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Serine/threonine-protein kinase StkP (Ser/Thr-protein kinase StkP) (EC 2.7.11.1) (Eukaryotic-type Ser/Thr protein kinase) (ESTPK)

 STKP_STREE              Reviewed;         659 AA.
Q8KY50;
11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
22-NOV-2017, entry version 90.
RecName: Full=Serine/threonine-protein kinase StkP;
Short=Ser/Thr-protein kinase StkP;
EC=2.7.11.1 {ECO:0000269|PubMed:15720398};
AltName: Full=Eukaryotic-type Ser/Thr protein kinase;
Short=ESTPK;
Name=stkP;
Streptococcus pneumoniae.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=1313;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Rx / Cp1015;
Echenique J.R., Trombe M.C.;
"A serine/threonine kinase involved in competence regulation.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF TARGET SUBSTRATES,
ENZYME REGULATION, PHOSPHORYLATION, PTM, PH DEPENDENCE, SUBCELLULAR
LOCATION, OPERON STRUCTURE, AND MUTAGENESIS OF LYS-42.
STRAIN=Rx / Cp1015;
PubMed=15720398; DOI=10.1111/j.1742-4658.2005.04560.x;
Novakova L., Saskova L., Pallova P., Janecek J., Novotna J.,
Ulrych A., Echenique J., Trombe M.C., Branny P.;
"Characterization of a eukaryotic type serine/threonine protein kinase
and protein phosphatase of Streptococcus pneumoniae and identification
of kinase substrates.";
FEBS J. 272:1243-1254(2005).
[3]
SUBUNIT, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION ACTIVITY, AND
DOMAIN.
STRAIN=Rx / Cp1015;
PubMed=17307148; DOI=10.1016/j.bbrc.2007.01.184;
Pallova P., Hercik K., Saskova L., Novakova L., Branny P.;
"A eukaryotic-type serine/threonine protein kinase StkP of
Streptococcus pneumoniae acts as a dimer in vivo.";
Biochem. Biophys. Res. Commun. 355:526-530(2007).
[4]
FUNCTION AS A GLOBAL TRANSCRIPTIONAL REGULATOR, AND DISRUPTION
PHENOTYPE.
STRAIN=Rx / Cp1015;
PubMed=17416671; DOI=10.1128/JB.01616-06;
Saskova L., Novakova L., Basler M., Branny P.;
"Eukaryotic-type serine/threonine protein kinase StkP is a global
regulator of gene expression in Streptococcus pneumoniae.";
J. Bacteriol. 189:4168-4179(2007).
[5]
FUNCTION IN COMPETENCE, INTERACTION WITH PHPP, SUBCELLULAR LOCATION,
AND TOPOLOGY.
STRAIN=Rx / Cp1015;
PubMed=19502404; DOI=10.1128/JB.00196-09;
Osaki M., Arcondeguy T., Bastide A., Touriol C., Prats H.,
Trombe M.C.;
"The StkP/PhpP signaling couple in Streptococcus pneumoniae: cellular
organization and physiological characterization.";
J. Bacteriol. 191:4943-4950(2009).
[6]
FUNCTION, ROLE IN CELL DIVISION, IDENTIFICATION OF TARGET SUBSTRATES,
ENZYME REGULATION, DISRUPTION PHENOTYPE, DOMAIN, AND MUTAGENESIS OF
LYS-42.
STRAIN=Rx / Cp1015;
PubMed=20453092; DOI=10.1128/JB.01564-09;
Novakova L., Bezouskova S., Pompach P., Spidlova P., Saskova L.,
Weiser J., Branny P.;
"Identification of multiple substrates of the StkP Ser/Thr protein
kinase in Streptococcus pneumoniae.";
J. Bacteriol. 192:3629-3638(2010).
[7]
PEPTIDOGLYCAN-BINDING, 3D-STRUCTURE MODELING OF 363-659, AND DOMAIN.
STRAIN=Rx / Cp1015;
PubMed=21167155; DOI=10.1016/j.febslet.2010.12.016;
Maestro B., Novakova L., Hesek D., Lee M., Leyva E., Mobashery S.,
Sanz J.M., Branny P.;
"Recognition of peptidoglycan and beta-lactam antibiotics by the
extracellular domain of the Ser/Thr protein kinase StkP from
Streptococcus pneumoniae.";
FEBS Lett. 585:357-363(2011).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=Rx1;
PubMed=22431591; DOI=10.1073/pnas.1119172109;
Beilharz K., Novakova L., Fadda D., Branny P., Massidda O.,
Veening J.W.;
"Control of cell division in Streptococcus pneumoniae by the conserved
Ser/Thr protein kinase StkP.";
Proc. Natl. Acad. Sci. U.S.A. 109:E905-E913(2012).
[9]
FUNCTION.
STRAIN=D39, R6, and Rx1;
PubMed=25550321; DOI=10.1128/mBio.01700-14;
Holeckova N., Doubravova L., Massidda O., Molle V., Buriankova K.,
Benada O., Kofronova O., Ulrych A., Branny P.;
"LocZ is a new cell division protein involved in proper septum
placement in Streptococcus pneumoniae.";
MBio 6:E01700-E01700(2015).
-!- 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, via the transduction of signals
culminating directly or indirectly in ComD activation. Is
important for the resistance of S.pneumoniae to various
environmental stress conditions. Appears to be a global regulator
that positively controls the transcription of a set of genes
encoding functions involved in cell wall metabolism, pyrimidine
biosynthesis, DNA repair, iron uptake, and oxidative stress
response, and that seems to down-regulate genes employed in
competence. Since StkP is unlikely to directly regulate
transcription, the input signal must be transmitted through an
effector molecule. Identified target substrates that are
specifically phosphorylated by StkP in vivo, mainly on threonine
residues, are DivIVA, GlmM, PpaC, MapZ, and StkP itself.
Autophosphorylated StkP is a substrate for the cotranscribed
protein phosphatase PhpP; PhpP and StkP appear to constitute a
functional signaling couple in vivo. {ECO:0000269|PubMed:15720398,
ECO:0000269|PubMed:17416671, ECO:0000269|PubMed:19502404,
ECO:0000269|PubMed:20453092, ECO:0000269|PubMed:22431591,
ECO:0000269|PubMed:25550321}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:15720398}.
-!- ENZYME REGULATION: StkP is activated continuously during growth
and its activity is inhibited upon growth arrest. Inhibited by
staurosporine, a known protein kinase inhibitor.
{ECO:0000269|PubMed:15720398, ECO:0000269|PubMed:20453092}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Active over the wide range of pH from 3 to 9.
{ECO:0000269|PubMed:15720398};
-!- 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. Interacts with PhpP via its kinase domain.
{ECO:0000269|PubMed:17307148, ECO:0000269|PubMed:19502404}.
-!- INTERACTION:
Q8KY51:phpP (xeno); NbExp=2; IntAct=EBI-6405629, EBI-6405646;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15720398,
ECO:0000269|PubMed:17307148, ECO:0000269|PubMed:19502404,
ECO:0000269|PubMed:22431591}; Single-pass membrane protein
{ECO:0000269|PubMed:15720398, ECO:0000269|PubMed:17307148,
ECO:0000269|PubMed:19502404, ECO:0000269|PubMed:22431591}.
Note=The C-terminal PASTA domain is located in the periplasmic
space, beneath the peptidoglycan cell wall, and the kinase domain
is located in the cytoplasm. However, another study in the
virulent strain TIGR4 (PubMed:20223804) showed that the C-terminal
PASTA domain is exposed extracellularly. Localizes to the midcell
division sites.
-!- INDUCTION: The phpP and stkP genes form an operon.
-!- 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 C-terminal domain binds to
synthetic and native peptidoglycan (PGN) subunits and to beta-
lactam antibiotics, which mimic the terminal portions of the PGN
stem peptide. Deletion of both the transmembrane domain and the
PASTA domain negatively affects the stability of the core kinase
domain. In contrast, the membrane anchored kinase domain and the
full-length form of StkP are stable and capable of
autophosphorylation. However, the membrane anchored kinase domain
(i.e. StkP lacking the C-terminal PASTA domain) is unable to
phosphorylate its substrates, which means that the PASTA domain is
essential for StkP activation and substrate phosphorylation. The
PASTA domain is also responsible for cellular targeting to midcell
(shown in the virulent strain D39). Both the transmembrane and
extracellular domains promote dimerization of StkP.
{ECO:0000269|PubMed:17307148, ECO:0000269|PubMed:20453092,
ECO:0000269|PubMed:21167155}.
-!- PTM: Autophosphorylation occurs predominantly at the threonine
residue and weakly at the serine residue. Dephosphorylated by
PhpP. {ECO:0000269|PubMed:15720398}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene have a significantly
reduced growth rate in the early exponential phase, exhibit an
increased rate of autolysis at the stationary phase of growth and
do not achieve the same final optical density as the wild-type
strain. Their growth is almost completely impaired at 40 degrees
Celsius, in contrast to that of the wild-type strain which is
unaffected at this temperature. The mutant strain is also more
susceptible to oxidative stress, to osmotic stress, and is less
tolerant to acidic pH. Moreover, inactivation of stkP leads to
morphological changes: a significant number of cells do not have
the typical ovoid shape but appear to be longer with rather oval
poles, and they exhibit an apparent cell division defect.
{ECO:0000269|PubMed:17416671, ECO:0000269|PubMed:20453092}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AF285441; AAM47530.1; -; Genomic_DNA.
ProteinModelPortal; Q8KY50; -.
SMR; Q8KY50; -.
IntAct; Q8KY50; 1.
eggNOG; ENOG4105D9P; Bacteria.
eggNOG; COG0515; LUCA.
eggNOG; COG2815; LUCA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
GO; GO:0051302; P:regulation of cell division; IMP:CACAO.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR005543; PASTA_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF03793; PASTA; 4.
Pfam; PF00069; Pkinase; 1.
SMART; SM00740; PASTA; 4.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51178; PASTA; 4.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Cell division; Cell membrane; Cell shape;
Competence; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Repeat; Septation; Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 659 Serine/threonine-protein kinase StkP.
/FTId=PRO_0000418143.
TOPO_DOM 1 342 Cytoplasmic.
{ECO:0000305|PubMed:19502404}.
TRANSMEM 343 363 Helical. {ECO:0000305}.
TOPO_DOM 364 659 Periplasmic.
{ECO:0000305|PubMed:19502404}.
DOMAIN 12 273 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 366 433 PASTA 1. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 434 505 PASTA 2. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 506 577 PASTA 3. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 578 651 PASTA 4. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
NP_BIND 18 26 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 136 136 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 42 42 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MUTAGEN 42 42 K->R: Dramatic reduction of
phosphorylation.
{ECO:0000269|PubMed:15720398,
ECO:0000269|PubMed:20453092}.
SEQUENCE 659 AA; 72378 MW; F0146D420F2C565D CRC64;
MIQIGKIFAG RYRIVKQIGR GGMADVYLAK DLILDGEEVA VKVLRTNYQT DPIAVARFQR
EARAMADLDH PHIVRITDIG EEDGQQYLAM EYVAGLDLKR YIKEHYPLSN EEAVRIMRQI
LLAMRLAHTR GIVHRDLKPQ NILLTPDGTA KVTDFGIAVA FAETSLTQTN SMLGSVHYLS
PEQARGSKAT VQSDIYAMGI IFYEMLTGHI PYDGDSAVTI ALQHFQNPLP SVIAENSSVP
QALENVIIKA TAKKLTNRYR SVSEMYVDLS SSLSYNRRNE SKLIFDETSK ADTKTLPKVS
QSTLTSIPKV QAQTEHKSIK NPSQAVTEET YQPQAPKKHR FKMRYLILLA SLVLVAASLI
WILSRSPATI AIPDVAGQTV AEAKATLKKA NFEIGEEKTE ASEKVEEGRI IRTDPGAGTG
RKEGTKINLV VSSGKQSFQI SNYVGRKSSD VIAELKEKKV PDNLIKIEEE ESNESEAGTV
LKQSLPEGTT YDLSKATQIV LTVAKKATTI QLGNYIGRNS TEVISELKQK KVPENLIKIE
EEESSESEPG TIMKQSPGAG TTYDVSKPTQ IVLTVAKKVT SVAMPSYIGS SLEFTKNNLI
QIVGIKEANI EVVEVTTAPA GSVEGMVVEQ SPRAGEKVDL NKTRVKISIY KPKTTSATP


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