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 |
| TRANSMEM 343 363 Helical; (By similarity) |
| 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 |
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