| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein kinase PrkC |
Protein Synonyms/Alias | Ser/Thr-protein kinase PrkC |
Gene Name | prkC |
Gene Synonyms/Alias | yloP; OrderedLocusNames=BSU15770 |
Created Date | 3-June-2014 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Phosphorylation | Position | Peptide | Code | Type | References | | 320 | TTAQENKTKKNGKRK | T | HTP | [1],UniProt | | 214 | RIPFDGESAVSIALK | S | HTP | [1],UniProt | | 167 | SSTTITHTNSVLGSV | T | HTP | [1],UniProt | | 163 | ATALSSTTITHTNSV | T | HTP | [1],UniProt | | 165 | ALSSTTITHTNSVLG | T | HTP | [1],UniProt | | 290 | IQEDEEMTKAIPIIK | T | HTP | [1],UniProt | | 313 | GEKEAEVTTAQENKT | T | HTP | [1],UniProt | | 162 | IATALSSTTITHTNS | T | HTP | [1],UniProt | |
Reference | [1]The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Macek B,Mijakovic I,Olsen JV,Gnad F,Kumar C,Jensen PR,Mann M Mol. Cell Proteomics 2007, Apr;6(4):697-707. [ PMID:17218307] |
Functional Description From UniProt | 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 |
| TRANSMEM 331 351 Helical; (Potential)
MOD_RES 162 162 Phosphothreonine; by autocatalysis
MOD_RES 163 163 Phosphothreonine; by autocatalysis
MOD_RES 165 165 Phosphothreonine; by autocatalysis
MOD_RES 167 167 Phosphothreonine; by autocatalysis
MOD_RES 214 214 Phosphoserine; by autocatalysis
MOD_RES 290 290 Phosphothreonine; by autocatalysis
MOD_RES 313 313 Phosphothreonine; by autocatalysis
MOD_RES 320 320 Phosphothreonine; by autocatalysis |
| ATP-binding; Completeproteome; Germination; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Referenceproteome; Repeat; Serine/threonine-proteinkinase; Signal-anchor; Transferase; Transmembrane; Transmembranehelix |
Protein Sequence | MLIGKRISGR YQILRVIGGG GMANVYLAED IILDREVAIK ILRFDYANDN EFIRRFRREA 60
QSASSLDHPN IVSIYDLGEE DDIYYIVMEY VEGMTLKEYI TANGPLHPKE ALNIMEQIVS 120
AIAHAHQNQI VHRDIKPHNI LIDHMGNIKV TDFGIATALS STTITHTNSV LGSVHYLSPE 180
QARGGLATKK SDIYALGIVL FELLTGRIPF DGESAVSIAL KHLQAETPSA KRWNPSVPQS 240
VENIILKATA KDPFHRYETA EDMEADIKTA FDADRLNEKR FTIQEDEEMT KAIPIIKDEE 300
LAKAAGEKEA EVTTAQENKT KKNGKRKKWP WVLLTICLVF ITAGILAVTV FPSLFMPKDV 360
KIPDVSGMEY EKAAGLLEKE GLQVDSEVLE ISDEKIEEGL MVKTDPKADT TVKEGATVTL 420
YKSTGKAKTE IGDVTGQTVD QAKKALKDQG FNHVTVNEVN DEKNAGTVID QNPSAGTELV 480
PSEDQVKLTV SIGPEDITLR DLKTYSKEAA SGYLEDNGLK LVEKEAYSDD VPEGQVVKQK 540
PAAGTAVKPG NEVEVTFSLG PEKKPAKTVK EKVKIPYEPE NEGDELQVQI AVDDADHSIS 600
DTYEEFKIKE PTERTIELKI EPGQKGYYQV MVNNKVVSYK TIEYPKDE 648 |
| GO:0016021 C:integral component of membrane IEA:UniProtKB-KW GO:0005886 C:plasma membrane IDA:UniProtKB GO:0005524 F:ATP binding IEA:UniProtKB-KW GO:0008658 F:penicillin binding IEA:InterPro GO:0042834 F:peptidoglycan binding IDA:UniProtKB GO:0004674 F:protein serine/threonine kinase activity IDA:UniProtKB GO:0071224 P:cellular response to peptidoglycan IMP:UniProtKB GO:0006468 P:protein phosphorylation IDA:UniProtKB GO:0007165 P:signal transduction IMP:UniProtKB GO:0009847 P:spore germination IMP:UniProtKB |
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