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P23873

- HIPB_ECOLI

UniProt

P23873 - HIPB_ECOLI

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Protein
Antitoxin HipB
Gene
hipB, b1508, JW1501
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

Degraded by Lon protease; degradation is inhibited in a HipA-HipB complex and when bound to the operator consensus sequence dsDNA.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi21 – 4727H-T-H motif1 Publication
Add
BLAST

GO - Molecular functioni

  1. sequence-specific DNA binding Source: EcoCyc

GO - Biological processi

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

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10442-MONOMER.
ECOL316407:JW1501-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Antitoxin HipB
Gene namesi
Name:hipB
Ordered Locus Names:b1508, JW1501
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10442. hipB.

Pathology & Biotechi

Disruption phenotypei

Cannot be disrupted, suggesting it is a functional antitoxin. No visible phenotype when the hipBA operon is deleted.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 8816Missing: Increased half-life in vivo and in vitro, no change in DNA or HipA-binding. 1 Publication
Add
BLAST
Mutagenesisi88 – 881W → A: No change in DNA or HipA-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8888Antitoxin HipB
PRO_0000149726Add
BLAST

Post-translational modificationi

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.

Expressioni

Gene expression databases

GenevestigatoriP23873.

Interactioni

Subunit structurei

Homodimer. Forms a HipA2HipB2 heterotetramer which can interact with DNA. This complex also blocks the toxic activity of HipA.2 Publications

Protein-protein interaction databases

IntActiP23873. 2 interactions.
STRINGi511145.b1508.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314
Helixi28 – 358
Helixi39 – 479
Helixi49 – 513
Helixi54 – 6310
Beta strandi67 – 715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WIUX-ray2.35B/D1-88[»]
3DNVX-ray2.68B1-88[»]
3HZIX-ray2.98B1-88[»]
ProteinModelPortaliP23873.

Miscellaneous databases

EvolutionaryTraceiP23873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 7155HTH cro/C1-type
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1396.
HOGENOMiHOG000225389.
KOiK15773.
OMAiWTQDALA.
OrthoDBiEOG61KBMJ.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
PfamiPF01381. HTH_3. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23873-1 [UniParc]FASTAAdd to Basket

« Hide

MMSFQKIYSP TQLANAMKLV RQQNGWTQSE LAKKIGIKQA TISNFENNPD   50
NTTLTTFFKI LQSLELSMTL CDAKNASPES TEQQNLEW 88
Length:88
Mass (Da):10,016
Last modified:November 1, 1991 - v1
Checksum:i63C0E13C1C06CBDA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M61242 Genomic DNA. Translation: AAA56877.1.
U00096 Genomic DNA. Translation: AAC74581.1.
AP009048 Genomic DNA. Translation: BAA15180.1.
PIRiA38112.
RefSeqiNP_416025.1. NC_000913.3.
YP_489772.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74581; AAC74581; b1508.
BAA15180; BAA15180; BAA15180.
GeneIDi12931227.
946065.
KEGGiecj:Y75_p1483.
eco:b1508.
PATRICi32118310. VBIEscCol129921_1575.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M61242 Genomic DNA. Translation: AAA56877.1 .
U00096 Genomic DNA. Translation: AAC74581.1 .
AP009048 Genomic DNA. Translation: BAA15180.1 .
PIRi A38112.
RefSeqi NP_416025.1. NC_000913.3.
YP_489772.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WIU X-ray 2.35 B/D 1-88 [» ]
3DNV X-ray 2.68 B 1-88 [» ]
3HZI X-ray 2.98 B 1-88 [» ]
ProteinModelPortali P23873.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P23873. 2 interactions.
STRINGi 511145.b1508.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74581 ; AAC74581 ; b1508 .
BAA15180 ; BAA15180 ; BAA15180 .
GeneIDi 12931227.
946065.
KEGGi ecj:Y75_p1483.
eco:b1508.
PATRICi 32118310. VBIEscCol129921_1575.

Organism-specific databases

EchoBASEi EB0437.
EcoGenei EG10442. hipB.

Phylogenomic databases

eggNOGi COG1396.
HOGENOMi HOG000225389.
KOi K15773.
OMAi WTQDALA.
OrthoDBi EOG61KBMJ.

Enzyme and pathway databases

BioCyci EcoCyc:EG10442-MONOMER.
ECOL316407:JW1501-MONOMER.

Miscellaneous databases

EvolutionaryTracei P23873.
PROi P23873.

Gene expression databases

Genevestigatori P23873.

Family and domain databases

Gene3Di 1.10.260.40. 1 hit.
InterProi IPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view ]
Pfami PF01381. HTH_3. 1 hit.
[Graphical view ]
SMARTi SM00530. HTH_XRE. 1 hit.
[Graphical view ]
SUPFAMi SSF47413. SSF47413. 1 hit.
PROSITEi PS50943. HTH_CROC1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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. "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.

Entry informationi

Entry nameiHIPB_ECOLI
AccessioniPrimary (citable) accession number: P23873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: September 3, 2014
This is version 106 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, Direct protein sequencing, 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

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