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P23873

- HIPB_ECOLI

UniProt

P23873 - HIPB_ECOLI

Protein

Antitoxin HipB

Gene

hipB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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 motifPROSITE-ProRule annotationAdd
    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

    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. 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 HipBPRO_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.4 Publications

    Protein-protein interaction databases

    IntActiP23873. 2 interactions.
    STRINGi511145.b1508.

    Structurei

    Secondary structure

    1
    88
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23873.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 7155HTH cro/C1-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    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

    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: October 1, 2014
    This is version 107 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