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Entry version 143 (08 May 2019)
Sequence version 2 (19 Jul 2003)
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Protein

Serine/threonine-protein kinase toxin HipA

Gene

hipA

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

Toxic component of a type II toxin-antitoxin (TA) system, first identified by mutations that increase production of persister cells, a fraction of cells that are phenotypic variants not killed by antibiotics, which lead to multidrug tolerance (PubMed:6348026, PubMed:8021189, PubMed:16707675, PubMed:26222023). Persistence may be ultimately due to global remodeling of the persister cell's ribosomes (PubMed:25425348). Phosphorylates Glu-tRNA-ligase (AC P04805, gltX, on 'Ser-239') in vivo (PubMed:24095282, PubMed:24343429). Phosphorylation of GltX prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance (PubMed:24095282, PubMed:24343429, PubMed:25848049). Once the level of HipA exceeds a threshold cells become dormant, and the length of dormancy is determined by how much HipA levels exceed the threshold (PubMed:20616060). The hipA7 mutation (a double G22S D291A mutation) leads to increased generation of persister cells (cells that survive antibiotic treatment) probably by entering into a dormant state, as well as cold-sensitivity (PubMed:14622409, PubMed:16707675). Wild-type cells produce persisters at a frequency of 10(-6) to 10(-5) whereas hipA7 cells produce about 100-fold more persisters (PubMed:14622409, PubMed:16707675, PubMed:25425348). hipA7 decreases the affinity for antitoxin HipB, leading to increased HipA levels and persistence (PubMed:20616060); depending on the protein level, can be toxic enough to reduce cell growth or even kill cells. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7 (PubMed:14622409, PubMed:25848049). Generation of persister cells by HipA also requires mRNA interferase toxins (such as MazF, RelE or YafO) and Lon protease; a strain deleted for 10 type II TAs does not produce persisters when HipA (or HipA7) is expressed, nor does a lon deletion strain or bacteria with alterations of polyphosphate levels, although levels of (p)ppGpp increase (PubMed:25848049). The toxic effect of HipA is neutralized by its cognate antitoxin HipB (PubMed:20616060). Also neutralized by overexpression of gltX (PubMed:24343429, PubMed:28430938). With HipB acts as a corepressor for transcription of the hipBA promoter (PubMed:8021189); binding of HipA-HipB to DNA induces a 70 degree bend (PubMed:19150849, PubMed:26222023). This brings together and dimerizes 2 HipA molecules, which distorts the promoter region, preventing sigma-factor binding; additionally HipA and HipB would physically prevent RNA core polymerase from contacting the -35 promoter box (PubMed:26222023). May play a role in biofilm formation (PubMed:23329678).15 Publications

Miscellaneous

The hipA7 allele (G22S and D291A) as well as a P86L mutation have been identified in E.coli isolates from human patients with urinary tract infections, showing the mutations may be clinically relevant (PubMed:26222023).1 Publication

Caution

Has been reported to phosphorylate EF-Tu in vitro (on 'Thr-383') (PubMed:19150849). According to another report, does not phosphorylate EF-Tu (PubMed:19622872).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Once phosphorylated no longer has kinase activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei181ATPCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei309Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi152 – 157ATPCombined sources1 Publication6
Nucleotide bindingi234 – 236ATPCombined sources1 Publication3
Nucleotide bindingi311 – 314ATPCombined sources1 Publication4
Nucleotide bindingi331 – 332ATPCombined sources1 Publication2
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi379 – 3821 Publication4

<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

GO - Biological processi

<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, Kinase, Repressor, Serine/threonine-protein kinase, Transferase
Biological processAntibiotic resistance, Toxin-antitoxin system
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10443-MONOMER
ECOL316407:JW1500-MONOMER
MetaCyc:EG10443-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:
Serine/threonine-protein kinase toxin HipA (EC:2.7.11.11 Publication)
Short name:
Ser/Thr-protein kinase HipA
Alternative name(s):
Toxin HipA
<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:hipA
Ordered Locus Names:b1507, JW1500
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
EG10443 hipA

<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

<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

A hipA or a hipB-hipA operon deletion have no visible phenotype (PubMed:20616060). Initially cells lacking hipA or the hipBA operon were thought not to produce persister cells at a high frequency; this was later shown to be a strain-specific phenotype (PubMed:8021189). 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>Mutagenesisi22G → S: Loss of toxicity, does not confer high persistence. Single mutation has decreased affinity for HipB-operator. Loss of toxicity, high levels of persister cells and cold sensitivity, decreased affinity for HipB; in hipA7; when associated with A-291. 3 Publications1
Mutagenesisi86P → L: High levels of persister cells formed which survive better than wild-type in ampicillin or ciprofloxacin, decreased affinity for HipB-operator. 1 Publication1
Mutagenesisi88D → N: Loss of toxicity, still confers high levels of persister cells. Decreased affinity for HipB-operator. 2 Publications1
Mutagenesisi150S → A: No phosphorylation; cells grow normally. 1 Publication1
Mutagenesisi291D → A: Retains toxicity and high persistence but not cold-sensitive. Loss of toxicity, high levels of persister cells and cold sensitivity, decreased affinity for HipB; in hipA7; when associated with S-22. 2 Publications1
Mutagenesisi309D → Q: Loss of autophosphorylation; cells grow normally; protein can accumulate to high levels in E.coli. 1 Publication1
Mutagenesisi332D → Q: Loss of autophosphorylation; cells grow normally. 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_00000839881 – 440Serine/threonine-protein kinase toxin HipAAdd BLAST440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei150Phosphoserine; by autocatalysis2 Publications1

<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

Autophosphorylates intermolecularly on Ser-150; phosphorylated form not seen to bind ATP and no longer has kinase activity.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P23874

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

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PaxDbi
P23874

PRoteomics IDEntifications database

More...
PRIDEi
P23874

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P23874

<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_00000970

<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

Forms a HipA2HipB2 heterotetramer which can interact with a single operator on DNA (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). Mutations present in allele hipA7 (G22S and D291A) decrease the affinity of HipA for HipB (PubMed:20616060).

7 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260220, 11 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-180 HipBA toxin-antitoxin complex

Database of interacting proteins

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DIPi
DIP-9898N

Protein interaction database and analysis system

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IntActi
P23874, 4 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1507

<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

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P23874

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P23874

<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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the HipA Ser/Thr kinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CAF Bacteria
COG3550 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000188799

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23874

KEGG Orthology (KO)

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KOi
K07154

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR012893 HipA-like_C
IPR017508 HipA_N1

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13657 Couple_hipA, 1 hit
PF07804 HipA_C, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03071 couple_hipA, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P23874-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPKLVTWMNN QRVGELTKLA NGAHTFKYAP EWLASRYARP LSLSLPLQRG
60 70 80 90 100
NITSDAVFNF FDNLLPDSPI VRDRIVKRYH AKSRQPFDLL SEIGRDSVGA
110 120 130 140 150
VTLIPEDETV THPIMAWEKL TEARLEEVLT AYKADIPLGM IREENDFRIS
160 170 180 190 200
VAGAQEKTAL LRIGNDWCIP KGITPTTHII KLPIGEIRQP NATLDLSQSV
210 220 230 240 250
DNEYYCLLLA KELGLNVPDA EIIKAGNVRA LAVERFDRRW NAERTVLLRL
260 270 280 290 300
PQEDMCQTFG LPSSVKYESD GGPGIARIMA FLMGSSEALK DRYDFMKFQV
310 320 330 340 350
FQWLIGATDG HAKNFSVFIQ AGGSYRLTPF YDIISAFPVL GGTGIHISDL
360 370 380 390 400
KLAMGLNASK GKKTAIDKIY PRHFLATAKV LRFPEVQMHE ILSDFARMIP
410 420 430 440
AALDNVKTSL PTDFPENVVT AVESNVLRLH GRLSREYGSK
Length:440
Mass (Da):49,276
Last modified:July 19, 2003 - v2
<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:i378771C4CAB55319
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti40P → Q in AAA56878 (PubMed:1715862).Curated1
Sequence conflicti214 – 215GL → WV in AAA56878 (PubMed:1715862).Curated2
Sequence conflicti274G → R in AAA56878 (PubMed:1715862).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 49143.80 Da from positions 1 - 440. Determined by MALDI. 1 Publication
Molecular mass is 49223.80 Da from positions 1 - 440. Determined by MALDI. Phosphorylated form.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M61242 Genomic DNA Translation: AAA56878.1
U00096 Genomic DNA Translation: AAC74580.1
AP009048 Genomic DNA Translation: BAA15179.2

Protein sequence database of the Protein Information Resource

More...
PIRi
F64904

NCBI Reference Sequences

More...
RefSeqi
NP_416024.1, NC_000913.3
WP_001125439.1, NZ_CP014272.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74580; AAC74580; b1507
BAA15179; BAA15179; BAA15179

Database of genes from NCBI RefSeq genomes

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GeneIDi
946064

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1500
eco:b1507

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.760

<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: AAA56878.1
U00096 Genomic DNA Translation: AAC74580.1
AP009048 Genomic DNA Translation: BAA15179.2
PIRiF64904
RefSeqiNP_416024.1, NC_000913.3
WP_001125439.1, NZ_CP014272.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WIUX-ray2.35A/C1-440[»]
3DNTX-ray1.66A/B1-440[»]
3DNUX-ray1.54A1-440[»]
3DNVX-ray2.68A1-440[»]
3FBRX-ray3.50A1-437[»]
3HZIX-ray2.98A1-440[»]
3TPBX-ray1.88A1-440[»]
3TPDX-ray1.50A1-440[»]
3TPEX-ray1.90A1-440[»]
3TPTX-ray2.25A/B1-440[»]
3TPVX-ray2.30B1-440[»]
4YG7X-ray3.77D/K2-437[»]
5K98X-ray3.99A/D2-440[»]
SMRiP23874
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4260220, 11 interactors
ComplexPortaliCPX-180 HipBA toxin-antitoxin complex
DIPiDIP-9898N
IntActiP23874, 4 interactors
STRINGi511145.b1507

PTM databases

iPTMnetiP23874

Proteomic databases

jPOSTiP23874
PaxDbiP23874
PRIDEiP23874

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74580; AAC74580; b1507
BAA15179; BAA15179; BAA15179
GeneIDi946064
KEGGiecj:JW1500
eco:b1507
PATRICifig|1411691.4.peg.760

Organism-specific databases

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

More...
EchoBASEi
EB0438
EcoGeneiEG10443 hipA

Phylogenomic databases

eggNOGiENOG4105CAF Bacteria
COG3550 LUCA
HOGENOMiHOG000188799
InParanoidiP23874
KOiK07154

Enzyme and pathway databases

BioCyciEcoCyc:EG10443-MONOMER
ECOL316407:JW1500-MONOMER
MetaCyc:EG10443-MONOMER

Miscellaneous databases

EvolutionaryTraceiP23874

Protein Ontology

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PROi
PR:P23874

Gene expression databases

CollecTFiEXPREG_00000970

Family and domain databases

InterProiView protein in InterPro
IPR012893 HipA-like_C
IPR017508 HipA_N1
PfamiView protein in Pfam
PF13657 Couple_hipA, 1 hit
PF07804 HipA_C, 1 hit
TIGRFAMsiTIGR03071 couple_hipA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiHIPA_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: P23874
Secondary accession number(s): P76139, P76880, P77507
<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: July 19, 2003
Last modified: May 8, 2019
This is version 143 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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