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P0AE72 (MAZE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Antitoxin MazE
Gene names
Name:mazE
Synonyms:chpAI, chpR
Ordered Locus Names:b2783, JW2754
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length82 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Antitoxin component of a toxin-antitoxin (TA) module. Labile antitoxin that binds to the MazF mRNA interferase toxin and neutralizes its endoribonuclease activity. Is considered to be an 'addiction' molecule as the cell will die in its absence. The endoribonuclease activity (MazF, a toxin) is inhibited by the labile cognate antitoxin MazE. Toxicity results when the levels of MazE decrease in the cell, leading to mRNA degradation. This effect can be rescued by expression of MazE, but after 6 hours in rich medium the overexpression of MazF leads to programmed cell death. Cell growth and viability are not affected when MazF and MazE are coexpressed. Both MazE and MazE-MazF bind to the promoter region of the mazE-mazF operon to inhibit their transcription. Ref.5 Ref.7 Ref.9 Ref.11

Cell death governed by the MazE-MazF and DinJ-YafQ TA modules seems to play a role in biofilm formation, while MazE-MazF is also implicated in cell death in liquid media. Ref.5 Ref.7 Ref.9 Ref.11

Subunit structure

Forms a heterohexamer composed of alternating toxin and antitoxin homodimers MazF(2)-MazE(2)-MazF2. Ref.6 Ref.14

Induction

Expressed in exponentially growing cells. Induction has been reported to occur after amino acid starvation in a ppGpp-independent fashion and to be Lon protease-dependent (Ref.8), but also to not occur after amino acid starvation and to be regulated by ppGpp (Ref.5). MazE alone and in combination with MazF, represses transcription of the mazE-mazF operon. Fis activates transcription. Part of the relA-mazE-mazF-mazG operon, there is also a second mazE-mazF specific promoter which is negatively autoregulated. Ref.5 Ref.6 Ref.8 Ref.10

Post-translational modification

Degraded by the ClpPA protease during steady state growth and possibly by the Lon protease during amino acid starvation.

Disruption phenotype

Decreased sensitivity to dramatic intracellular increases of ppGpp. Double mazE-mazF deletions survive high temperature, various DNA-damaging agents and H2O2 exposure better than wild-type cells. They produce more P1 phage than wild-type cells, while introduction of lysogens into a growing non-lysogenic deletion culture is lethal. Double mazE-mazF deletions show reduced biofilm formation, and survive antibiotic treatment in log phase better than wild-type cells. Ref.8 Ref.11

Sequence similarities

Belongs to the PemI family.

Contains 1 AbrB-like domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   LigandDNA-binding
   Molecular functionRepressor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8282Antitoxin MazE
PRO_0000089649

Regions

Domain7 – 5145AbrB-like

Experimental info

Mutagenesis81R → A: Binds poorly to DNA. Ref.13
Mutagenesis161R → A: Does not bind to DNA. Ref.13

Secondary structure

........... 82
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AE72 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: CD452A9AA4FB362E

FASTA829,356
        10         20         30         40         50         60 
MIHSSVKRWG NSPAVRIPAT LMQALNLNID DEVKIDLVDG KLIIEPVRKE PVFTLAELVN 

        70         80 
DITPENLHEN IDWGEPKDKE VW 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence and characterization of the relA gene of Escherichia coli."
Metzger S., Dror I.B., Aizenman E., Schreiber G., Toone M., Friesen J.D., Cashel M., Glaser G.
J. Biol. Chem. 263:15699-15704(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE.
Strain: K12.
[2]"chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100."
Masuda Y., Miyakawa K., Nishimura Y., Ohtsubo E.
J. Bacteriol. 175:6850-6856(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / MC1000 / ATCC 39531.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"An Escherichia coli chromosomal 'addiction module' regulated by guanosine 3',5'-bispyrophosphate: a model for programmed bacterial cell death."
Aizenman E., Engelberg-Kulka H., Glaser G.
Proc. Natl. Acad. Sci. U.S.A. 93:6059-6063(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CLEAVAGE BY THE CLPPA PROTEASE, INTERACTION WITH MAZF, INDUCTION, OPERON STRUCTURE.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[6]"The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome."
Marianovsky I., Aizenman E., Engelberg-Kulka H., Glaser G.
J. Biol. Chem. 276:5975-5984(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTION REGULATION, DNA-BINDING, SUBUNIT.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[7]"Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins."
Pedersen K., Christensen S.K., Gerdes K.
Mol. Microbiol. 45:501-510(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ANTITOXIN.
Strain: K12.
[8]"Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA."
Christensen S.K., Pedersen K., Hansen F.G., Gerdes K.
J. Mol. Biol. 332:809-819(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, POSSIBLE CLEAVAGE BY THE LON PROTEASE, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
[9]"MazF-mediated cell death in Escherichia coli: a point of no return."
Amitai S., Yassin Y., Engelberg-Kulka H.
J. Bacteriol. 186:8295-8300(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN PROGRAMMED CELL DEATH.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[10]"MazG -- a regulator of programmed cell death in Escherichia coli."
Gross M., Marianovsky I., Glaser G.
Mol. Microbiol. 59:590-601(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, OPERON STRUCTURE.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574 and K12 / W3110 / ATCC 27325 / DSM 5911.
[11]"A differential effect of E. coli toxin-antitoxin systems on cell death in liquid media and biofilm formation."
Kolodkin-Gal I., Verdiger R., Shlosberg-Fedida A., Engelberg-Kulka H.
PLoS ONE 4:E6785-E6785(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL DEATH, FUNCTION IN BIOFILM FORMATION, DISRUPTION PHENOTYPE.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[12]"mRNA interferases, sequence-specific endoribonucleases from the toxin-antitoxin systems."
Yamaguchi Y., Inouye M.
Prog. Mol. Biol. Transl. Sci. 85:467-500(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Crystal structure of the intrinsically flexible addiction antidote MazE."
Loris R., Marianovsky I., Lah J., Laeremans T., Engelberg-Kulka H., Glaser G., Muyldermans S., Wyns L.
J. Biol. Chem. 278:28252-28257(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH AN ANTIBODY FRAGMENT, DNA-BINDING, MUTAGENESIS OF ARG-8 AND ARG-16.
[14]"Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition."
Kamada K., Hanaoka F., Burley S.K.
Mol. Cell 11:875-884(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16450 Genomic DNA. Translation: BAA41177.1.
J04039 Unassigned DNA. Translation: AAA03238.1.
U29580 Genomic DNA. Translation: AAA69293.1.
U00096 Genomic DNA. Translation: AAC75825.1.
AP009048 Genomic DNA. Translation: BAE76857.1.
PIRBVECZE. B31996.
RefSeqNP_417263.1. NC_000913.3.
YP_490991.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVFX-ray1.65D/E1-82[»]
1UB4X-ray1.70C1-82[»]
ProteinModelPortalP0AE72.
SMRP0AE72. Positions 2-76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0AE72. 10 interactions.
STRING511145.b2783.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75825; AAC75825; b2783.
BAE76857; BAE76857; BAE76857.
GeneID12933307.
947245.
KEGGecj:Y75_p2720.
eco:b2783.
PATRIC32120982. VBIEscCol129921_2883.

Organism-specific databases

EchoBASEEB0566.
EcoGeneEG10571. mazE.

Phylogenomic databases

eggNOGCOG2336.
HOGENOMHOG000289070.
KOK07172.
OMAPENRHEE.
OrthoDBEOG6Z3KS9.
PhylomeDBP0AE72.

Enzyme and pathway databases

BioCycEcoCyc:EG10571-MONOMER.
ECOL316407:JW2754-MONOMER.

Gene expression databases

GenevestigatorP0AE72.

Family and domain databases

InterProIPR007159. AbrB-like_dom.
[Graphical view]
PfamPF04014. Antitoxin-MazE. 1 hit.
[Graphical view]
SMARTSM00966. SpoVT_AbrB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AE72.
PROP0AE72.

Entry information

Entry nameMAZE_ECOLI
AccessionPrimary (citable) accession number: P0AE72
Secondary accession number(s): P18534, Q2MA49
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene