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Protein

Serine/threonine-protein kinase PrkC

Gene

prkC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei40ATPPROSITE-ProRule annotation1
Sitei40Required for activity1
Active sitei134Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 25ATPCurated9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • peptidoglycan binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • cellular response to peptidoglycan Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • signal transduction Source: UniProtKB
  • 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
Proteomesi
  • UP000001570 Componenti: Chromosome

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.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 330CytoplasmicCuratedAdd BLAST330
Transmembranei331 – 351HelicalSequence analysisAdd BLAST21
Topological domaini352 – 648ExtracellularCuratedAdd BLAST297

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi40K → A: Does not support germination in response to peptidoglycan. 2 Publications1
Mutagenesisi40K → R: Abolishes autophosphorylation and decreases spore production and biofilm formation. 2 Publications1
Mutagenesisi162T → A: 4-fold reduction in activity. Abolished activity; when associated with A-163; A-165 and A-167. 1 Publication1
Mutagenesisi163T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-165 and A-167. 1 Publication1
Mutagenesisi165T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-163 and A-167. 1 Publication1
Mutagenesisi167T → A: 4-fold reduction in activity. Abolished activity; when associated with A-162; A-163 and A-165. 1 Publication1
Mutagenesisi214S → A: 4-fold reduction in activity. 1 Publication1
Mutagenesisi290T → A: Slightly reduced activity. 1 Publication1
Mutagenesisi313T → A: Unchanged activity. 1 Publication1
Mutagenesisi320T → A: 2-fold reduction in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001711831 – 648Serine/threonine-protein kinase PrkCAdd BLAST648

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei162Phosphothreonine; by autocatalysis1 Publication1
Modified residuei163Phosphothreonine; by autocatalysis1 Publication1
Modified residuei165Phosphothreonine; by autocatalysis1 Publication1
Modified residuei167Phosphothreonine; by autocatalysis1 Publication1
Modified residuei214Phosphoserine; by autocatalysis1 Publication1
Modified residuei290Phosphothreonine; by autocatalysis2 Publications1
Modified residuei313Phosphothreonine; by autocatalysis1 Publication1
Modified residuei320Phosphothreonine; by autocatalysis1 Publication1

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

iPTMnetiO34507.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
yabTP375622EBI-6667154,EBI-9303331
ybdMO314353EBI-6667154,EBI-5255200
ywqDP967162EBI-6667154,EBI-9302929

Protein-protein interaction databases

IntActiO34507. 8 interactors.
STRINGi224308.Bsubs1_010100008706.

Structurei

3D structure databases

ProteinModelPortaliO34507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 271Protein kinasePROSITE-ProRule annotationAdd BLAST261
Domaini356 – 424PASTA 1PROSITE-ProRule annotationAdd BLAST69
Domaini425 – 492PASTA 2PROSITE-ProRule annotationAdd BLAST68
Domaini493 – 559PASTA 3PROSITE-ProRule annotationAdd BLAST67

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

eggNOGiENOG4105D9P. Bacteria.
COG0515. LUCA.
COG2815. LUCA.
HOGENOMiHOG000037186.
InParanoidiO34507.
KOiK12132.
OMAiIRMYIND.
PhylomeDBiO34507.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR005543. PASTA_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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

        10         20         30         40         50
MLIGKRISGR YQILRVIGGG GMANVYLAED IILDREVAIK ILRFDYANDN
60 70 80 90 100
EFIRRFRREA QSASSLDHPN IVSIYDLGEE DDIYYIVMEY VEGMTLKEYI
110 120 130 140 150
TANGPLHPKE ALNIMEQIVS AIAHAHQNQI VHRDIKPHNI LIDHMGNIKV
160 170 180 190 200
TDFGIATALS STTITHTNSV LGSVHYLSPE QARGGLATKK SDIYALGIVL
210 220 230 240 250
FELLTGRIPF DGESAVSIAL KHLQAETPSA KRWNPSVPQS VENIILKATA
260 270 280 290 300
KDPFHRYETA EDMEADIKTA FDADRLNEKR FTIQEDEEMT KAIPIIKDEE
310 320 330 340 350
LAKAAGEKEA EVTTAQENKT KKNGKRKKWP WVLLTICLVF ITAGILAVTV
360 370 380 390 400
FPSLFMPKDV KIPDVSGMEY EKAAGLLEKE GLQVDSEVLE ISDEKIEEGL
410 420 430 440 450
MVKTDPKADT TVKEGATVTL YKSTGKAKTE IGDVTGQTVD QAKKALKDQG
460 470 480 490 500
FNHVTVNEVN DEKNAGTVID QNPSAGTELV PSEDQVKLTV SIGPEDITLR
510 520 530 540 550
DLKTYSKEAA SGYLEDNGLK LVEKEAYSDD VPEGQVVKQK PAAGTAVKPG
560 570 580 590 600
NEVEVTFSLG PEKKPAKTVK EKVKIPYEPE NEGDELQVQI AVDDADHSIS
610 620 630 640
DTYEEFKIKE PTERTIELKI EPGQKGYYQV MVNNKVVSYK TIEYPKDE
Length:648
Mass (Da):71,866
Last modified:January 1, 1998 - v1
Checksum:i9653AB5CFBAA7900
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13937 Genomic DNA. Translation: CAA74267.1.
AL009126 Genomic DNA. Translation: CAB13450.1.
PIRiH69878.
RefSeqiNP_389459.1. NC_000964.3.
WP_003232062.1. NZ_JNCM01000035.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13937 Genomic DNA. Translation: CAA74267.1.
AL009126 Genomic DNA. Translation: CAB13450.1.
PIRiH69878.
RefSeqiNP_389459.1. NC_000964.3.
WP_003232062.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO34507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO34507. 8 interactors.
STRINGi224308.Bsubs1_010100008706.

PTM databases

iPTMnetiO34507.

Proteomic databases

PaxDbiO34507.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105D9P. Bacteria.
COG0515. LUCA.
COG2815. LUCA.
HOGENOMiHOG000037186.
InParanoidiO34507.
KOiK12132.
OMAiIRMYIND.
PhylomeDBiO34507.

Enzyme and pathway databases

BioCyciBSUB:BSU15770-MONOMER.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR005543. PASTA_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

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 5, 2016
This is version 125 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.