Q8DNS0 · STKP_STRR6
- ProteinSerine/threonine-protein kinase StkP
- GenestkP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids659 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. Identified target substrates that are specifically phosphorylated by StkP in vivo, mainly on threonine residues, are DivIVA, KhpB (also called EloR/Jag) 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.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein kinase binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | division septum assembly | |
Biological Process | regulation of autophagy | |
Biological Process | regulation of cell shape | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase StkP
- EC number
- Short namesSer/Thr-protein kinase StkP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionQ8DNS0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Note: The kinase domain is located intracellularly, while the C-terminal PASTA domain is exposed extracellularly. Localizes to the midcell division sites. Time-lapse microscopy shows that StkP displays an intermediate timing of recruitment to midcell: StkP arrives shortly after FtsA but before DivIVA. Furthermore, StkP remains at midcell longer than FtsA, until division is complete. Delocalizes from the septum in the presence of antibiotics that target the latest stages of cell-wall biosynthesis and in cells that have stopped dividing.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-342 | Cytoplasmic | ||||
Sequence: MIQIGKIFAGRYRIVKQIGRGGMADVYLAKDLILDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAMEYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQNPLPSVIAENSSVPQALENVIIKATAKKLTNRYRSVSEMYVDLSSSLSYNRRNESKLIFDETSKADTKTLPKVSQSTLTSIPKVQAQTEHKSIKNPSQAVTEETYQPQAPKKHRFK | ||||||
Transmembrane | 343-363 | Helical | ||||
Sequence: MRYLILLASLVLVAASLIWIL | ||||||
Topological domain | 364-659 | Extracellular | ||||
Sequence: SRTPATIAIPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVSSGKQSFQISNYVGRKSSDVIAELKEKKVPDNLIKIEEEESNESEAGTVLKQSLPEGTTYDLSKATQIVLTVAKKATTIQLGNYIGRNSTEVISELKQKKVPENLIKIEEEESSESEPGTIMKQSPGAGTTYDVSKPTQIVLTVAKKVTSVAMPSYIGSSLEFTKNNLIQIVGIKEANIEVVEVTTAPAGSVEGMVVEQSPRAGEKVDLNKTRVKISIYKPKTTSATP |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
According to PubMed:22211696, cells lacking this gene show round shape (the cell shape of wild-type strain is ovoid) and form long chains with unsplit cross-wall joining cells. Their septa either are not positioned at the equator, or display an aberrant ultrastructure (curly aspects). They display delocalized sites of peptidoglycan synthesis. According to PubMed:22431591, cells in which StkP is depleted clearly show an elongated phenotype, with cell-wall synthesis occurring along the peripheral side between the septal zones. Reduces transcription of the peptidoglycan hydrolase pcsB gene (PubMed:27902439).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 42 | Cells form very elongated and unchained cells. They have a giant length size and show the aberrant presence of multiple septa that do not seem functional. StkP is properly recruited to each non-constricted septum site. No phosphorylation activity. Slight reduction in transcription of the peptidoglycan hydrolase pcsB gene, but less than effect of deletion mutant. | ||||
Sequence: K → M |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000418146 | 1-659 | Serine/threonine-protein kinase StkP | |||
Sequence: MIQIGKIFAGRYRIVKQIGRGGMADVYLAKDLILDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAMEYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQNPLPSVIAENSSVPQALENVIIKATAKKLTNRYRSVSEMYVDLSSSLSYNRRNESKLIFDETSKADTKTLPKVSQSTLTSIPKVQAQTEHKSIKNPSQAVTEETYQPQAPKKHRFKMRYLILLASLVLVAASLIWILSRTPATIAIPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVSSGKQSFQISNYVGRKSSDVIAELKEKKVPDNLIKIEEEESNESEAGTVLKQSLPEGTTYDLSKATQIVLTVAKKATTIQLGNYIGRNSTEVISELKQKKVPENLIKIEEEESSESEPGTIMKQSPGAGTTYDVSKPTQIVLTVAKKVTSVAMPSYIGSSLEFTKNNLIQIVGIKEANIEVVEVTTAPAGSVEGMVVEQSPRAGEKVDLNKTRVKISIYKPKTTSATP |
Post-translational modification
Autophosphorylation occurs predominantly at the threonine residue and weakly at the serine residue. Dephosphorylated by PhpP (By similarity).
Keywords
- PTM
Interaction
Subunit
Homodimer. StkP forms dimers through its transmembrane and extracellular domains. Dimer formation likely promotes autophosphorylation activity and might be necessary for targeting StkP substrate (By similarity).
Interacts with MreC in the elongasome (PubMed:28710862).
May interact with sensor histidine kinase WalK, thereby playing a role in signal transduction by WalK
Interacts with MreC in the elongasome (PubMed:28710862).
May interact with sensor histidine kinase WalK, thereby playing a role in signal transduction by WalK
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-273 | Protein kinase | ||||
Sequence: YRIVKQIGRGGMADVYLAKDLILDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAMEYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQNPLPSVIAENSSVPQALENVIIKATAKKLTNRYRSVSEMYVDLSSSL | ||||||
Domain | 366-433 | PASTA 1 | ||||
Sequence: TPATIAIPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVSS | ||||||
Domain | 434-505 | PASTA 2 | ||||
Sequence: GKQSFQISNYVGRKSSDVIAELKEKKVPDNLIKIEEEESNESEAGTVLKQSLPEGTTYDLSKATQIVLTVAK | ||||||
Domain | 506-577 | PASTA 3 | ||||
Sequence: KATTIQLGNYIGRNSTEVISELKQKKVPENLIKIEEEESSESEPGTIMKQSPGAGTTYDVSKPTQIVLTVAK | ||||||
Region | 541-561 | Disordered | ||||
Sequence: EEESSESEPGTIMKQSPGAGT | ||||||
Domain | 578-651 | PASTA 4 | ||||
Sequence: KVTSVAMPSYIGSSLEFTKNNLIQIVGIKEANIEVVEVTTAPAGSVEGMVVEQSPRAGEKVDLNKTRVKISIYK |
Domain
Consists of an N-terminal kinase domain, a transmembrane domain, and a C-terminal domain containing four repeats of the PASTA signature sequence (Penicillin-binding protein and Ser/Thr protein kinase associated domain). The PASTA domain binds to peptidoglycan (PGN) subunits (shown in strain Rx / Cp1015), is essential for StkP activation and substrate phosphorylation, and is required for cellular targeting to midcell.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length659
- Mass (Da)72,293
- Last updated2003-03-01 v1
- ChecksumA469FB99617B1586
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE007317 EMBL· GenBank· DDBJ | AAL00380.1 EMBL· GenBank· DDBJ | Genomic DNA |