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UniProtKB - P23837 (PHOQ_ECOLI)

Entry version 199 (07 Apr 2021)
Sequence version 1 (01 Nov 1991)
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Protein

Sensor protein PhoQ

Gene

phoQ

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

Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg2+ environments and the control of acid resistance genes. In low periplasmic Mg2+, PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg2+, acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By similarity). PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, or treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB are required for its action on PhoQ, which then acts on PhoP. Mediates magnesium influx to the cytosol by activation of mgtA. Promotes expression of the two-component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.By similarity1 Publication

Miscellaneous

There is a close linkage between the PhoP/PhoQ and Rcs signaling systems, and both signaling systems respond to certain external divalent cations (zinc and magnesium).
Two-component regulatory system EvgA/EvgS interacts with PhoP/PhoQ via signal transduction mediated by phospho-EvgA.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. EC:2.7.13.3

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Acetyl-CoA acts as a non-competitive inhibitor of the PhoQ autokinase activity. Feedback inhibited by MgrB, which seems to bind PhoQ, altering its activity and that of downstream effector PhoP.3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=20.93 µM for ATP (at 22 degrees Celsius and pH 8, in the presence of 50 mM KCl and 1 mM MgCl2)2 Publications
  2. KM=55 µM for ATP (at 22 degrees Celsius and pH 8, in the presence of 25 mM KCl and 0.4 mM MgCl2)2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi151Divalent metal cation1
    Metal bindingi152Divalent metal cation1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei202Plays a critical role in the switching between kinase and phosphatase states1
    Metal bindingi385Magnesium1
    Metal bindingi442Magnesium1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi385 – 393ATP9
    Nucleotide bindingi415 – 420ATP6
    Nucleotide bindingi434 – 446ATPAdd BLAST13

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    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 functionHydrolase, Kinase, Protein phosphatase, Transferase
    Biological processTwo-component regulatory system
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:PHOQ-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.13.3, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P23837

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Sensor protein PhoQ (EC:2.7.13.3, EC:3.1.3.-)
    Alternative name(s):
    Sensor histidine protein kinase/phosphatase PhoQ
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:phoQ
    Ordered Locus Names:b1129, JW1115
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    <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

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 16CytoplasmicSequence analysisAdd BLAST16
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei17 – 37HelicalSequence analysisAdd BLAST21
    Topological domaini38 – 194PeriplasmicSequence analysisAdd BLAST157
    Transmembranei195 – 215HelicalSequence analysisAdd BLAST21
    Topological domaini216 – 486CytoplasmicSequence analysisAdd BLAST271

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    <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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi27V → N: Shows Mg(2+)-dependent signaling and partial gene activation activity; when associated with A-202. 1 Publication1
    Mutagenesisi30L → N: Shows Mg(2+)-dependent signaling and displays higher gene activation activity than wild-type; when associated with A-202. 1 Publication1
    Mutagenesisi47T → L: No significant effect (with or without MgCl(2) or CaCl(2)). 1 Publication1
    Mutagenesisi48T → A, C, E, M, N, Q, S or V: No significant effect (with or without MgCl(2) or CaCl(2)). 1 Publication1
    Mutagenesisi48T → D, G, H, I, K, L, P or R: Confers less than 30% of the wild-type levels of PhoP/PhoQ-signaling cascade in absence of CaCl(2) or MgCl(2). 1 Publication1
    Mutagenesisi48T → F or W: Decreased sensitivity to repression by calcium but not by magnesium. 1 Publication1
    Mutagenesisi48T → Y: Higher activity than wild-type (with or without MgCl(2) or CaCl(2)). 1 Publication1
    Mutagenesisi50R → D: Large decrease in the transcriptional activation of PhoQ-dependent genes. 1 Publication1
    Mutagenesisi54G → D: Very large decrease in the transcriptional activation of PhoQ-dependent genes. 1 Publication1
    Mutagenesisi68N → L: No significant effect (with or without MgCl(2) or CaCl(2)). 1 Publication1
    Mutagenesisi90D → A: No significant effect (with or without MgCl(2) or CaCl(2)). 1 Publication1
    Mutagenesisi148 – 154EDDDDAE → QNNNNAQ: Unable to bind divalent cations in vitro and impaired in the ability to respond to Mg(2+) deprivation in vivo. 1 Publication7
    Mutagenesisi149D → A: Wild-type effect concerning mgrB transcription. 1 Publication1
    Mutagenesisi150D → I: Wild-type effect concerning mgrB transcription. 1 Publication1
    Mutagenesisi151D → I: Wild-type effect concerning mgrB transcription. 1 Publication1
    Mutagenesisi152D → F: Wild-type effect concerning mgrB transcription. 1 Publication1
    Mutagenesisi179D → L or A: Locked-on mutant defective in Mg(2+)-sensing and unable to control its phosphorylation state and phosphotransfer to phoP. 2 Publications1
    Mutagenesisi179D → R: Very large decrease in the transcriptional activation of PhoQ-dependent genes. 2 Publications1
    Mutagenesisi199L → N: Shows Mg(2+)-dependent signaling and partial gene activation activity; when associated with A-202. 1 Publication1
    Mutagenesisi202N → A: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild-type PhoQ. Shows no detectable autophosphorylation. Still displays phosphatase activity. Recovers Mg(2+)-dependent signaling and partial gene activation activity; when associated with N-27 or N-199 or N-203 or N-205. Recovers Mg(2+)-dependent signaling and displays higher gene activation activity than wild-type; when associated with N-30. 1 Publication1
    Mutagenesisi202N → I, L, M, F, W, Y, V, C, G or P: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild-type PhoQ. 1 Publication1
    Mutagenesisi202N → R, D, Q, E or H: Shows similar activity profile to wild-type. 1 Publication1
    Mutagenesisi203L → N: Shows Mg(2+)-dependent signaling and partial gene activation activity; when associated with A-202. 1 Publication1
    Mutagenesisi205L → N: Shows Mg(2+)-dependent signaling and partial gene activation activity; when associated with A-202. 1 Publication1
    Mutagenesisi392K → A: 44-fold decrease in ATP affinity and 6-fold decrease in activity. 1 Publication1
    Mutagenesisi434R → A: 2-fold decrease in ATP affinity and 51-fold decrease in activity. 1 Publication1
    Mutagenesisi439R → A: 3-fold decrease in ATP affinity and 2-fold increase in activity. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB04395, Phosphoaminophosphonic Acid-Adenylate Ester

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000748371 – 486Sensor protein PhoQAdd BLAST486

    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 residuei277Phosphohistidine; by autocatalysisPROSITE-ProRule annotation1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P23837

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

    More...    PaxDbi    		P23837

    PRoteomics IDEntifications database

    More...    PRIDEi    		P23837

    <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

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    The phoP/phoQ operon is positively autoregulated by both PhoP and PhoQ in a Mg2+-dependent manner, inhibited at high Mg2+ concentrations (PubMed:10464230). Induced by dsbA disruption and dithiothreitol (PubMed:22267510).2 Publications

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer; probably dimerizes via the cytoplasmic domain (Probable). Probably interacts with MgrB in the periplasm, altering its activity and that of downstream effector PhoP.

    Curated3 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    P23837
    With#Exp.IntAct
    itself2EBI-1113605,EBI-1113605

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260662, 3 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-10501N

    Protein interaction database and analysis system

    More...    IntActi    		P23837, 2 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b1129

    <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

    1486
    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

    More...    SMRi    		P23837

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P23837

    <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%5Fand%5Fdomains%5Fsection">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>Domaini215 – 266HAMPPROSITE-ProRule annotationAdd BLAST52
    Domaini274 – 480Histidine kinasePROSITE-ProRule annotationAdd BLAST207

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG2205, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_000445_42_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P23837

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P23837

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.30.450.140, 1 hit
    3.30.565.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR003660, HAMP_dom
    IPR003594, HATPase_C
    IPR036890, HATPase_C_sf
    IPR005467, His_kinase_dom
    IPR036097, HisK_dim/P_sf
    IPR015014, PhoQ_Sensor
    IPR038429, PhoQ_Sensor_sf
    IPR004358, Sig_transdc_His_kin-like_C

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02518, HATPase_c, 1 hit
    PF08918, PhoQ_Sensor, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00344, BCTRLSENSOR

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00387, HATPase_c, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF47384, SSF47384, 1 hit
    SSF55874, SSF55874, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS50885, HAMP, 1 hit
    PS50109, HIS_KIN, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P23837-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKKLLRLFFP LSLRVRFLLA TAAVVLVLSL AYGMVALIGY SVSFDKTTFR 
            60         70         80         90        100
    LLRGESNLFY TLAKWENNKL HVELPENIDK QSPTMTLIYD ENGQLLWAQR 
           110        120        130        140        150
    DVPWLMKMIQ PDWLKSNGFH EIEADVNDTS LLLSGDHSIQ QQLQEVREDD 
           160        170        180        190        200
    DDAEMTHSVA VNVYPATSRM PKLTIVVVDT IPVELKSSYM VWSWFIYVLS 
           210        220        230        240        250
    ANLLLVIPLL WVAAWWSLRP IEALAKEVRE LEEHNRELLN PATTRELTSL 
           260        270        280        290        300
    VRNLNRLLKS ERERYDKYRT TLTDLTHSLK TPLAVLQSTL RSLRSEKMSV 
           310        320        330        340        350
    SDAEPVMLEQ ISRISQQIGY YLHRASMRGG TLLSRELHPV APLLDNLTSA 
           360        370        380        390        400
    LNKVYQRKGV NISLDISPEI SFVGEQNDFV EVMGNVLDNA CKYCLEFVEI 
           410        420        430        440        450
    SARQTDEHLY IVVEDDGPGI PLSKREVIFD RGQRVDTLRP GQGVGLAVAR 
           460        470        480 
    EITEQYEGKI VAGESMLGGA RMEVIFGRQH SAPKDE
    Length:486
    Mass (Da):55,300
    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:i89C6D97A3C9B8809
    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
    		D90393 Genomic DNA Translation: BAA14391.1
    U00096 Genomic DNA Translation: AAC74213.1
    AP009048 Genomic DNA Translation: BAA35951.1
    M81433 Genomic DNA No translation available.

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		B41966

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415647.1, NC_000913.3
    WP_000735412.1, NZ_STEB01000016.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC74213; AAC74213; b1129
    BAA35951; BAA35951; BAA35951

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		58461247
    946326

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW1115
    eco:b1129

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1137

    <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
    		D90393 Genomic DNA Translation: BAA14391.1
    U00096 Genomic DNA Translation: AAC74213.1
    AP009048 Genomic DNA Translation: BAA35951.1
    M81433 Genomic DNA No translation available.
    PIRiB41966
    RefSeqiNP_415647.1, NC_000913.3
    WP_000735412.1, NZ_STEB01000016.1

    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
    1ID0X-ray1.60A335-486[»]
    3BQ8X-ray2.50A/B43-190[»]
    3BQAX-ray2.00A/B43-190[»]
    6A8UX-ray1.85A/B43-190[»]
    6A8VX-ray2.70A/B43-190[»]
    SMRiP23837
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260662, 3 interactors
    DIPiDIP-10501N
    IntActiP23837, 2 interactors
    STRINGi511145.b1129

    Chemistry databases

    DrugBankiDB04395, Phosphoaminophosphonic Acid-Adenylate Ester

    Proteomic databases

    jPOSTiP23837
    PaxDbiP23837
    PRIDEiP23837

    Genome annotation databases

    EnsemblBacteriaiAAC74213; AAC74213; b1129
    BAA35951; BAA35951; BAA35951
    GeneIDi58461247
    946326
    KEGGiecj:JW1115
    eco:b1129
    PATRICifig|1411691.4.peg.1137

    Organism-specific databases

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

    More...    EchoBASEi    		EB0725

    Phylogenomic databases

    eggNOGiCOG2205, Bacteria
    HOGENOMiCLU_000445_42_0_6
    InParanoidiP23837
    PhylomeDBiP23837

    Enzyme and pathway databases

    BioCyciEcoCyc:PHOQ-MONOMER
    BRENDAi2.7.13.3, 2026
    SABIO-RKiP23837

    Miscellaneous databases

    EvolutionaryTraceiP23837

    Protein Ontology

    More...    PROi    		PR:P23837

    Family and domain databases

    Gene3Di3.30.450.140, 1 hit
    3.30.565.10, 1 hit
    InterProiView protein in InterPro
    IPR003660, HAMP_dom
    IPR003594, HATPase_C
    IPR036890, HATPase_C_sf
    IPR005467, His_kinase_dom
    IPR036097, HisK_dim/P_sf
    IPR015014, PhoQ_Sensor
    IPR038429, PhoQ_Sensor_sf
    IPR004358, Sig_transdc_His_kin-like_C
    PfamiView protein in Pfam
    PF02518, HATPase_c, 1 hit
    PF08918, PhoQ_Sensor, 1 hit
    PRINTSiPR00344, BCTRLSENSOR
    SMARTiView protein in SMART
    SM00387, HATPase_c, 1 hit
    SUPFAMiSSF47384, SSF47384, 1 hit
    SSF55874, SSF55874, 1 hit
    PROSITEiView protein in PROSITE
    PS50885, HAMP, 1 hit
    PS50109, HIS_KIN, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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 nameiPHOQ_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: P23837
    <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%5Fand%5Fisoforms">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: April 7, 2021
    This is version 199 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, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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