STKP_STRR6
ID STKP_STRR6 Reviewed; 659 AA.
AC Q8DNS0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
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; Synonyms=pkn2; OrderedLocusNames=spr1577;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION IN CELL SHAPE AND DIVISION, CATALYTIC ACTIVITY, IDENTIFICATION OF
RP DIVIVA AS SUBSTRATE, AUTOPHOSPHORYLATION ACTIVITY, DOMAIN, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-42.
RC STRAIN=R6 / R800;
RX PubMed=22211696; DOI=10.1111/j.1365-2958.2011.07962.x;
RA Fleurie A., Cluzel C., Guiral S., Freton C., Galisson F., Zanella-Cleon I.,
RA Di Guilmi A.M., Grangeasse C.;
RT "Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell
RT division of Streptococcus pneumoniae.";
RL Mol. Microbiol. 83:746-758(2012).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LYS-42.
RC STRAIN=ATCC BAA-255 / R6;
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 [4]
RP FUNCTION, SUBSTRATE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF LYS-42.
RC STRAIN=R6 / R704;
RX PubMed=28710862; DOI=10.1111/mmi.13748;
RA Stamsaas G.A., Straume D., Ruud Winther A., Kjos M., Frantzen C.A.,
RA Haavarstein L.S.;
RT "Identification of EloR (Spr1851) as a regulator of cell elongation in
RT Streptococcus pneumoniae.";
RL Mol. Microbiol. 105:954-967(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. Identified target substrates that are specifically
CC phosphorylated by StkP in vivo, mainly on threonine residues, are
CC DivIVA, KhpB (also called EloR/Jag) and StkP itself. Autophosphorylated
CC StkP is a substrate for the cotranscribed protein phosphatase PhpP
CC (shown in the avirulent strain Rx / Cp1015); PhpP and StkP appear to
CC constitute a functional signaling couple in vivo.
CC {ECO:0000269|PubMed:22211696, ECO:0000269|PubMed:22431591,
CC ECO:0000269|PubMed:28710862}.
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:22211696};
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:22211696};
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). Interacts with MreC in the elongasome
CC (PubMed:28710862). {ECO:0000250, ECO:0000269|PubMed:28710862}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22211696,
CC ECO:0000269|PubMed:22431591, ECO:0000269|PubMed:28710862}; Single-pass
CC membrane protein {ECO:0000269|PubMed:22211696,
CC ECO:0000269|PubMed:22431591}. Note=The kinase domain is located
CC intracellularly, while the C-terminal PASTA domain is exposed
CC extracellularly. Localizes to the midcell division sites. Time-lapse
CC microscopy shows that StkP displays an intermediate timing of
CC recruitment to midcell: StkP arrives shortly after FtsA but before
CC DivIVA. Furthermore, StkP remains at midcell longer than FtsA, until
CC division is complete. Delocalizes from the septum in the presence of
CC antibiotics that target the latest stages of cell-wall biosynthesis and
CC in cells that have stopped dividing.
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 (shown in strain Rx / Cp1015), is essential for StkP
CC activation and substrate phosphorylation, and is required for cellular
CC targeting to midcell. {ECO:0000269|PubMed:22211696,
CC ECO:0000269|PubMed:28710862}.
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: According to PubMed:22211696, cells lacking this
CC gene show round shape (the cell shape of wild-type strain is ovoid) and
CC form long chains with unsplit cross-wall joining cells. Their septa
CC either are not positioned at the equator, or display an aberrant
CC ultrastructure (curly aspects). They display delocalized sites of
CC peptidoglycan synthesis. According to PubMed:22431591, cells in which
CC StkP is depleted clearly show an elongated phenotype, with cell-wall
CC synthesis occurring along the peripheral side between the septal zones.
CC {ECO:0000269|PubMed:22211696, ECO:0000269|PubMed:22431591}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AE007317; AAL00380.1; -; Genomic_DNA.
DR PIR; G98068; G98068.
DR RefSeq; NP_359169.1; NC_003098.1.
DR RefSeq; WP_000614552.1; NC_003098.1.
DR PDB; 5NOD; X-ray; 1.90 A; A=578-659.
DR PDBsum; 5NOD; -.
DR AlphaFoldDB; Q8DNS0; -.
DR SMR; Q8DNS0; -.
DR BioGRID; 4180581; 1.
DR DIP; DIP-61347N; -.
DR IntAct; Q8DNS0; 1.
DR STRING; 171101.spr1577; -.
DR EnsemblBacteria; AAL00380; AAL00380; spr1577.
DR GeneID; 60232905; -.
DR KEGG; spr:spr1577; -.
DR PATRIC; fig|171101.6.peg.1704; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OMA; DPDYRYQ; -.
DR Proteomes; UP000000586; 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; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; 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 3D-structure; ATP-binding; Cell cycle; Cell division; Cell membrane;
KW Cell shape; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Septation; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..659
FT /note="Serine/threonine-protein kinase StkP"
FT /id="PRO_0000418146"
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"
FT MUTAGEN 42
FT /note="K->M: Cells form very elongated and unchained cells.
FT They have a giant length size and show the aberrant
FT presence of multiple septa that do not seem functional.
FT StkP is properly recruited to each non-constricted septum
FT site. No phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:22211696,
FT ECO:0000269|PubMed:22431591, ECO:0000269|PubMed:28710862"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:5NOD"
FT HELIX 592..601
FT /evidence="ECO:0007829|PDB:5NOD"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:5NOD"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:5NOD"
FT STRAND 626..632
FT /evidence="ECO:0007829|PDB:5NOD"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:5NOD"
FT TURN 640..642
FT /evidence="ECO:0007829|PDB:5NOD"
FT STRAND 645..650
FT /evidence="ECO:0007829|PDB:5NOD"
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
