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UniProtKB - P23873 (HIPB_ECOLI)

Entry version 138 (08 May 2019)
Sequence version 1 (01 Nov 1991)
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Protein

Antitoxin HipB

Gene

hipB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi21 – 47H-T-H motifPROSITE-ProRule annotation1 PublicationAdd BLAST27

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Repressor
Biological processToxin-antitoxin system, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Antitoxin HipB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:hipB
Ordered Locus Names:b1508, JW1501
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10442 hipB

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cannot be disrupted, suggesting it is a functional antitoxin; no visible phenotype when the hipBA operon is deleted (PubMed:8021189, PubMed:20616060). A hipA or a hipB-hipA operon deletion show decreased biofilm production in the absence of antibiotics (PubMed:23329678).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi73 – 88Missing : Increased half-life in vivo and in vitro, no change in DNA or HipA-binding. 1 PublicationAdd BLAST16
Mutagenesisi88W → A: No change in DNA or HipA-binding. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001497261 – 88Antitoxin HipBAdd BLAST88

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 (PubMed:22720069).1 Publication

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P23873

PRoteomics IDEntifications database

More...PRIDEi		P23873

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

CollecTF database of bacterial transcription factor binding sites

More...CollecTFi		EXPREG_00000960

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
hipAP238742EBI-1129654,EBI-560590

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4260221, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-180 HipBA toxin-antitoxin complex

Database of interacting proteins

More...DIPi		DIP-9899N

Protein interaction database and analysis system

More...IntActi		P23873, 2 interactors

STRING: functional protein association networks

More...STRINGi		511145.b1508

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
4Z58X-ray2.50A4-74[»]
4Z59X-ray2.30A4-74[»]
4Z5CX-ray2.50A/B4-74[»]
4Z5DX-ray2.15A/B4-74[»]
4Z5HX-ray2.10A3-74[»]
5K98X-ray3.99B/P1-88[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P23873

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P23873

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini17 – 71HTH cro/C1-typePROSITE-ProRule annotation1 PublicationAdd BLAST55

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG41061P8 Bacteria
COG1396 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000225389

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P23873

KEGG Orthology (KO)

More...KOi		K15773

Family and domain databases

Conserved Domains Database

More...CDDi		cd00093 HTH_XRE, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001387 Cro/C1-type_HTH
IPR010982 Lambda_DNA-bd_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01381 HTH_3, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00530 HTH_XRE, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47413 SSF47413, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50943 HTH_CROC1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i63C0E13C1C06CBDA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M61242 Genomic DNA Translation: AAA56877.1
U00096 Genomic DNA Translation: AAC74581.1
AP009048 Genomic DNA Translation: BAA15180.1

Protein sequence database of the Protein Information Resource

More...PIRi		A38112

NCBI Reference Sequences

More...RefSeqi		NP_416025.1, NC_000913.3
WP_001301023.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74581; AAC74581; b1508
BAA15180; BAA15180; BAA15180

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946065

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1501
eco:b1508

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.759

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PDB 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[»]
4Z58X-ray2.50A4-74[»]
4Z59X-ray2.30A4-74[»]
4Z5CX-ray2.50A/B4-74[»]
4Z5DX-ray2.15A/B4-74[»]
4Z5HX-ray2.10A3-74[»]
5K98X-ray3.99B/P1-88[»]
SMRiP23873
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260221, 3 interactors
ComplexPortaliCPX-180 HipBA toxin-antitoxin complex
DIPiDIP-9899N
IntActiP23873, 2 interactors
STRINGi511145.b1508

Proteomic databases

PaxDbiP23873
PRIDEiP23873

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74581; AAC74581; b1508
BAA15180; BAA15180; BAA15180
GeneIDi946065
KEGGiecj:JW1501
eco:b1508
PATRICifig|1411691.4.peg.759

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0437
EcoGeneiEG10442 hipB

Phylogenomic databases

eggNOGiENOG41061P8 Bacteria
COG1396 LUCA
HOGENOMiHOG000225389
InParanoidiP23873
KOiK15773

Enzyme and pathway databases

BioCyciEcoCyc:EG10442-MONOMER
ECOL316407:JW1501-MONOMER
MetaCyc:EG10442-MONOMER

Miscellaneous databases

EvolutionaryTraceiP23873

Protein Ontology

More...PROi		PR:P23873

Gene expression databases

CollecTFiEXPREG_00000960

Family and domain databases

CDDicd00093 HTH_XRE, 1 hit
InterProiView protein in InterPro
IPR001387 Cro/C1-type_HTH
IPR010982 Lambda_DNA-bd_dom_sf
PfamiView protein in Pfam
PF01381 HTH_3, 1 hit
SMARTiView protein in SMART
SM00530 HTH_XRE, 1 hit
SUPFAMiSSF47413 SSF47413, 1 hit
PROSITEiView protein in PROSITE
PS50943 HTH_CROC1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHIPB_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P23873
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: May 8, 2019
This is version 138 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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