Sporulation kinase A

<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

<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

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

<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

• ATP binding Source: UniProtKB-KW
• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "The histidine kinase inhibitor Sda binds near the site of autophosphorylation and may sterically hinder autophosphorylation and phosphotransfer to Spo0F."
    Cunningham K.A., Burkholder W.F.
    Mol. Microbiol. 71:659-677(2009) [PubMed] [Europe PMC] [Abstract]
  • "In vivo domain-based functional analysis of the major sporulation sensor kinase, KinA, in Bacillus subtilis."
    Eswaramoorthy P., Guo T., Fujita M.
    J. Bacteriol. 191:5358-5368(2009) [PubMed] [Europe PMC] [Abstract]
  • "Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis."
    Dago A.E., Schug A., Procaccini A., Hoch J.A., Weigt M., Szurmant H.
    Proc. Natl. Acad. Sci. U.S.A. 109:E1733-42(2012) [PubMed] [Europe PMC] [Abstract]
• phosphorelay sensor kinase activity Source: InterPro

GO - Biological processⁱ

• positive regulation of sporulation Source: CACAO <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "AbrB and Spo0E control the proper timing of sporulation in Bacillus subtilis."
    Shafikhani S.H., Leighton T.
    Curr. Microbiol. 48:262-269(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of transcription, DNA-templated Source: InterPro
• sporulation resulting in formation of a cellular spore Source: CACAO <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A."
    Fujita M., Losick R.
    Genes Dev. 19:2236-2244(2005) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

<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 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

Chemistry databases

<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

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

<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%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

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "The histidine kinase inhibitor Sda binds near the site of autophosphorylation and may sterically hinder autophosphorylation and phosphotransfer to Spo0F."
    Cunningham K.A., Burkholder W.F.
    Mol. Microbiol. 71:659-677(2009) [PubMed] [Europe PMC] [Abstract]
  • "In vivo domain-based functional analysis of the major sporulation sensor kinase, KinA, in Bacillus subtilis."
    Eswaramoorthy P., Guo T., Fujita M.
    J. Bacteriol. 191:5358-5368(2009) [PubMed] [Europe PMC] [Abstract]
  • "Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis."
    Dago A.E., Schug A., Procaccini A., Hoch J.A., Weigt M., Szurmant H.
    Proc. Natl. Acad. Sci. U.S.A. 109:E1733-42(2012) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<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.

        10         20         30         40         50
MEQDTQHVKP LQTKTDIHAV LASNGRIIYI SANSKLHLGY LQGEMIGSFL 
        60         70         80         90        100
KTFLHEEDQF LVESYFYNEH HLMPCTFRFI KKDHTIVWVE AAVEIVTTRA 
       110        120        130        140        150
ERTEREIILK MKVLEEETGH QSLNCEKHEI EPASPESTTY ITDDYERLVE 
       160        170        180        190        200
NLPSPLCISV KGKIVYVNSA MLSMLGAKSK DAIIGKSSYE FIEEEYHDIV 
       210        220        230        240        250
KNRIIRMQKG MEVGMIEQTW KRLDGTPVHL EVKASPTVYK NQQAELLLLI 
       260        270        280        290        300
DISSRKKFQT ILQKSRERYQ LLIQNSIDTI AVIHNGKWVF MNESGISLFE 
       310        320        330        340        350
AATYEDLIGK NIYDQLHPCD HEDVKERIQN IAEQKTESEI VKQSWFTFQN 
       360        370        380        390        400
RVIYTEMVCI PTTFFGEAAV QVILRDISER KQTEELMLKS EKLSIAGQLA 
       410        420        430        440        450
AGIAHEIRNP LTAIKGFLQL MKPTMEGNEH YFDIVFSELS RIELILSELL 
       460        470        480        490        500
MLAKPQQNAV KEYLNLKKLI GEVSALLETQ ANLNGIFIRT SYEKDSIYIN 
       510        520        530        540        550
GDQNQLKQVF INLIKNAVES MPDGGTVDII ITEDEHSVHV TVKDEGEGIP 
       560        570        580        590        600
EKVLNRIGEP FLTTKEKGTG LGLMVTFNII ENHQGVIHVD SHPEKGTAFK 

ISFPKK                                                 

Experimental Info

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. Bacillus subtilis
   Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList