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O34507 (PRKC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PrkC

Short name=Ser/Thr-protein kinase PrkC
EC=2.7.11.1
Gene names
Name:prkC
Synonyms:yloP
Ordered Locus Names:BSU15770
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length648 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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

Subunit structure

Homodimer. Ref.4

Subcellular location

Spore core membrane; Single-pass type II membrane protein. Note: Is associated with the inner membrane of the spore. Ref.7

Domain

The C-terminal extracellular domain containing the PASTA repeats binds peptidoglycan. Ref.9

Post-translational modification

Autophosphorylation on threonine residue(s) and serine residue considerably increases the kinase activity of the protein. Dephosphorylated in vitro by PrpC. Ref.4 Ref.5

Disruption phenotype

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. Ref.7

Miscellaneous

Ref.7 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.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 3 PASTA domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 648648Serine/threonine-protein kinase PrkC
PRO_0000171183

Regions

Topological domain1 – 330330Cytoplasmic Probable
Transmembrane331 – 35121Helical; Potential
Topological domain352 – 648297Extracellular Probable
Domain11 – 271261Protein kinase
Domain356 – 42469PASTA 1
Domain425 – 49268PASTA 2
Domain493 – 55967PASTA 3
Nucleotide binding17 – 259ATP Probable

Sites

Active site1341Proton acceptor By similarity
Binding site401ATP By similarity
Site401Required for activity

Amino acid modifications

Modified residue1621Phosphothreonine; by autocatalysis Ref.5
Modified residue1631Phosphothreonine; by autocatalysis Ref.5
Modified residue1651Phosphothreonine; by autocatalysis Ref.5
Modified residue1671Phosphothreonine; by autocatalysis Ref.5
Modified residue2141Phosphoserine; by autocatalysis Ref.5
Modified residue2901Phosphothreonine; by autocatalysis Ref.5 Ref.6
Modified residue3131Phosphothreonine; by autocatalysis Ref.5
Modified residue3201Phosphothreonine; by autocatalysis Ref.5

Experimental info

Mutagenesis401K → A: Does not support germination in response to peptidoglycan. Ref.4 Ref.7
Mutagenesis401K → R: Abolishes autophosphorylation and decreases spore production and biofilm formation. Ref.4 Ref.7
Mutagenesis1621T → A: 4-fold reduction in activity. Abolished activity; when associated with A-163; A-165 and A-167. Ref.5
Mutagenesis1631T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-165 and A-167. Ref.5
Mutagenesis1651T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-163 and A-167. Ref.5
Mutagenesis1671T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-163 and A-165. Ref.5
Mutagenesis2141S → A: 4-fold reduction in activity. Ref.5
Mutagenesis2901T → A: Slightly reduced activity. Ref.5
Mutagenesis3131T → A: Unchanged activity. Ref.5
Mutagenesis3201T → A: 2-fold reduction in activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O34507 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9653AB5CFBAA7900

FASTA64871,866
        10         20         30         40         50         60 
MLIGKRISGR YQILRVIGGG GMANVYLAED IILDREVAIK ILRFDYANDN EFIRRFRREA 

        70         80         90        100        110        120 
QSASSLDHPN IVSIYDLGEE DDIYYIVMEY VEGMTLKEYI TANGPLHPKE ALNIMEQIVS 

       130        140        150        160        170        180 
AIAHAHQNQI VHRDIKPHNI LIDHMGNIKV TDFGIATALS STTITHTNSV LGSVHYLSPE 

       190        200        210        220        230        240 
QARGGLATKK SDIYALGIVL FELLTGRIPF DGESAVSIAL KHLQAETPSA KRWNPSVPQS 

       250        260        270        280        290        300 
VENIILKATA KDPFHRYETA EDMEADIKTA FDADRLNEKR FTIQEDEEMT KAIPIIKDEE 

       310        320        330        340        350        360 
LAKAAGEKEA EVTTAQENKT KKNGKRKKWP WVLLTICLVF ITAGILAVTV FPSLFMPKDV 

       370        380        390        400        410        420 
KIPDVSGMEY EKAAGLLEKE GLQVDSEVLE ISDEKIEEGL MVKTDPKADT TVKEGATVTL 

       430        440        450        460        470        480 
YKSTGKAKTE IGDVTGQTVD QAKKALKDQG FNHVTVNEVN DEKNAGTVID QNPSAGTELV 

       490        500        510        520        530        540 
PSEDQVKLTV SIGPEDITLR DLKTYSKEAA SGYLEDNGLK LVEKEAYSDD VPEGQVVKQK 

       550        560        570        580        590        600 
PAAGTAVKPG NEVEVTFSLG PEKKPAKTVK EKVKIPYEPE NEGDELQVQI AVDDADHSIS 

       610        620        630        640 
DTYEEFKIKE PTERTIELKI EPGQKGYYQV MVNNKVVSYK TIEYPKDE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13937 Genomic DNA. Translation: CAA74267.1.
AL009126 Genomic DNA. Translation: CAB13450.1.
PIRH69878.
RefSeqNP_389459.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34507.
SMRO34507. Positions 6-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO34507. 1 interaction.
STRING224308.BSU15770.

PTM databases

PhosSiteP0606169.

Proteomic databases

PaxDbO34507.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13450; CAB13450; BSU15770.
GeneID936132.
KEGGbsu:BSU15770.
PATRIC18974961. VBIBacSub10457_1672.

Organism-specific databases

GenoListBSU15770. [Micado]

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000037186.
KOK08884.
OMATGKDPGT.
OrthoDBEOG6B35XT.
ProtClustDBCLSK2301459.

Enzyme and pathway databases

BioCycBSUB:BSU15770-MONOMER.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR005543. PASTA.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF03793. PASTA. 3 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00740. PASTA. 3 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51178. PASTA. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRKC_BACSU
AccessionPrimary (citable) accession number: O34507
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList