416509.1; NC_000913.3.
DR RefSeq; WP_000854814.1; NZ_LN832404.1.
DR AlphaFoldDB; P64524; -.
DR BioGRID; 4261508; 8.
DR IntAct; P64524; 6.
DR STRING; 511145.b2005; -.
DR PaxDb; P64524; -.
DR PRIDE; P64524; -.
DR EnsemblBacteria; AAC75066; AAC75066; b2005.
DR EnsemblBacteria; BAE76565; BAE76565; BAE76565.
DR GeneID; 58391593; -.
DR GeneID; 946534; -.
DR KEGG; ecj:JW1987; -.
DR KEGG; eco:b2005; -.
DR PATRIC; fig|1411691.4.peg.248; -.
DR EchoBASE; EB3170; -.
DR eggNOG; ENOG5030KUQ; Bacteria.
DR HOGENOM; CLU_129204_1_0_6; -.
DR PhylomeDB; P64524; -.
DR BioCyc; EcoCyc:G7085-MON; -.
DR PRO; PR:P64524; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:EcoCyc.
DR GO; GO:0001896; P:autolysis; IMP:EcoCyc.
DR GO; GO:0051494; P:negative regulation of cytoskeleton organization; IMP:EcoCyc.
DR GO; GO:2000245; P:negative regulation of FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoCyc.
DR InterPro; IPR009610; CbtA_toxin.
DR Pfam; PF06755; CbtA_toxin; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cytoplasm; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..124
FT /note="Cytoskeleton-binding toxin CbtA"
FT /id="PRO_0000169116"
FT REGION 1..73
FT /note="Sufficient for toxicity, toxin less stabile; cells
FT filament, protein does not interact with MreB but probably
FT still interacts with FtsZ"
FT /evidence="ECO:0000269|PubMed:21166897"
FT REGION 74..124
FT /note="Required for interaction with MreB"
FT /evidence="ECO:0000269|PubMed:21166897"
FT MUTAGEN 1..15
FT /note="Missing: No longer toxic, cells become lemon-shaped
FT more quickly than wild-type on overexpression."
FT /evidence="ECO:0000269|PubMed:21166897"
FT MUTAGEN 15
FT /note="R->C: Wild-type toxicity, wild-type interaction with
FT FtsZ, no longer interacts with MreB, no longer blocks cell
FT elongation, cells become filamentous. No longer toxic, no
FT altered morphology; when associated with S-65."
FT /evidence="ECO:0000269|PubMed:28931012"
FT MUTAGEN 65
FT /note="F->S: Slightly reduced toxicity, wild-type
FT interaction with MreB, no longer interacts with FtsZ, no
FT longer blocks cell division, cells become spheroid. No
FT longer toxic, no altered morphology; when associated with
FT C-15."
FT /evidence="ECO:0000269|PubMed:28931012"
SQ SEQUENCE 124 AA; 13899 MW; 4327D21EC2A8159A CRC64;
MKTLPVLPGQ AASSRPSPVE IWQILLSRLL DQHYGLTLND TPFADERVIE QHIEAGISLC
DAVNFLVEKY ALVRTDQPGF SACTRSQLIN SIDILRARRA TGLMTRDNYR TVNNITLGKY
PEAK
