cbeA

Functionⁱ

Antitoxin component of a type IV toxin-antitoxin (TA) module. Labile antitoxin that counteracts the effect of its cognate toxin CbtA (YeeV). It does not bind to the toxin but instead binds to MreB and FtsZ (the toxin targets), enhancing their polymerization by forming higher-order bundles; it is probably retained in the MreB and FtsZ filament bundles. The mechanism has been proposed to require intergenic DNA, in cis, between the cbeA (yeeU) and cbta (yeeV) genes (PubMed:14594833). The intergenic region was not found to be necessary in another study (PubMed:22515815). Also counteracts the morphological defects caused by overexpression of SulA and DicB on cell shape.2 Publications

Cofactorⁱ

Mg²⁺1 PublicationNote: Binds 1 Mg²⁺ ion per subunit.1 Publication

Sites

Feature key	Position(s)	Length	Description
Metal bindingⁱ	86 – 86	1	Magnesium; via carbonyl oxygen1 Publication Manual assertion based on experiment inⁱ Ref.6 "Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems." Arbing M.A., Handelman S.K., Kuzin A.P., Verdon G., Wang C., Su M., Rothenbacher F.P., Abashidze M., Liu M., Hurley J.M., Xiao R., Acton T., Inouye M., Montelione G.T., Woychik N.A., Hunt J.F. Structure 18:996-1010(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR, SUBUNIT.
Metal bindingⁱ	88 – 88	1	Magnesium; via amide nitrogen and carbonyl oxygen1 Publication Manual assertion based on experiment inⁱ Ref.6 "Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems." Arbing M.A., Handelman S.K., Kuzin A.P., Verdon G., Wang C., Su M., Rothenbacher F.P., Abashidze M., Liu M., Hurley J.M., Xiao R., Acton T., Inouye M., Montelione G.T., Woychik N.A., Hunt J.F. Structure 18:996-1010(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR, SUBUNIT.
Metal bindingⁱ	102 – 102	1	Magnesium1 Publication Manual assertion based on experiment inⁱ Ref.6 "Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems." Arbing M.A., Handelman S.K., Kuzin A.P., Verdon G., Wang C., Su M., Rothenbacher F.P., Abashidze M., Liu M., Hurley J.M., Xiao R., Acton T., Inouye M., Montelione G.T., Woychik N.A., Hunt J.F. Structure 18:996-1010(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR, SUBUNIT.

GO - Molecular functionⁱ

cytoskeletal protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 22515815
metal ion binding Source: UniProtKB-KW

GO - Biological processⁱ

positive regulation of cytoskeleton organization
Source: EcoCyc
Inferred from direct assayⁱ
- 22515815

Complete GO annotation...

Keywords - Ligandⁱ

Magnesium, Metal-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7084-MONOMER. ECOL316407:JW1986-MONOMER.

BioCycⁱ

EcoCyc:G7084-MONOMER.
ECOL316407:JW1986-MONOMER.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cytoskeleton bundling-enhancing protein CbeACurated Alternative name(s): Antitoxin CbeA Antitoxin YeeU1 Publication Manual assertion based on opinion inⁱ Ref.5 "YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli." Masuda H., Tan Q., Awano N., Wu K.P., Inouye M. Mol. Microbiol. 84:979-989(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN ANTITOXIN, FUNCTION IN CYTOSKELETON BUNDLING, INTERACTION WITH MREB AND FTSZ.
Gene namesⁱ	Name:cbeA Synonyms:yeeU Ordered Locus Names:b2004, JW1986
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG13388. cbeA.

EcoGeneⁱ

EG13388. cbeA.

Subcellular locationⁱ

Cytoplasm Curated

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 122	122	Cytoskeleton bundling-enhancing protein CbeA		PRO_0000169115	Add BLAST

Proteomic databases

PaxDbⁱ	P76364.

PaxDbⁱ

P76364.

Interactionⁱ

Subunit structureⁱ

Homodimer (Probable). Interacts with polymerized and monomeric MreB and polymerized FtsZ.Curated2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
ftsZ	P0A9A6	2	EBI-1126877,EBI-370963
mreB	P0A9X4	2	EBI-1126877,EBI-371008

With

Entry

#Exp.

IntAct

Notes

ftsZ

P0A9A6

2

EBI-1126877,EBI-370963

mreB

P0A9X4

2

EBI-1126877,EBI-371008

GO - Molecular functionⁱ

cytoskeletal protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 22515815

Protein-protein interaction databases

BioGridⁱ	4261519. 12 interactions.
IntActⁱ	P76364. 6 interactions.
STRINGⁱ	511145.b2004.

Structureⁱ

Secondary structure

1

122

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description
Beta strandⁱ	27 – 37	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28
Beta strandⁱ	40 – 42	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28
Helixⁱ	45 – 47	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28
Beta strandⁱ	48 – 52	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28
Helixⁱ	56 – 79	24	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28
Beta strandⁱ	80 – 82	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28
Beta strandⁱ	90 – 94	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28
Beta strandⁱ	97 – 102	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28
Beta strandⁱ	107 – 116	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2H28

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H28	X-ray	2.10	A/B	1-122	[»]

ProteinModelPortalⁱ

P76364.

SMRⁱ

P76364. Positions 16-122.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P76364.

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the CbeA/YafW/YfjZ antitoxin family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105MAW. Bacteria. ENOG4111V4B. LUCA.
HOGENOMⁱ	HOG000290944.
KOⁱ	K18838.
OMAⁱ	KQPELML.
PhylomeDBⁱ	P76364.

Family and domain databases

InterProⁱ	IPR009320. YagB_YeeU_YfjZ. [Graphical view]
Pfamⁱ	PF06154. CbeA_antitoxin. 1 hit. [Graphical view]

Sequenceⁱ

Sequence statusⁱ: Complete.

P76364-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSDTLPGTTL PDDNHDRPWW GLPCTVTPCF GARLVQEGNR LHYLADRAGI 
        60         70         80         90        100
RGLFSDADAY HLDQAFPLLM KQLELMLTSG ELNPRHQHTV TLYAKGLTCK 
       110        120 
ADTLSSCDYV YLAVYPTPEM KN

Length:122

Mass (Da):13,684

Last modified:February 1, 1997 - v1

Checksum:ⁱE6F703DEA3D67290

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA. Translation: AAC75065.1. AP009048 Genomic DNA. Translation: BAA15827.1.
PIRⁱ	C64965.
RefSeqⁱ	NP_416508.1. NC_000913.3. WP_001285584.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaⁱ	AAC75065; AAC75065; b2004. BAA15827; BAA15827; BAA15827.
GeneIDⁱ	946510.
KEGGⁱ	ecj:JW1986. eco:b2004.
PATRICⁱ	32119341. VBIEscCol129921_2080.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA. Translation: AAC75065.1. AP009048 Genomic DNA. Translation: BAA15827.1.
PIRⁱ	C64965.
RefSeqⁱ	NP_416508.1. NC_000913.3. WP_001285584.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H28	X-ray	2.10	A/B	1-122	[»]

ProteinModelPortalⁱ

P76364.

SMRⁱ

P76364. Positions 16-122.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

BioGridⁱ	4261519. 12 interactions.
IntActⁱ	P76364. 6 interactions.
STRINGⁱ	511145.b2004.

Proteomic databases

PaxDbⁱ	P76364.

PaxDbⁱ

P76364.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75065; AAC75065; b2004. BAA15827; BAA15827; BAA15827.
GeneIDⁱ	946510.
KEGGⁱ	ecj:JW1986. eco:b2004.
PATRICⁱ	32119341. VBIEscCol129921_2080.

Organism-specific databases

EchoBASEⁱ	EB3169.
EcoGeneⁱ	EG13388. cbeA.

Phylogenomic databases

eggNOGⁱ	ENOG4105MAW. Bacteria. ENOG4111V4B. LUCA.
HOGENOMⁱ	HOG000290944.
KOⁱ	K18838.
OMAⁱ	KQPELML.
PhylomeDBⁱ	P76364.

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7084-MONOMER. ECOL316407:JW1986-MONOMER.

BioCycⁱ

EcoCyc:G7084-MONOMER.
ECOL316407:JW1986-MONOMER.

Miscellaneous databases

EvolutionaryTraceⁱ	P76364.
PROⁱ	P76364.

Family and domain databases

InterProⁱ	IPR009320. YagB_YeeU_YfjZ. [Graphical view]
Pfamⁱ	PF06154. CbeA_antitoxin. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

CBEA_ECOLI

Accessionⁱ

Primary (citable) accession number: P76364
Secondary accession number(s): O07991, O07994

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	September 7, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P76364 (CBEA_ECOLI)

UniProt

P76364 - CBEA_ECOLI

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Cytoskeleton bundling-enhancing protein CbeA

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ