Serine/threonine-protein kinase PrkC - Bacillus subtilis (strain 168)

Preferred order of sections

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length	648 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Germination
Cellular component	Membrane
Domain	Repeat Signal-anchor Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to peptidoglycan Inferred from mutant phenotype Ref.7. Source: UniProtKB signal transduction Inferred from mutant phenotype Ref.7. Source: UniProtKB spore germination Inferred from mutant phenotype Ref.7. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW penicillin binding Inferred from electronic annotation. Source: InterPro peptidoglycan binding Inferred from direct assay Ref.7. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 648

648

Serine/threonine-protein kinase PrkC

PRO_0000171183

Regions

Topological domain

1 – 330

330

Cytoplasmic Probable

Transmembrane

331 – 351

21

Helical; Potential

Topological domain

352 – 648

297

Extracellular Probable

Domain

11 – 271

261

Protein kinase

Domain

356 – 424

69

PASTA 1

Domain

425 – 492

68

PASTA 2

Domain

493 – 559

67

PASTA 3

Nucleotide binding

17 – 25

9

ATP Probable

Sites

Active site

134

1

Proton acceptor By similarity

Binding site

40

1

ATP By similarity

Site

40

1

Required for activity

Amino acid modifications

Modified residue

162

1

Phosphothreonine; by autocatalysis Ref.5

Modified residue

163

1

Phosphothreonine; by autocatalysis Ref.5

Modified residue

165

1

Phosphothreonine; by autocatalysis Ref.5

Modified residue

167

1

Phosphothreonine; by autocatalysis Ref.5

Modified residue

214

1

Phosphoserine; by autocatalysis Ref.5

Modified residue

290

1

Phosphothreonine; by autocatalysis Ref.5 Ref.6

Modified residue

313

1

Phosphothreonine; by autocatalysis Ref.5

Modified residue

320

1

Phosphothreonine; by autocatalysis Ref.5

Experimental info

Mutagenesis

40

1

K → A: Does not support germination in response to peptidoglycan. Ref.4 Ref.7

Mutagenesis

40

1

K → R: Abolishes autophosphorylation and decreases spore production and biofilm formation. Ref.4 Ref.7

Mutagenesis

162

1

T → A: 4-fold reduction in activity. Abolished activity; when associated with A-163; A-165 and A-167. Ref.5

Mutagenesis

163

1

T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-165 and A-167. Ref.5

Mutagenesis

165

1

T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-163 and A-167. Ref.5

Mutagenesis

167

1

T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-163 and A-165. Ref.5

Mutagenesis

214

1

S → A: 4-fold reduction in activity. Ref.5

Mutagenesis

290

1

T → A: Slightly reduced activity. Ref.5

Mutagenesis

313

1

T → A: Unchanged activity. Ref.5

Mutagenesis

320

1

T → A: 2-fold reduction in activity. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

O34507 [UniParc].

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

648

71,866

        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

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References

	« Hide 'large scale' referencesShow '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. 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, 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, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y13937 Genomic DNA. Translation: CAA74267.1. AL009126 Genomic DNA. Translation: CAB13450.1.
PIR	H69878.
RefSeq	NP_389459.1. NC_000964.3.
3D structure databases
ProteinModelPortal	O34507.
SMR	O34507. Positions 6-277.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU15770.
PTM databases
PhosSite	P0606169.
Proteomic databases
PaxDb	O34507.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB13450; CAB13450; BSU15770.
GeneID	936132.
KEGG	bsu:BSU15770.
PATRIC	18974961. VBIBacSub10457_1672.
Organism-specific databases
GenoList	BSU15770. [Micado]
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000037186.
KO	K08884.
OMA	TGKDPGT.
ProtClustDB	CLSK2301459.
Enzyme and pathway databases
BioCyc	BSUB:BSU15770-MONOMER.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR005543. PASTA. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF03793. PASTA. 3 hits. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00740. PASTA. 3 hits. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51178. PASTA. 3 hits. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRKC_BACSU

Accession

Primary (citable) accession number: O34507

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2003
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents