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O34507

- PRKC_BACSU

UniProt

O34507 - PRKC_BACSU

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Protein
Serine/threonine-protein kinase PrkC
Gene
prkC, yloP, BSU15770
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 401ATP By similarity
Sitei40 – 401Required for activity
Active sitei134 – 1341Proton acceptor By similarity

Regions

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

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
Complete GO annotation...

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 330330Cytoplasmic Inferred
Add
BLAST
Transmembranei331 – 35121Helical; Reviewed prediction
Add
BLAST
Topological domaini352 – 648297Extracellular Inferred
Add
BLAST

GO - Cellular componenti

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

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 PrkC
PRO_0000171183Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621Phosphothreonine; by autocatalysis1 Publication
Modified residuei163 – 1631Phosphothreonine; by autocatalysis1 Publication
Modified residuei165 – 1651Phosphothreonine; by autocatalysis1 Publication
Modified residuei167 – 1671Phosphothreonine; by autocatalysis1 Publication
Modified residuei214 – 2141Phosphoserine; by autocatalysis1 Publication
Modified residuei290 – 2901Phosphothreonine; by autocatalysis2 Publications
Modified residuei313 – 3131Phosphothreonine; by autocatalysis1 Publication
Modified residuei320 – 3201Phosphothreonine; by autocatalysis1 Publication

Post-translational modificationi

Autophosphorylation on threonine residue(s) and serine residue considerably increases the kinase activity of the protein. Dephosphorylated in vitro by PrpC.2 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 271261Protein kinase
Add
BLAST
Domaini356 – 42469PASTA 1
Add
BLAST
Domaini425 – 49268PASTA 2
Add
BLAST
Domaini493 – 55967PASTA 3
Add
BLAST

Domaini

The C-terminal extracellular domain containing the PASTA repeats binds peptidoglycan.1 Publication

Sequence similaritiesi

Contains 3 PASTA domains.

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

1 Publication 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

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