※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase StkP
Protein Synonyms/Alias
 Ser/Thr-protein kinase StkP;  ESTPK
Gene Name
 stkP
Gene Synonyms/Alias
 SPD_1542
Created Date
 3-June-2014
Organism
 Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
NCBI Taxa ID
 373153
Phosphorylation
Position
Peptide
Code
Type
References
590 AMPSYIGSSLEFTKN S HTP [1]
587 TSVAMPSYIGSSLEF Y HTP [1]
Reference
 [1]Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae.
 Sun X,Ge F,Xiao CL,Yin XF,Ge R,Zhang LH,He QY
 J. Proteome Res. 2010, Jan;9(1):275-82. [PMID:19894762]
Functional Description From UniProt
 FUNCTION: Protein kinase involved in signal transduction pathways that regulate various cellular processes. Likely senses intracellular peptidoglycan subunits present in the cell division septa of actively growing cells; thus, intracellular unlinked peptidoglycan may serve as the signal molecules that trigger StkP phosphorylation activity on a set of substrates. Plays a crucial role in the regulation of cell shape and cell division of S.pneumoniae through control of at least DivIVA activity. Is involved in competence triggering, and is required for the expression of the central competence operon comCDE. StkP also plays an important role for bacterial survival in vivo. Identified target substrates that are specifically phosphorylated by StkP in vivo, mainly on threonine residues, are DivIVA, GlmM, PpaC, spr0334, and StkP itself. Autophosphorylated StkP is a substrate for the cotranscribed protein phosphatase PhpP (shown in the avirulent strain Rx / Cp1015); PhpP and StkP appear to constitute a functional signaling couple in vivo
Sequence Annotation From UniProt
 TRANSMEM 343 363 Helical; (By similarity)
Key Word From UniProt
 ATP-binding; Cellcycle; Celldivision; Cellmembrane; Cellshape; Competence; Completeproteome; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Repeat; Septation; Serine/threonine-proteinkinase; Transferase; Transmembrane; Transmembranehelix; Virulence
Protein Sequence
 MIQIGKIFAG RYRIVKQIGR GGMADVYLAK DLILDGEEVA VKVLRTNYQT DPIAVARFQR 60
 EARAMADLDH PHIVRITDIG EEDGQQYLAM EYVAGLDLKR YIKEHYPLSN EEAVRIMGQI 120
 LLAMRLAHTR GIVHRDLKPQ NILLTPDGTA KVTDFGIAVA FAETSLTQTN SMLGSVHYLS 180
 PEQARGSKAT VQSDIYAMGI IFYEMLTGHI PYDGDSAVTI ALQHFQNPLP SVIAENSSVP 240
 QALENVIIKA TAKKLTNRYR SVSEMYVDLS SSLSYNRRNE SKLIFDETSK ADTKTLPKVS 300
 QSTLTSIPKV QAQTEHKSIK NPSQAVTEET YQPQAPKKHR FKMRYLILLA SLVLVAASLI 360
 WILSRTPATI AIPDVAGQTV AEAKATLKKA NFEIGEEKTE ASEKVEEGRI IRTDPGAGTG 420
 RKEGTKINLV VSSGKQSFQI SNYVGRKSSD VIAELKEKKV PDNLIKIEEE ESNESEAGTV 480
 LKQSLPEGTT YDLSKATQIV LTVAKKATTI QLGNYIGRNS TEVISELKQK KVPENLIKIE 540
 EEESSESEPG TIMKQSPGAG TTYDVSKPTQ IVLTVAKKVT SVAMPSYIGS SLEFTKNNLI 600
 QIVGIKEANI EVVEVTTAPA GSVEGMVVEQ SPRAGEKVDL NKTRVKISIY KPKTTSATP 659
  GO:0016021   C:integral component of membrane IEA:UniProtKB-KW
  GO:0005886   C:plasma membrane IEA:UniProtKB-SubCell
  GO:0005524   F:ATP binding IEA:UniProtKB-KW
  GO:0008658   F:penicillin binding IEA:InterPro
  GO:0004674   F:protein serine/threonine kinase activity IEA:UniProtKB-KW
  GO:0000917   P:barrier septum assembly IEA:UniProtKB-KW
  GO:0030420   P:establishment of competence for transformation IEA:UniProtKB-KW
  GO:0009405   P:pathogenesis IEA:UniProtKB-KW
  GO:0008360   P:regulation of cell shape IEA:UniProtKB-KW
  IPR011009   Kinase-like_dom.
  IPR005543   PASTA.
  IPR000719   Prot_kinase_dom.
  IPR017441   Protein_kinase_ATP_BS.
  IPR008271   Ser/Thr_kinase_AS.
  PF03793   PASTA.
  PF00069   Pkinase.
  SM00740   PASTA.
  PS51178   PASTA.
  PS00107   PROTEIN_KINASE_ATP.
  PS50011   PROTEIN_KINASE_DOM.
  PS00108   PROTEIN_KINASE_ST.