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P23873 (HIPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. 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 HipB
Gene names
Name:hipB
Ordered Locus Names:b1508, JW1501
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length88 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Antitoxin component of a toxin-antitoxin (TA) module. Neutralizes the toxic effect of cognate toxin HipA. Binds to operator sites with the consensus sequence 5-'TATCCN8GGATA-3' to repress the hipBA operon promoter; binding to DNA induces a 70 degree bend. Ref.5

Enzyme regulation

Degraded by Lon protease; degradation is inhibited in a HipA-HipB complex and when bound to the operator consensus sequence dsDNA. Ref.6

Subunit structure

Homodimer. Forms a HipA2HipB2 heterotetramer which can interact with DNA. This complex also blocks the toxic activity of HipA. Ref.5 Ref.7

Post-translational modification

Degraded by Lon protease in vivo; half-life is 17 minutes in wild-type cells and over 200 minutes in a lon deletion strain. In vitro degradation by Lon is Mg2+-ATP-dependent.

Disruption phenotype

Cannot be disrupted, suggesting it is a functional antitoxin. No visible phenotype when the hipBA operon is deleted. Ref.5

Sequence similarities

Contains 1 HTH cro/C1-type DNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8888Antitoxin HipB
PRO_0000149726

Regions

Domain17 – 7155HTH cro/C1-type
DNA binding21 – 4727H-T-H motif Ref.5

Experimental info

Mutagenesis73 – 8816Missing: Increased half-life in vivo and in vitro, no change in DNA or HipA-binding. Ref.6
Mutagenesis881W → A: No change in DNA or HipA-binding. Ref.6

Secondary structure

............. 88
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23873 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 63C0E13C1C06CBDA

FASTA8810,016
        10         20         30         40         50         60 
MMSFQKIYSP TQLANAMKLV RQQNGWTQSE LAKKIGIKQA TISNFENNPD NTTLTTFFKI 

        70         80 
LQSLELSMTL CDAKNASPES TEQQNLEW 

« Hide

References

« Hide 'large scale' references
[1]"Structure and organization of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis."
Black D.S., Kelly A.J., Mardis M.J., Moyed H.S.
J. Bacteriol. 173:5732-5739(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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]"Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis."
Black D.S., Irwin B., Moyed H.S.
J. Bacteriol. 176:4081-4091(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-6, CHARACTERIZATION, DNA-BINDING, FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, SUBUNIT, DISRUPTION PHENOTYPE.
Strain: K12.
[6]"Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis."
Hansen S., Vulic M., Min J., Yen T.J., Schumacher M.A., Brennan R.G., Lewis K.
PLoS ONE 7:E39185-E39185(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, CLEAVAGE BY LON, MUTAGENESIS OF 73-ALA--TRP-88 AND TRP-88.
[7]"Interaction investigations of HipA binding to HipB dimer and HipB dimer + DNA complex: a molecular dynamics simulation study."
Li C., Wang Y., Wang Y., Chen G.
J. Mol. Recognit. 26:556-567(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MODELING OF INTERACTION.
[8]"New kinase regulation mechanism found in HipBA: a bacterial persistence switch."
Evdokimov A., Voznesensky I., Fennell K., Anderson M., Smith J.F., Fisher D.A.
Acta Crystallogr. D 65:875-879(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH HIPA.
Strain: K12 / DH5-alpha.
[9]"Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB."
Schumacher M.A., Piro K.M., Xu W., Hansen S., Lewis K., Brennan R.G.
Science 323:396-401(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) IN COMPLEX WITH HIPA AND DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61242 Genomic DNA. Translation: AAA56877.1.
U00096 Genomic DNA. Translation: AAC74581.1.
AP009048 Genomic DNA. Translation: BAA15180.1.
PIRA38112.
RefSeqNP_416025.1. NC_000913.3.
YP_489772.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WIUX-ray2.35B/D1-88[»]
3DNVX-ray2.68B1-88[»]
3HZIX-ray2.98B1-88[»]
ProteinModelPortalP23873.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP23873. 1 interaction.
STRING511145.b1508.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74581; AAC74581; b1508.
BAA15180; BAA15180; BAA15180.
GeneID12931227.
946065.
KEGGecj:Y75_p1483.
eco:b1508.
PATRIC32118310. VBIEscCol129921_1575.

Organism-specific databases

EchoBASEEB0437.
EcoGeneEG10442. hipB.

Phylogenomic databases

eggNOGCOG1396.
HOGENOMHOG000225389.
KOK15773.
OMAWTQDALA.
OrthoDBEOG61KBMJ.

Enzyme and pathway databases

BioCycEcoCyc:EG10442-MONOMER.
ECOL316407:JW1501-MONOMER.

Gene expression databases

GenevestigatorP23873.

Family and domain databases

Gene3D1.10.260.40. 1 hit.
InterProIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
PfamPF01381. HTH_3. 1 hit.
[Graphical view]
SMARTSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMSSF47413. SSF47413. 1 hit.
PROSITEPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23873.
PROP23873.

Entry information

Entry nameHIPB_ECOLI
AccessionPrimary (citable) accession number: P23873
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 11, 2014
This is version 105 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