SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0AE72

- MAZE_ECOLI

UniProt

P0AE72 - MAZE_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Antitoxin MazE
Gene
mazE, chpAI, chpR, b2783, JW2754
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications
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.4 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10571-MONOMER.
ECOL316407:JW2754-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Antitoxin MazE
Gene namesi
Name:mazE
Synonyms:chpAI, chpR
Ordered Locus Names:b2783, JW2754
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10571. mazE.

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81R → A: Binds poorly to DNA. 1 Publication
Mutagenesisi16 – 161R → A: Does not bind to DNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8282Antitoxin MazE
PRO_0000089649Add
BLAST

Post-translational modificationi

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

Expressioni

Inductioni

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 (1 Publication), but also to not occur after amino acid starvation and to be regulated by ppGpp (1 Publication). 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.4 Publications

Gene expression databases

GenevestigatoriP0AE72.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP0AE72. 10 interactions.
STRINGi511145.b2783.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94
Beta strandi12 – 154
Helixi19 – 246
Helixi55 – 606
Turni64 – 663

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVFX-ray1.65D/E1-82[»]
1UB4X-ray1.70C1-82[»]
ProteinModelPortaliP0AE72.
SMRiP0AE72. Positions 2-76.

Miscellaneous databases

EvolutionaryTraceiP0AE72.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 5145AbrB-like
Add
BLAST

Sequence similaritiesi

Belongs to the PemI family.
Contains 1 AbrB-like domain.

Phylogenomic databases

eggNOGiCOG2336.
HOGENOMiHOG000289070.
KOiK07172.
OMAiPENRHEE.
OrthoDBiEOG6Z3KS9.
PhylomeDBiP0AE72.

Family and domain databases

InterProiIPR007159. AbrB-like_dom.
[Graphical view]
PfamiPF04014. Antitoxin-MazE. 1 hit.
[Graphical view]
SMARTiSM00966. SpoVT_AbrB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AE72-1 [UniParc]FASTAAdd to Basket

« Hide

MIHSSVKRWG NSPAVRIPAT LMQALNLNID DEVKIDLVDG KLIIEPVRKE   50
PVFTLAELVN DITPENLHEN IDWGEPKDKE VW 82
Length:82
Mass (Da):9,356
Last modified:December 6, 2005 - v1
Checksum:iCD452A9AA4FB362E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiB31996. BVECZE.
RefSeqiNP_417263.1. NC_000913.3.
YP_490991.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75825; AAC75825; b2783.
BAE76857; BAE76857; BAE76857.
GeneIDi12933307.
947245.
KEGGiecj:Y75_p2720.
eco:b2783.
PATRICi32120982. VBIEscCol129921_2883.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi B31996. BVECZE.
RefSeqi NP_417263.1. NC_000913.3.
YP_490991.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MVF X-ray 1.65 D/E 1-82 [» ]
1UB4 X-ray 1.70 C 1-82 [» ]
ProteinModelPortali P0AE72.
SMRi P0AE72. Positions 2-76.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0AE72. 10 interactions.
STRINGi 511145.b2783.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75825 ; AAC75825 ; b2783 .
BAE76857 ; BAE76857 ; BAE76857 .
GeneIDi 12933307.
947245.
KEGGi ecj:Y75_p2720.
eco:b2783.
PATRICi 32120982. VBIEscCol129921_2883.

Organism-specific databases

EchoBASEi EB0566.
EcoGenei EG10571. mazE.

Phylogenomic databases

eggNOGi COG2336.
HOGENOMi HOG000289070.
KOi K07172.
OMAi PENRHEE.
OrthoDBi EOG6Z3KS9.
PhylomeDBi P0AE72.

Enzyme and pathway databases

BioCyci EcoCyc:EG10571-MONOMER.
ECOL316407:JW2754-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AE72.
PROi P0AE72.

Gene expression databases

Genevestigatori P0AE72.

Family and domain databases

InterProi IPR007159. AbrB-like_dom.
[Graphical view ]
Pfami PF04014. Antitoxin-MazE. 1 hit.
[Graphical view ]
SMARTi SM00966. SpoVT_AbrB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiMAZE_ECOLI
AccessioniPrimary (citable) accession number: P0AE72
Secondary accession number(s): P18534, Q2MA49
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi