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Entry version 145 (10 Apr 2019)
Sequence version 3 (23 Jan 2007)
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Protein

HPr kinase/phosphorylase

Gene

hprK

Organism
Bacillus subtilis (strain 168)
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

Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-45' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on 'Ser-46'. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.1 Publication

Miscellaneous

Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions.
According to PubMed:12779331, the mutation G152A reduces the kinase activity about twofold and has little effect on phosphorylase activity, whereas according to PubMed:12055300, it completely prevents both functions. This conflicting result may be explained by limiting amounts substrates conditions used in PubMed:12779331 assays.

Caution

Was originally called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was found to follow a quite unique mechanism (PubMed:12359880), in which Pi instead of H2O is used for the nucleophilic attack on the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not a phosphohydrolysis but a phosphophosphorolysis reaction, and the bifunctional enzyme was dubbed HPr kinase/phosphorylase.1 Publication

<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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication, Ca2+1 PublicationNote: The enzyme may harbor two different cation-binding sites, one that interacts specifically with the nucleotide, and the other that is involved in the binding of the protein substrate.1 Publication

<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

Is active as a kinase only at high ATP concentrations or at low ATP concentrations in the presence of the allosteric activator fructose 1,6-bisphosphate (FBP). The pyrophosphate-dependent HPr phosphorylation is not stimulated by FBP. Kinase activity is inhibited by inorganic phosphate (Pi). Dephosphorylation of HPr(Ser-P) by B.subtilis HPrK/P becomes prevalent when the concentration of Pi increases. Thus, the kinase activity may prevail under conditions of good nutrient supply, whereas the phosphorylase activity is dominant if carbon and energy sources become limiting.

<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=78 µM for HPr
  2. KM=85 µM for P-Ser-HPr
  3. KM=265 µM for phosphate
  4. KM=785 µM for pyrophosphate

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi138MagnesiumSequence analysis1
    <p>This subsection of the ‘Function’ 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 sitei159By similarity1
    Metal bindingi160MagnesiumCurated1
    Active sitei177Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activityBy similarity1
    Metal bindingi202MagnesiumCurated1
    Active sitei243By similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi153 – 160ATPCurated8

    <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 functionAllosteric enzyme, Kinase, Multifunctional enzyme, Serine/threonine-protein kinase, Transferase
    Biological processCarbohydrate metabolism
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    BSUB:BSU35000-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    O34483

    <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:
    HPr kinase/phosphorylase (EC:2.7.11.-, EC:2.7.4.-)
    Short name:
    HPrK/P
    Alternative name(s):
    HPr kinase/phosphatase
    HPr(Ser) kinase/phosphorylase
    <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:hprK
    Synonyms:ptsK, yvoB
    Ordered Locus Names:BSU35000
    <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>OrganismiBacillus subtilis (strain 168)
    <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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    <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
    • UP000001570 <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

    <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

    • cytosol Source: GO_Central

    <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_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>Mutagenesisi138H → A: No effect on both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi148G → A: Loss of both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi153G → A: Loss of both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi155S → A or T: Nearly no effect on both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi155S → C: Loss of both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi156G → A: Loss of both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi158G → A: Loss of both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi159K → R: Slight reduction in both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi160S → A: Loss of both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi160S → T: Nearly no effect on both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi171H → R: Loss of both kinase and phosphorylase activities. 1 Publication1
    Mutagenesisi202E → A: No effect on ATP-dependent kinase activity, but loss of both PPi-kinase and phosphorylase activities. 1
    Mutagenesisi204R → A: Reduced kinase activity and loss of phosphorylase activity. 1
    Mutagenesisi205G → A: No effect on ATP-dependent kinase activity, but loss of both PPi-kinase and phosphorylase activities. 1
    Mutagenesisi207G → A: Reduced kinase activity and loss of phosphorylase activity. No effect on FBP binding. 1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4974

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00000589462 – 310HPr kinase/phosphorylaseAdd BLAST309

    Proteomic databases

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

    More...
    PaxDbi
    O34483

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O34483

    <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

    Constitutively expressed, with or without glucose in the growth medium.1 Publication

    <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

    Homohexamer.

    <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

    Protein interaction database and analysis system

    More...
    IntActi
    O34483, 6 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    224308.BSU35000

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    O34483

    <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

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    O34483

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

    More...
    SMRi
    O34483

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni201 – 210Important for the catalytic mechanism of both phosphorylation and dephosphorylation10
    Regioni264 – 269Important for the catalytic mechanism of dephosphorylationBy similarity6

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The Walker A ATP-binding motif also binds Pi and PPi.

    <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 HPrK/P family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105D1C Bacteria
    COG1493 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000099173

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O34483

    KEGG Orthology (KO)

    More...
    KOi
    K06023

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    IQKPGLA

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    O34483

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01918 HprK_C, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.1390.20, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01249 HPr_kinase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003755 HPr(Ser)_kin/Pase
    IPR011104 Hpr_kin/Pase_C
    IPR011126 Hpr_kin/Pase_Hpr_N
    IPR028979 Ser_kin/Pase_Hpr-like_N_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR30305:SF1 PTHR30305:SF1, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07475 Hpr_kinase_C, 1 hit
    PF02603 Hpr_kinase_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF75138 SSF75138, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00679 hpr-ser, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    O34483-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAKVRTKDVM EQFNLELISG EEGINRPITM SDLSRPGIEI AGYFTYYPRE
    60 70 80 90 100
    RVQLLGKTEL SFFEQLPEEE KKQRMDSLCT DVTPAIILSR DMPIPQELID
    110 120 130 140 150
    ASEKNGVPVL RSPLKTTRLS SRLTNFLESR LAPTTAIHGV LVDIYGVGVL
    160 170 180 190 200
    ITGKSGVGKS ETALELVKRG HRLVADDCVE IRQEDQDTLV GNAPELIEHL
    210 220 230 240 250
    LEIRGLGIIN VMTLFGAGAV RSNKRITIVM NLELWEQGKQ YDRLGLEEET
    260 270 280 290 300
    MKIIDTEITK LTIPVRPGRN LAVIIEVAAM NFRLKRMGLN AAEQFTNKLA
    310
    DVIEDGEQEE
    Length:310
    Mass (Da):34,702
    Last modified:January 23, 2007 - v3
    <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:iC44ABD220881EC31
    GO

    <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 34529 Da from positions 2 - 310. Determined by MALDI. 1 Publication

    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
    AF017113 Genomic DNA Translation: AAC67286.1
    AL009126 Genomic DNA Translation: CAB15505.1
    U63310 Genomic DNA Translation: AAD09500.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E70044

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_391380.1, NC_000964.3
    WP_003228097.1, NZ_JNCM01000033.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAB15505; CAB15505; BSU35000

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    936615

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bsu:BSU35000

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|224308.179.peg.3788

    <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
    AF017113 Genomic DNA Translation: AAC67286.1
    AL009126 Genomic DNA Translation: CAB15505.1
    U63310 Genomic DNA Translation: AAD09500.1
    PIRiE70044
    RefSeqiNP_391380.1, NC_000964.3
    WP_003228097.1, NZ_JNCM01000033.1

    3D structure databases

    ProteinModelPortaliO34483
    SMRiO34483
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiO34483, 6 interactors
    STRINGi224308.BSU35000

    Chemistry databases

    BindingDBiO34483
    ChEMBLiCHEMBL4974

    Proteomic databases

    PaxDbiO34483
    PRIDEiO34483

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB15505; CAB15505; BSU35000
    GeneIDi936615
    KEGGibsu:BSU35000
    PATRICifig|224308.179.peg.3788

    Phylogenomic databases

    eggNOGiENOG4105D1C Bacteria
    COG1493 LUCA
    HOGENOMiHOG000099173
    InParanoidiO34483
    KOiK06023
    OMAiIQKPGLA
    PhylomeDBiO34483

    Enzyme and pathway databases

    BioCyciBSUB:BSU35000-MONOMER
    SABIO-RKiO34483

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:O34483

    Family and domain databases

    CDDicd01918 HprK_C, 1 hit
    Gene3Di3.40.1390.20, 1 hit
    HAMAPiMF_01249 HPr_kinase, 1 hit
    InterProiView protein in InterPro
    IPR003755 HPr(Ser)_kin/Pase
    IPR011104 Hpr_kin/Pase_C
    IPR011126 Hpr_kin/Pase_Hpr_N
    IPR028979 Ser_kin/Pase_Hpr-like_N_sf
    PANTHERiPTHR30305:SF1 PTHR30305:SF1, 1 hit
    PfamiView protein in Pfam
    PF07475 Hpr_kinase_C, 1 hit
    PF02603 Hpr_kinase_N, 1 hit
    SUPFAMiSSF75138 SSF75138, 1 hit
    TIGRFAMsiTIGR00679 hpr-ser, 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 nameiHPRK_BACSU
    <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: O34483
    Secondary accession number(s): Q9R9E3
    <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: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: April 10, 2019
    This is version 145 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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