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Protein

Serine/threonine-protein kinase StkP

Gene

stkP

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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, MapZ (shown in the avirulent strain Rx / Cp1015), and StkP itself. Also able to phosphorylate FtsZ in vitro, however FtsZ may not be a target of StkP in vivo. 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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei42ATPPROSITE-ProRule annotation1
Active sitei136Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 26ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Septation, Virulence

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase StkP (EC:2.7.11.1)
Short name:
Ser/Thr-protein kinase StkP
Alternative name(s):
Eukaryotic-type Ser/Thr protein kinase
Short name:
ESTPK
Gene namesi
Name:stkP
Ordered Locus Names:SP_1732
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000585 Componenti: Chromosome

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass membrane protein 1 Publication

  • Note: The kinase domain is located intracellularly, while the C-terminal PASTA domain is exposed extracellularly, being surface accessible in vivo and recognized by the immune system (PubMed:20223804). However, another study in an avirulent strain (PubMed:19502404) showed that the C-terminal PASTA domain is located in the periplasmic space, beneath the peptidoglycan cell wall. Localizes to the midcell division sites in dividing cells of growing cultures but in the stationary phase, the characteristic midcell localization of StkP disappears and StkP shows a diffuse membrane localization. Displays a temporal colocalization with FtsZ.1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 342CytoplasmicBy similarityAdd BLAST342
Transmembranei343 – 363HelicalBy similarityAdd BLAST21
Topological domaini364 – 659ExtracellularBy similarityAdd BLAST296

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Biotechnological usei

Was identified as an important pneumococcal antigen that provides significant cross-protection in models of pneumococcal sepsis and pneumonia. Was selected as one of the lead candidates for development of a new pneumococcus protein-based vaccine. Is a component of a trivalent recombinant protein-based vaccine candidate for protection against S.pneumoniae, whose initial formulation development evaluations are described in PubMed:22538529.2 Publications

Disruption phenotypei

Disruption of this gene results in a strong reduction of bacterial growth, and increased antibiotic sensitivity to penicillin, cephalosporins (e.g. ceftazidime), and vancomycin in vitro. Cells lacking this gene are highly attenuated in virulence, and demonstrate an elongated shape and very few division septa separating the daughter cells. The lack of StkP does not disturb FtsZ ring formation and does not affect the expression level and the phosphorylation status of FtsZ.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004181441 – 659Serine/threonine-protein kinase StkPAdd BLAST659

Post-translational modificationi

Autophosphorylation occurs predominantly at the threonine residue and weakly at the serine residue. Dephosphorylated by PhpP (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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 FtsZ in vitro via its kinase domain.By similarity1 Publication

Protein-protein interaction databases

STRINGi170187.SpneT_02001125.

Structurei

3D structure databases

ProteinModelPortaliQ97PA9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 273Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini366 – 433PASTA 1PROSITE-ProRule annotationAdd BLAST68
Domaini434 – 505PASTA 2PROSITE-ProRule annotationAdd BLAST72
Domaini506 – 577PASTA 3PROSITE-ProRule annotationAdd BLAST72
Domaini578 – 651PASTA 4PROSITE-ProRule annotationAdd BLAST74

Domaini

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, is essential for StkP activation and substrate phosphorylation, and is responsible for cellular targeting to midcell (By similarity).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 4 PASTA domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D9P. Bacteria.
COG0515. LUCA.
COG2815. LUCA.
HOGENOMiHOG000037186.
KOiK12132.
OMAiMQIPIVN.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR005543. PASTA_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00740. PASTA. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q97PA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQIGKIFAG RYRIVKQIGR GGMADVYLAK DLILDGEEVA VKVLRTNYQT
60 70 80 90 100
DPIAVARFQR EARAMADLDH PHIVRITDIG EEDGQQYLAM EYVAGLDLKR
110 120 130 140 150
YIKEHYPLSN EEAVRIMGQI LLAMRLAHTR GIVHRDLKPQ NILLTPDGTA
160 170 180 190 200
KVTDFGIAVA FAETSLTQTN SMLGSVHYLS PEQARGSKAT VQSDIYAMGI
210 220 230 240 250
IFYEMLTGHI PYDGDSAVTI ALQHFQKPLP SVIAENPSVP QALENVIIKA
260 270 280 290 300
TAKKLTNRYR SVSEMYVDLS SSLSYNRRNE SKLIFDETSK ADTKTLPKVS
310 320 330 340 350
QSTLTSIPKV QAQTEHKSIK NPSQAVTEET YQPQAPKKHR FKMRYLILLA
360 370 380 390 400
SLVLVAASLI WILSRTPATI AIPDVAGQTV AEAKATLKKA NFEIGEEKTE
410 420 430 440 450
ASEKVEEGRI IRTDPGAGTG RKEGTKINLV VSSGKQSFQI SNYVGRKSSD
460 470 480 490 500
VIAELKEKKV PDNLIKIEEE ESNESEAGTV LKQSLPEGTT YDLSKATQIV
510 520 530 540 550
LTVAKKATTI QLGNYIGRNS TEVISELKQK KVPENLIKIE EEESSESEPG
560 570 580 590 600
TIMKQSPGAG TTYDVSKPTQ IVLTVAKKVT SVAMPSYIGS SLEFTKNNLI
610 620 630 640 650
QIVGIKEANI EVVEVTTAPA GSAEGMVVEQ SPRAGEKVDL NKTRVKISIY

KPKTTSATP
Length:659
Mass (Da):72,289
Last modified:October 1, 2001 - v1
Checksum:i4723AE1001BCE4CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005672 Genomic DNA. Translation: AAK75808.1.
PIRiG95201.
RefSeqiWP_000614538.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK75808; AAK75808; SP_1732.
KEGGispn:SP_1732.
PATRICi19707915. VBIStrPne105772_1800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005672 Genomic DNA. Translation: AAK75808.1.
PIRiG95201.
RefSeqiWP_000614538.1. NZ_AKVY01000001.1.

3D structure databases

ProteinModelPortaliQ97PA9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi170187.SpneT_02001125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK75808; AAK75808; SP_1732.
KEGGispn:SP_1732.
PATRICi19707915. VBIStrPne105772_1800.

Phylogenomic databases

eggNOGiENOG4105D9P. Bacteria.
COG0515. LUCA.
COG2815. LUCA.
HOGENOMiHOG000037186.
KOiK12132.
OMAiMQIPIVN.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR005543. PASTA_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00740. PASTA. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTKP_STRPN
AccessioniPrimary (citable) accession number: Q97PA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: October 1, 2001
Last modified: November 30, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.