CBEA_ECOLI
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 03-AUG-2022, entry version 139.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 (2.1 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR,
RP 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_LN832404.1.
DR PDB; 2H28; X-ray; 2.10 A; A/B=1-122.
DR PDBsum; 2H28; -.
DR AlphaFoldDB; P76364; -.
DR SMR; P76364; -.
DR BioGRID; 4261519; 12.
DR BioGRID; 850859; 3.
DR IntAct; P76364; 6.
DR STRING; 511145.b2004; -.
DR PaxDb; P76364; -.
DR PRIDE; P76364; -.
DR EnsemblBacteria; AAC75065; AAC75065; b2004.
DR EnsemblBacteria; BAA15827; BAA15827; BAA15827.
DR GeneID; 946510; -.
DR KEGG; ecj:JW1986; -.
DR KEGG; eco:b2004; -.
DR PATRIC; fig|1411691.4.peg.249; -.
DR EchoBASE; EB3169; -.
DR HOGENOM; CLU_144696_0_0_6; -.
DR OMA; NNDRTWW; -.
DR PhylomeDB; P76364; -.
DR BioCyc; EcoCyc:G7084-MON; -.
DR EvolutionaryTrace; P76364; -.
DR PRO; PR:P76364; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IDA:EcoCyc.
DR InterPro; IPR009320; Antitoxin_CbeA.
DR InterPro; IPR038025; CbeA_sf.
DR Pfam; PF06154; CbeA_antitoxin; 1.
DR SUPFAM; SSF143737; SSF143737; 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 80..82
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
