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O34507

- PRKC_BACSU

UniProt

O34507 - PRKC_BACSU

Protein

Serine/threonine-protein kinase PrkC

Gene

prkC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates FusA (EF-G, elongation factor G); the latter modification is likely necessary for germination in response to peptidoglycan. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests that they form a functional couple in vivo. Might also be involved in sporulation and biofilm formation. Does not seem to be involved in stress response.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Bryostatin activates PrkC activity and induces germination, whereas staurosporine inhibits PrkC and significantly reduced peptidoglycan-dependent germination.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401ATPPROSITE-ProRule annotation
    Sitei40 – 401Required for activity
    Active sitei134 – 1341Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 259ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. penicillin binding Source: InterPro
    3. peptidoglycan binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to peptidoglycan Source: UniProtKB
    2. protein phosphorylation Source: UniProtKB
    3. signal transduction Source: UniProtKB
    4. spore germination Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Germination

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU15770-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PrkC (EC:2.7.11.1)
    Short name:
    Ser/Thr-protein kinase PrkC
    Gene namesi
    Name:prkC
    Synonyms:yloP
    Ordered Locus Names:BSU15770
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU15770. [Micado]

    Subcellular locationi

    Spore core membrane 1 Publication; Single-pass type II membrane protein 1 Publication
    Note: Is associated with the inner membrane of the spore.

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Spores lacking this gene fail to germinate in the presence of peptidoglycan fragments or purified GlcNAc-MurNAc tripeptides and tetrapeptides. They still respond to the nutrient germinant L-alanine and to the chemical germinant Ca2+-dipicolinic acid, indicating that the spores are still capable of germinating and that PrkC is not involved in nutrient or chemical germination.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401K → A: Does not support germination in response to peptidoglycan. 2 Publications
    Mutagenesisi40 – 401K → R: Abolishes autophosphorylation and decreases spore production and biofilm formation. 2 Publications
    Mutagenesisi162 – 1621T → A: 4-fold reduction in activity. Abolished activity; when associated with A-163; A-165 and A-167. 1 Publication
    Mutagenesisi163 – 1631T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-165 and A-167. 1 Publication
    Mutagenesisi165 – 1651T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-163 and A-167. 1 Publication
    Mutagenesisi167 – 1671T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-163 and A-165. 1 Publication
    Mutagenesisi214 – 2141S → A: 4-fold reduction in activity. 1 Publication
    Mutagenesisi290 – 2901T → A: Slightly reduced activity. 1 Publication
    Mutagenesisi313 – 3131T → A: Unchanged activity. 1 Publication
    Mutagenesisi320 – 3201T → A: 2-fold reduction in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 648648Serine/threonine-protein kinase PrkCPRO_0000171183Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei162 – 1621Phosphothreonine; by autocatalysis2 Publications
    Modified residuei163 – 1631Phosphothreonine; by autocatalysis2 Publications
    Modified residuei165 – 1651Phosphothreonine; by autocatalysis2 Publications
    Modified residuei167 – 1671Phosphothreonine; by autocatalysis2 Publications
    Modified residuei214 – 2141Phosphoserine; by autocatalysis2 Publications
    Modified residuei290 – 2901Phosphothreonine; by autocatalysis3 Publications
    Modified residuei313 – 3131Phosphothreonine; by autocatalysis2 Publications
    Modified residuei320 – 3201Phosphothreonine; by autocatalysis2 Publications

    Post-translational modificationi

    Autophosphorylation on threonine residue(s) and serine residue considerably increases the kinase activity of the protein. Dephosphorylated in vitro by PrpC.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO34507.

    PTM databases

    PhosSiteiP0606169.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiO34507. 1 interaction.
    STRINGi224308.BSU15770.

    Structurei

    3D structure databases

    ProteinModelPortaliO34507.
    SMRiO34507. Positions 6-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 330330CytoplasmicCuratedAdd
    BLAST
    Topological domaini352 – 648297ExtracellularCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei331 – 35121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 271261Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini356 – 42469PASTA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini425 – 49268PASTA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini493 – 55967PASTA 3PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The C-terminal extracellular domain containing the PASTA repeats binds peptidoglycan.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 3 PASTA domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000037186.
    KOiK08884.
    OMAiMSKNPAN.
    OrthoDBiEOG6B35XT.
    PhylomeDBiO34507.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR005543. PASTA_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF03793. PASTA. 3 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00740. PASTA. 3 hits.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51178. PASTA. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O34507-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLIGKRISGR YQILRVIGGG GMANVYLAED IILDREVAIK ILRFDYANDN    50
    EFIRRFRREA QSASSLDHPN IVSIYDLGEE DDIYYIVMEY VEGMTLKEYI 100
    TANGPLHPKE ALNIMEQIVS AIAHAHQNQI VHRDIKPHNI LIDHMGNIKV 150
    TDFGIATALS STTITHTNSV LGSVHYLSPE QARGGLATKK SDIYALGIVL 200
    FELLTGRIPF DGESAVSIAL KHLQAETPSA KRWNPSVPQS VENIILKATA 250
    KDPFHRYETA EDMEADIKTA FDADRLNEKR FTIQEDEEMT KAIPIIKDEE 300
    LAKAAGEKEA EVTTAQENKT KKNGKRKKWP WVLLTICLVF ITAGILAVTV 350
    FPSLFMPKDV KIPDVSGMEY EKAAGLLEKE GLQVDSEVLE ISDEKIEEGL 400
    MVKTDPKADT TVKEGATVTL YKSTGKAKTE IGDVTGQTVD QAKKALKDQG 450
    FNHVTVNEVN DEKNAGTVID QNPSAGTELV PSEDQVKLTV SIGPEDITLR 500
    DLKTYSKEAA SGYLEDNGLK LVEKEAYSDD VPEGQVVKQK PAAGTAVKPG 550
    NEVEVTFSLG PEKKPAKTVK EKVKIPYEPE NEGDELQVQI AVDDADHSIS 600
    DTYEEFKIKE PTERTIELKI EPGQKGYYQV MVNNKVVSYK TIEYPKDE 648
    Length:648
    Mass (Da):71,866
    Last modified:January 1, 1998 - v1
    Checksum:i9653AB5CFBAA7900
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13937 Genomic DNA. Translation: CAA74267.1.
    AL009126 Genomic DNA. Translation: CAB13450.1.
    PIRiH69878.
    RefSeqiNP_389459.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13450; CAB13450; BSU15770.
    GeneIDi936132.
    KEGGibsu:BSU15770.
    PATRICi18974961. VBIBacSub10457_1672.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13937 Genomic DNA. Translation: CAA74267.1 .
    AL009126 Genomic DNA. Translation: CAB13450.1 .
    PIRi H69878.
    RefSeqi NP_389459.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O34507.
    SMRi O34507. Positions 6-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O34507. 1 interaction.
    STRINGi 224308.BSU15770.

    PTM databases

    PhosSitei P0606169.

    Proteomic databases

    PaxDbi O34507.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13450 ; CAB13450 ; BSU15770 .
    GeneIDi 936132.
    KEGGi bsu:BSU15770.
    PATRICi 18974961. VBIBacSub10457_1672.

    Organism-specific databases

    GenoListi BSU15770. [Micado ]

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000037186.
    KOi K08884.
    OMAi MSKNPAN.
    OrthoDBi EOG6B35XT.
    PhylomeDBi O34507.

    Enzyme and pathway databases

    BioCyci BSUB:BSU15770-MONOMER.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR005543. PASTA_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF03793. PASTA. 3 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00740. PASTA. 3 hits.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51178. PASTA. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence of a 28 Kbp seqment of DNA from the spoVM region of Bacillus subtilis."
      Foulger D., Errington J.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells."
      Gaidenko T.A., Kim T.-J., Price C.W.
      J. Bacteriol. 184:6109-6114(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
    4. "Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes."
      Madec E., Laszkiewicz A., Iwanicki A., Obuchowski M., Seror S.
      Mol. Microbiol. 46:571-586(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, PHOSPHORYLATION, MUTAGENESIS OF LYS-40.
      Strain: 168.
    5. "Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis."
      Madec E., Stensballe A., Kjellstrom S., Cladiere L., Obuchowski M., Jensen O.N., Seror S.J.
      J. Mol. Biol. 330:459-472(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-162; THR-163; THR-165; THR-167; SER-214; THR-290; THR-313 AND THR-320, MUTAGENESIS OF THR-162; THR-163; THR-165; THR-167; SER-214; THR-290; THR-313 AND THR-320, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
      Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
      Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-290, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.
    7. "A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments."
      Shah I.M., Laaberki M.H., Popham D.L., Dworkin J.
      Cell 135:486-496(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PEPTIDOGLYCAN-DEPENDENT GERMINATION, DISRUPTION PHENOTYPE, PEPTIDOGLYCAN-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-40.
      Strain: 168 / PY79.
    8. "Theoretical modeling of PrkCc, serine-threonine protein kinase intracellular domain, complexed with ATP derivatives."
      Gruszczyski P., Kamierkiewicz R., Obuchowski M., Lammek B.
      QSAR Comb. Sci. 27:437-444(2008)
      Cited for: 3D-STRUCTURE MODELING OF 6-269 IN COMPLEX WITH ATP ANALOGS.
    9. "Phosphorylation and ATP-binding induced conformational changes in the PrkC, Ser/Thr kinase from B. subtilis."
      Gruszczynski P., Obuchowski M., Kazmierkiewicz R.
      J. Comput. Aided Mol. Des. 24:733-747(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.

    Entry informationi

    Entry nameiPRKC_BACSU
    AccessioniPrimary (citable) accession number: O34507
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2003
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    PubMed:18984160 shows that peptidoglycan fragments serve as a novel mechanism of interspecies bacterial signaling that likely indicates the presence of growing bacteria and thus serve as a signal for dormant cells that growth-promoting conditions exist.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3