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Q97PA9 (STKP2_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase StkP

Short name=Ser/Thr-protein kinase StkP
EC=2.7.11.1
Alternative name(s):
Eukaryotic-type Ser/Thr protein kinase
Short name=ESTPK
Gene names
Name:stkP
Ordered Locus Names:SP_1732
OrganismStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]
Taxonomic identifier170187 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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, spr0334 (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. Ref.3

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.3

Subunit structure

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. Ref.3

Subcellular location

Cell membrane; Single-pass membrane protein. 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 (Ref.3). 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. Ref.3

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

Post-translational modification

Autophosphorylation occurs predominantly at the threonine residue and weakly at the serine residue. Dephosphorylated by PhpP By similarity. Ref.3

Disruption phenotype

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. Ref.2 Ref.3

Biotechnological use

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 Ref.4. Ref.2 Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 4 PASTA domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 659659Serine/threonine-protein kinase StkP
PRO_0000418144

Regions

Topological domain1 – 342342Cytoplasmic By similarity
Transmembrane343 – 36321Helical; By similarity
Topological domain364 – 659296Extracellular By similarity
Domain12 – 273262Protein kinase
Domain366 – 43368PASTA 1
Domain434 – 50572PASTA 2
Domain506 – 57772PASTA 3
Domain578 – 65174PASTA 4
Nucleotide binding18 – 269ATP By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97PA9 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 4723AE1001BCE4CF

FASTA65972,289
        10         20         30         40         50         60 
MIQIGKIFAG RYRIVKQIGR GGMADVYLAK DLILDGEEVA VKVLRTNYQT DPIAVARFQR 

        70         80         90        100        110        120 
EARAMADLDH PHIVRITDIG EEDGQQYLAM EYVAGLDLKR YIKEHYPLSN EEAVRIMGQI 

       130        140        150        160        170        180 
LLAMRLAHTR GIVHRDLKPQ NILLTPDGTA KVTDFGIAVA FAETSLTQTN SMLGSVHYLS 

       190        200        210        220        230        240 
PEQARGSKAT VQSDIYAMGI IFYEMLTGHI PYDGDSAVTI ALQHFQKPLP SVIAENPSVP 

       250        260        270        280        290        300 
QALENVIIKA TAKKLTNRYR SVSEMYVDLS SSLSYNRRNE SKLIFDETSK ADTKTLPKVS 

       310        320        330        340        350        360 
QSTLTSIPKV QAQTEHKSIK NPSQAVTEET YQPQAPKKHR FKMRYLILLA SLVLVAASLI 

       370        380        390        400        410        420 
WILSRTPATI AIPDVAGQTV AEAKATLKKA NFEIGEEKTE ASEKVEEGRI IRTDPGAGTG 

       430        440        450        460        470        480 
RKEGTKINLV VSSGKQSFQI SNYVGRKSSD VIAELKEKKV PDNLIKIEEE ESNESEAGTV 

       490        500        510        520        530        540 
LKQSLPEGTT YDLSKATQIV LTVAKKATTI QLGNYIGRNS TEVISELKQK KVPENLIKIE 

       550        560        570        580        590        600 
EEESSESEPG TIMKQSPGAG TTYDVSKPTQ IVLTVAKKVT SVAMPSYIGS SLEFTKNNLI 

       610        620        630        640        650 
QIVGIKEANI EVVEVTTAPA GSAEGMVVEQ SPRAGEKVDL NKTRVKISIY KPKTTSATP 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.
[2]"Discovery of a novel class of highly conserved vaccine antigens using genomic scale antigenic fingerprinting of pneumococcus with human antibodies."
Giefing C., Meinke A.L., Hanner M., Henics T., Bui M.D., Gelbmann D., Lundberg U., Senn B.M., Schunn M., Habel A., Henriques-Normark B., Ortqvist A., Kalin M., von Gabain A., Nagy E.
J. Exp. Med. 205:117-131(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A VACCINE ANTIGEN, BIOTECHNOLOGY, DISRUPTION PHENOTYPE.
Strain: ATCC BAA-334 / TIGR4.
[3]"The pneumococcal eukaryotic-type serine/threonine protein kinase StkP co-localizes with the cell division apparatus and interacts with FtsZ in vitro."
Giefing C., Jelencsics K.E., Gelbmann D., Senn B.M., Nagy E.
Microbiology 156:1697-1707(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ROLE IN CELL DIVISION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION ACTIVITY, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE.
Strain: ATCC BAA-334 / TIGR4 and PJ1324 / Serotype 6B.
[4]"Preformulation characterization of an aluminum salt-adjuvanted trivalent recombinant protein-based vaccine candidate against Streptococcus pneumoniae."
Iyer V., Hu L., Liyanage M.R., Esfandiary R., Reinisch C., Meinke A., Maisonneuve J., Volkin D.B., Joshi S.B., Middaugh C.R.
J. Pharm. Sci. 101:3078-3090(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOTECHNOLOGY.
Strain: ATCC BAA-334 / TIGR4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005672 Genomic DNA. Translation: AAK75808.1.
PIRG95201.
RefSeqNP_346168.1. NC_003028.3.

3D structure databases

ProteinModelPortalQ97PA9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING170187.SP_1732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK75808; AAK75808; SP_1732.
GeneID931099.
KEGGspn:SP_1732.
PATRIC19707915. VBIStrPne105772_1800.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000037186.
KOK08884.
OMAMQIPIVN.
OrthoDBEOG6B35XT.
ProtClustDBCLSK884143.

Enzyme and pathway databases

BioCycSPNE170187:GHGN-1739-MONOMER.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR005543. PASTA.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00740. PASTA. 4 hits.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSTKP2_STRPN
AccessionPrimary (citable) accession number: Q97PA9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: October 1, 2001
Last modified: February 19, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families