UniProtKB - P23873 (HIPB_ECOLI)
Antitoxin HipB
hipB
Functioni
Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the toxic effect of cognate toxin HipA (PubMed:20616060).
Also neutralizes the toxic effect of non-cognate toxin YjjJ (PubMed:28430938).
Binds to operator sites with the consensus sequence 5-'TATCCN8GGATA-3' to repress the hipBA operon promoter (PubMed:8021189, PubMed:19150849); binding of HipB2 to DNA induces a 70 degree bend (PubMed:19150849).
This forces HipA dimerization, which blocks HipA's active site and thus its toxic action (PubMed:26222023).
May play a role in biofilm formation (PubMed:23329678).
6 PublicationsActivity regulationi
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 21 – 47 | H-T-H motifPROSITE-ProRule annotation1 PublicationAdd BLAST | 27 |
GO - Molecular functioni
- DNA-binding transcription repressor activity Source: CollecTF
- sequence-specific DNA binding Source: EcoCyc
- transcription cis-regulatory region binding Source: CollecTF
GO - Biological processi
- negative regulation of transcription, DNA-templated Source: EcoCyc
- regulation of growth Source: ComplexPortal
- regulation of transcription, DNA-templated Source: ComplexPortal
- transcription, DNA-templated Source: EcoCyc
Keywordsi
Molecular function | DNA-binding, Repressor |
Biological process | Toxin-antitoxin system, Transcription, Transcription regulation |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10442-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Antitoxin HipB |
Gene namesi | Name:hipB Ordered Locus Names:b1508, JW1501 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
- protein-DNA complex Source: CollecTF
- toxin-antitoxin complex Source: ComplexPortal
Pathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 73 – 88 | Missing : Increased half-life in vivo and in vitro, no change in DNA or HipA-binding. 1 PublicationAdd BLAST | 16 | |
Mutagenesisi | 88 | W → A: No change in DNA or HipA-binding. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000149726 | 1 – 88 | Antitoxin HipBAdd BLAST | 88 |
Post-translational modificationi
Proteomic databases
jPOSTi | P23873 |
PaxDbi | P23873 |
PRIDEi | P23873 |
Interactioni
Subunit structurei
Homodimer (PubMed:8021189). Binds operator DNA sites in the absence of HipA, inducing a 70 degree bend in consecutive operators and deforming DNA between the operators so that HipB dimers bind on opposite faces of the DNA (PubMed:26222023).
Forms a HipA2HipB2 heterotetramer which can interact with a single operator site on DNA, inducing a 70 degree bend (PubMed:19150849). When 2 operators are present each HipB dimer contacts 1 HipA molecule, which are brought together by the DNA bend and dimerize, blocking the HipA active site and inactivating its toxic activity (PubMed:26222023). HipA-HipB-induced bending also distorts the -35 and -10 boxes of the promoter and probably prevents sigma-factor binding, and additionally bound HipB and HipA block RNA polymerase access to the -35 box, thus repressing the operon (PubMed:26222023). This complex also blocks the toxic activity of HipA (PubMed:19150849). Mutations present in allele hipA7 (G22S and D291A) decrease the affinity of HipA for HipB (PubMed:20616060).
6 PublicationsBinary interactionsi
P23873
With | #Exp. | IntAct |
---|---|---|
hipA [P23874] | 2 | EBI-1129654,EBI-560590 |
Protein-protein interaction databases
BioGRIDi | 4260221, 3 interactors |
ComplexPortali | CPX-180, HipBA toxin-antitoxin complex |
DIPi | DIP-9899N |
IntActi | P23873, 2 interactors |
STRINGi | 511145.b1508 |
Structurei
Secondary structure
3D structure databases
SMRi | P23873 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P23873 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 17 – 71 | HTH cro/C1-typePROSITE-ProRule annotation1 PublicationAdd BLAST | 55 |
Phylogenomic databases
eggNOGi | COG1396, Bacteria |
HOGENOMi | CLU_066192_47_2_6 |
InParanoidi | P23873 |
PhylomeDBi | P23873 |
Family and domain databases
CDDi | cd00093, HTH_XRE, 1 hit |
DisProti | DP02899 |
Gene3Di | 1.10.260.40, 1 hit |
InterProi | View protein in InterPro IPR001387, Cro/C1-type_HTH IPR010982, Lambda_DNA-bd_dom_sf |
Pfami | View protein in Pfam PF01381, HTH_3, 1 hit |
SMARTi | View protein in SMART SM00530, HTH_XRE, 1 hit |
SUPFAMi | SSF47413, SSF47413, 1 hit |
PROSITEi | View protein in PROSITE PS50943, HTH_CROC1, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MMSFQKIYSP TQLANAMKLV RQQNGWTQSE LAKKIGIKQA TISNFENNPD
60 70 80
NTTLTTFFKI LQSLELSMTL CDAKNASPES TEQQNLEW
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 |
PIRi | A38112 |
RefSeqi | NP_416025.1, NC_000913.3 WP_001301023.1, NZ_SSZK01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC74581; AAC74581; b1508 BAA15180; BAA15180; BAA15180 |
GeneIDi | 946065 |
KEGGi | ecj:JW1501 eco:b1508 |
PATRICi | fig|1411691.4.peg.759 |
Similar proteinsi
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 |
PIRi | A38112 |
RefSeqi | NP_416025.1, NC_000913.3 WP_001301023.1, NZ_SSZK01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
4YG1 | X-ray | 3.25 | A/B/C/D | 1-72 | [»] | |
4YG4 | X-ray | 3.50 | A/B/C/D | 4-74 | [»] | |
4YG7 | X-ray | 3.77 | B/C/E/G | 4-74 | [»] | |
4Z58 | X-ray | 2.50 | A | 4-74 | [»] | |
4Z59 | X-ray | 2.30 | A | 4-74 | [»] | |
4Z5C | X-ray | 2.50 | A/B | 4-74 | [»] | |
4Z5D | X-ray | 2.15 | A/B | 4-74 | [»] | |
4Z5H | X-ray | 2.10 | A | 3-74 | [»] | |
5K98 | X-ray | 3.99 | B/P | 1-88 | [»] | |
SMRi | P23873 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260221, 3 interactors |
ComplexPortali | CPX-180, HipBA toxin-antitoxin complex |
DIPi | DIP-9899N |
IntActi | P23873, 2 interactors |
STRINGi | 511145.b1508 |
Proteomic databases
jPOSTi | P23873 |
PaxDbi | P23873 |
PRIDEi | P23873 |
Genome annotation databases
EnsemblBacteriai | AAC74581; AAC74581; b1508 BAA15180; BAA15180; BAA15180 |
GeneIDi | 946065 |
KEGGi | ecj:JW1501 eco:b1508 |
PATRICi | fig|1411691.4.peg.759 |
Organism-specific databases
EchoBASEi | EB0437 |
Phylogenomic databases
eggNOGi | COG1396, Bacteria |
HOGENOMi | CLU_066192_47_2_6 |
InParanoidi | P23873 |
PhylomeDBi | P23873 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10442-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P23873 |
PROi | PR:P23873 |
Gene expression databases
CollecTFi | EXPREG_00000960 |
Family and domain databases
CDDi | cd00093, HTH_XRE, 1 hit |
DisProti | DP02899 |
Gene3Di | 1.10.260.40, 1 hit |
InterProi | View protein in InterPro IPR001387, Cro/C1-type_HTH IPR010982, Lambda_DNA-bd_dom_sf |
Pfami | View protein in Pfam PF01381, HTH_3, 1 hit |
SMARTi | View protein in SMART SM00530, HTH_XRE, 1 hit |
SUPFAMi | SSF47413, SSF47413, 1 hit |
PROSITEi | View protein in PROSITE PS50943, HTH_CROC1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | HIPB_ECOLI | |
Accessioni | P23873Primary (citable) accession number: P23873 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1991 |
Last sequence update: | November 1, 1991 | |
Last modified: | February 23, 2022 | |
This is version 152 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references