ID   CBEA_ECOLI              Reviewed;         122 AA.
AC   P76364; O07991; O07994;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   04-NOV-2026, entry version 158.
DE   RecName: Full=Cytoskeleton bundling-enhancing antitoxin CbeA {ECO:0000303|PubMed:22515815};
DE   AltName: Full=Antitoxin CbeA;
DE   AltName: Full=Antitoxin YeeU {ECO:0000303|PubMed:14594833};
GN   Name=cbeA; Synonyms=yeeU; OrderedLocusNames=b2004, JW1986;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION AS AN ANTITOXIN.
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   [5]
RP   FUNCTION AS AN ANTITOXIN, FUNCTION IN CYTOSKELETON BUNDLING, AND
RP   INTERACTION WITH MREB AND FTSZ.
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 AN ANTITOXIN, INDUCTION, AND DISRUPTION 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).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH MAGNESIUM, COFACTOR, AND SUBUNIT.
RX   PubMed=20696400; DOI=10.1016/j.str.2010.04.018;
RA   Arbing M.A., Handelman S.K., Kuzin A.P., Verdon G., Wang C., Su M.,
RA   Rothenbacher F.P., Abashidze M., Liu M., Hurley J.M., Xiao R., Acton T.,
RA   Inouye M., Montelione G.T., Woychik N.A., Hunt J.F.;
RT   "Crystal structures of Phd-Doc, HigA, and YeeU establish multiple
RT   evolutionary links between microbial growth-regulating toxin-antitoxin
RT   systems.";
RL   Structure 18:996-1010(2010).
CC   -!- FUNCTION: Antitoxin component of a type IV toxin-antitoxin (TA) system
CC       (PubMed:14594833, PubMed:22515815, PubMed:28257056). Antitoxin that
CC       counteracts the effect of its cognate toxin CbtA (YeeV)
CC       (PubMed:14594833, PubMed:22515815, PubMed:28257056). It does not bind
CC       to the toxin but instead binds to MreB and FtsZ (the toxin targets),
CC       enhancing their polymerization by forming higher-order bundles; it is
CC       probably retained in the MreB and FtsZ filament bundles
CC       (PubMed:22515815). The mechanism has been proposed to require
CC       intergenic DNA, in cis, between the cbeA (yeeU) and cbta (yeeV) genes
CC       (PubMed:14594833). The intergenic region was not found to be necessary
CC       in another study (PubMed:22515815). Also counteracts the morphological
CC       defects caused by overexpression of SulA and DicB on cell shape
CC       (PubMed:22515815). Also counteracts the effect of non-cognate toxins
CC       YfkI and YpjF (PubMed:28257056). {ECO:0000269|PubMed:14594833,
CC       ECO:0000269|PubMed:22515815, ECO:0000269|PubMed:28257056}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:20696400};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:20696400};
CC   -!- SUBUNIT: Homodimer (Probable). Interacts with polymerized and monomeric
CC       MreB and polymerized FtsZ (PubMed:22515815).
CC       {ECO:0000269|PubMed:22515815, ECO:0000305|PubMed:20696400}.
CC   -!- INTERACTION:
CC       P76364; P0A9A6: ftsZ; NbExp=2; IntAct=EBI-1126877, EBI-370963;
CC       P76364; P0A9X4: mreB; NbExp=2; IntAct=EBI-1126877, EBI-371008;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Expressed in mid-log phase at considerably lower levels than
CC       antitoxin relB. {ECO:0000269|PubMed:28257056}.
CC   -!- DISRUPTION PHENOTYPE: Single deletion has no effect on expression of
CC       cognate toxin cbtA i.e. the probable operon is not autoregulatory
CC       (PubMed:28257056). Deletion of 3 type IV antitoxin genes (cbeA, yafW,
CC       yfjZ) has no effect on cell growth (PubMed:28257056).
CC       {ECO:0000269|PubMed:28257056}.
CC   -!- MISCELLANEOUS: Encoded in prophage CP4-44. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CbeA/YafW/YfjZ antitoxin family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC75065.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15827.1; -; Genomic_DNA.
DR   PIR; C64965; C64965.
DR   RefSeq; NP_416508.1; NC_000913.3.
DR   RefSeq; WP_001285584.1; NZ_CP009789.1.
DR   PDB; 2H28; X-ray; 2.10 A; A/B=1-122.
DR   AlphaFoldDB; P76364; -.
DR   SMR; P76364; -.
DR   BioGRID; 4261519; 13.
DR   BioGRID; 850859; 3.
DR   FunCoup; P76364; 31.
DR   IntAct; P76364; 6.
DR   STRING; 511145.b2004; -.
DR   PaxDb; 511145-b2004; -.
DR   EnsemblBacteria; AAC75065; AAC75065; b2004.
DR   GeneID; 946510; -.
DR   KEGG; ecj:JW1986; -.
DR   KEGG; eco:b2004; -.
DR   KEGG; ecoc:C3026_11300; -.
DR   PATRIC; fig|1411691.4.peg.249; -.
DR   EchoBASE; EB3169; -.
DR   HOGENOM; CLU_144696_0_0_6; -.
DR   InParanoid; P76364; -.
DR   OMA; HLELMML; -.
DR   OrthoDB; 5588975at2; -.
DR   PhylomeDB; P76364; -.
DR   BioCyc; EcoCyc:G7084-MONOMER; -.
DR   EvolutionaryTrace; P76364; -.
DR   PRO; PR:P76364; -.
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:0031342; P:negative regulation of cell killing; EXP:EcoCyc.
DR   GO; GO:0051495; P:positive regulation of cytoskeleton organization; IDA:EcoCyc.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR009320; Antitoxin_CbeA.
DR   InterPro; IPR038025; CbeA_sf.
DR   Pfam; PF06154; CbeA_antitoxin; 1.
DR   SUPFAM; SSF143737; YeeU-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Magnesium; Metal-binding; Reference proteome;
KW   Toxin-antitoxin system.
FT   CHAIN           1..122
FT                   /note="Cytoskeleton bundling-enhancing antitoxin CbeA"
FT                   /id="PRO_0000169115"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:20696400"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:20696400"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:20696400"
FT   STRAND          27..37
FT                   /evidence="ECO:0007829|PDB:2H28"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:2H28"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:2H28"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:2H28"
FT   HELIX           56..79
FT                   /evidence="ECO:0007829|PDB:2H28"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:2H28"
FT   STRAND          97..102
FT                   /evidence="ECO:0007829|PDB:2H28"
FT   STRAND          107..116
FT                   /evidence="ECO:0007829|PDB:2H28"
SQ   SEQUENCE   122 AA;  13684 MW;  E6F703DEA3D67290 CRC64;
     MSDTLPGTTL PDDNHDRPWW GLPCTVTPCF GARLVQEGNR LHYLADRAGI RGLFSDADAY
     HLDQAFPLLM KQLELMLTSG ELNPRHQHTV TLYAKGLTCK ADTLSSCDYV YLAVYPTPEM
     KN
//