STKP_STRP2
ID STKP_STRP2 Reviewed; 659 AA.
AC Q04J43;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Serine/threonine-protein kinase StkP;
DE Short=Ser/Thr-protein kinase StkP;
DE EC=2.7.11.1;
DE AltName: Full=Eukaryotic-type Ser/Thr protein kinase;
DE Short=ESTPK;
GN Name=stkP; OrderedLocusNames=SPD_1542;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=23477, and D39 / NCTC 7466;
RX PubMed=15039376; DOI=10.1128/iai.72.4.2434-2437.2004;
RA Echenique J., Kadioglu A., Romao S., Andrew P.W., Trombe M.C.;
RT "Protein serine/threonine kinase StkP positively controls virulence and
RT competence in Streptococcus pneumoniae.";
RL Infect. Immun. 72:2434-2437(2004).
RN [3]
RP TARGET PROTEIN SUBSTRATES.
RC STRAIN=D39 / NCTC 7466;
RX PubMed=20453092; DOI=10.1128/jb.01564-09;
RA Novakova L., Bezouskova S., Pompach P., Spidlova P., Saskova L., Weiser J.,
RA Branny P.;
RT "Identification of multiple substrates of the StkP Ser/Thr protein kinase
RT in Streptococcus pneumoniae.";
RL J. Bacteriol. 192:3629-3638(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF DIVIVA AS SUBSTRATE,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=D39 / NCTC 7466;
RX PubMed=22431591; DOI=10.1073/pnas.1119172109;
RA Beilharz K., Novakova L., Fadda D., Branny P., Massidda O., Veening J.W.;
RT "Control of cell division in Streptococcus pneumoniae by the conserved
RT Ser/Thr protein kinase StkP.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E905-E913(2012).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=D39 / NCTC 7466;
RX PubMed=28941257; DOI=10.1111/mmi.13847;
RA Zheng J.J., Perez A.J., Tsui H.T., Massidda O., Winkler M.E.;
RT "Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins suppresses
RT the requirement for PBP2b by overproduction of FtsA in Streptococcus
RT pneumoniae D39.";
RL Mol. Microbiol. 106:793-814(2017).
CC -!- FUNCTION: Protein kinase involved in signal transduction pathways that
CC regulate various cellular processes. Likely senses intracellular
CC peptidoglycan subunits present in the cell division septa of actively
CC growing cells; thus, intracellular unlinked peptidoglycan may serve as
CC the signal molecules that trigger StkP phosphorylation activity on a
CC set of substrates. Plays a crucial role in the regulation of cell shape
CC and cell division of S.pneumoniae through control of at least DivIVA
CC activity. Is involved in competence triggering, and is required for the
CC expression of the central competence operon comCDE. StkP also plays an
CC important role for bacterial survival in vivo. Identified target
CC substrates that are specifically phosphorylated by StkP in vivo, mainly
CC on threonine residues, are DivIVA, GlmM, PpaC, MapZ, KhpB (also called
CC EloR/Jag, shown in strains R6 and Rx1) and StkP itself.
CC Autophosphorylated StkP is a substrate for the cotranscribed protein
CC phosphatase PhpP (shown in the avirulent strain Rx / Cp1015); PhpP and
CC StkP appear to constitute a functional signaling couple in vivo.
CC {ECO:0000269|PubMed:22431591}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:22431591};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22431591};
CC -!- SUBUNIT: Homodimer. StkP forms dimers through its transmembrane and
CC extracellular domains. Dimer formation likely promotes
CC autophosphorylation activity and might be necessary for targeting StkP
CC substrate (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22431591};
CC Single-pass membrane protein {ECO:0000269|PubMed:22431591}.
CC Note=Localizes to the midcell division sites, colocalizes with PBP2b.
CC {ECO:0000269|PubMed:22431591, ECO:0000269|PubMed:28941257}.
CC -!- DOMAIN: Consists of an N-terminal kinase domain, a transmembrane
CC domain, and a C-terminal domain containing four repeats of the PASTA
CC signature sequence (Penicillin-binding protein and Ser/Thr protein
CC kinase associated domain). The PASTA domain binds to peptidoglycan
CC (PGN) subunits, is essential for StkP activation and substrate
CC phosphorylation (shown in the avirulent strain Rx / Cp1015), and is
CC responsible for cellular targeting to midcell.
CC {ECO:0000269|PubMed:22431591}.
CC -!- PTM: Autophosphorylation occurs predominantly at the threonine residue
CC and weakly at the serine residue. Dephosphorylated by PhpP (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Disruption of stkP gene results in strong
CC repression of competence development for genetic transformation in
CC vitro. Strains D39 (serotype 2) and 23477 (serotype 6) lacking this
CC gene show a greatly attenuated virulence in lung infection and
CC bloodstream invasion in mice, but no in vitro growth defect.
CC {ECO:0000269|PubMed:15039376}.
CC -!- MISCELLANEOUS: PubMed:20453092 shows that the patterns of
CC phosphorylated proteins are similar for S.pneumoniae Rx / Cp1015 and
CC D39 (avirulent and virulent strains, respectively) when they are grown
CC in complex CAT medium. Thus, in both strains, StkP phosphorylates the
CC same set of substrates that are probably important for sustaining
CC normal growth in laboratory conditions.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000410; ABJ55478.1; -; Genomic_DNA.
DR RefSeq; WP_000614552.1; NC_008533.2.
DR AlphaFoldDB; Q04J43; -.
DR SMR; Q04J43; -.
DR STRING; 373153.SPD_1542; -.
DR EnsemblBacteria; ABJ55478; ABJ55478; SPD_1542.
DR GeneID; 60232905; -.
DR KEGG; spd:SPD_1542; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OMA; DPDYRYQ; -.
DR OrthoDB; 1377603at2; -.
DR BioCyc; SPNE373153:G1G6V-1665-MON; -.
DR Proteomes; UP000001452; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell membrane; Cell shape;
KW Competence; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Repeat;
KW Septation; Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..659
FT /note="Serine/threonine-protein kinase StkP"
FT /id="PRO_0000418145"
FT TOPO_DOM 1..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 364..659
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT DOMAIN 12..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 366..433
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 434..505
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 506..577
FT /note="PASTA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 578..651
FT /note="PASTA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT REGION 541..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 659 AA; 72293 MW; A469FB99617B1586 CRC64;
MIQIGKIFAG RYRIVKQIGR GGMADVYLAK DLILDGEEVA VKVLRTNYQT DPIAVARFQR
EARAMADLDH PHIVRITDIG EEDGQQYLAM EYVAGLDLKR YIKEHYPLSN EEAVRIMGQI
LLAMRLAHTR GIVHRDLKPQ NILLTPDGTA KVTDFGIAVA FAETSLTQTN SMLGSVHYLS
PEQARGSKAT VQSDIYAMGI IFYEMLTGHI PYDGDSAVTI ALQHFQNPLP SVIAENSSVP
QALENVIIKA TAKKLTNRYR SVSEMYVDLS SSLSYNRRNE SKLIFDETSK ADTKTLPKVS
QSTLTSIPKV QAQTEHKSIK NPSQAVTEET YQPQAPKKHR FKMRYLILLA SLVLVAASLI
WILSRTPATI 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
