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Protein

Antitoxin HipB

Gene

hipB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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 motifPROSITE-ProRule annotation1 PublicationAdd
BLAST

GO - Molecular functioni

  • bacterial-type RNA polymerase core promoter sequence-specific DNA binding Source: EcoCyc
  • sequence-specific DNA binding Source: EcoCyc

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • 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
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: 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 PublicationAdd
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.

Proteomic databases

PaxDbiP23873.

Expressioni

Gene expression databases

CollecTFiEXPREG_00000960.

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

BioGridi4260221. 3 interactions.
DIPiDIP-9899N.
IntActiP23873. 2 interactions.
STRINGi511145.b1508.

Structurei

Secondary structure

1
88
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314Combined sources
Helixi28 – 358Combined sources
Helixi39 – 479Combined sources
Helixi49 – 513Combined sources
Helixi54 – 6310Combined sources
Beta strandi67 – 715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WIUX-ray2.35B/D1-88[»]
3DNVX-ray2.68B1-88[»]
3HZIX-ray2.98B1-88[»]
4YG1X-ray3.25A/B/C/D1-72[»]
4YG4X-ray3.50A/B/C/D4-74[»]
4YG7X-ray3.77B/C/E/G4-74[»]
ProteinModelPortaliP23873.
SMRiP23873. Positions 4-74.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 7155HTH cro/C1-typePROSITE-ProRule annotation1 PublicationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG41061P8. Bacteria.
COG1396. LUCA.
HOGENOMiHOG000225389.
InParanoidiP23873.
KOiK15773.
OMAiHALEVHC.

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

        10         20         30         40         50
MMSFQKIYSP TQLANAMKLV RQQNGWTQSE LAKKIGIKQA TISNFENNPD
60 70 80
NTTLTTFFKI LQSLELSMTL CDAKNASPES TEQQNLEW
Length:88
Mass (Da):10,016
Last modified:November 1, 1991 - v1
Checksum:i63C0E13C1C06CBDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001301023.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74581; AAC74581; b1508.
BAA15180; BAA15180; BAA15180.
GeneIDi946065.
KEGGiecj:JW1501.
eco:b1508.
PATRICi32118310. VBIEscCol129921_1575.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001301023.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WIUX-ray2.35B/D1-88[»]
3DNVX-ray2.68B1-88[»]
3HZIX-ray2.98B1-88[»]
4YG1X-ray3.25A/B/C/D1-72[»]
4YG4X-ray3.50A/B/C/D4-74[»]
4YG7X-ray3.77B/C/E/G4-74[»]
ProteinModelPortaliP23873.
SMRiP23873. Positions 4-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260221. 3 interactions.
DIPiDIP-9899N.
IntActiP23873. 2 interactions.
STRINGi511145.b1508.

Proteomic databases

PaxDbiP23873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74581; AAC74581; b1508.
BAA15180; BAA15180; BAA15180.
GeneIDi946065.
KEGGiecj:JW1501.
eco:b1508.
PATRICi32118310. VBIEscCol129921_1575.

Organism-specific databases

EchoBASEiEB0437.
EcoGeneiEG10442. hipB.

Phylogenomic databases

eggNOGiENOG41061P8. Bacteria.
COG1396. LUCA.
HOGENOMiHOG000225389.
InParanoidiP23873.
KOiK15773.
OMAiHALEVHC.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP23873.
PROiP23873.

Gene expression databases

CollecTFiEXPREG_00000960.

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]
ProtoNetiSearch...

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 7, 2016
This is version 120 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.