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Q97PA9

- STKP2_STRPN

UniProt

Q97PA9 - STKP2_STRPN

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Protein
Serine/threonine-protein kinase StkP
Gene
stkP, SP_1732
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - 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, 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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421ATP By similarity
Active sitei136 – 1361Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. penicillin binding Source: InterPro
  3. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. barrier septum assembly Source: UniProtKB-KW
  2. pathogenesis Source: UniProtKB-KW
  3. regulation of cell shape Source: UniProtKB-KW
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

Enzyme and pathway databases

BioCyciSPNE170187:GHGN-1739-MONOMER.

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
ProteomesiUP000000585: Chromosome

Subcellular locationi

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 (1 Publication). 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 342342Cytoplasmic By similarity
Add
BLAST
Transmembranei343 – 36321Helical; By similarity
Add
BLAST
Topological domaini364 – 659296Extracellular By similarity
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
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 1 Publication.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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659Serine/threonine-protein kinase StkP
PRO_0000418144Add
BLAST

Post-translational modificationi

Autophosphorylation occurs predominantly at the threonine residue and weakly at the serine residue. Dephosphorylated by PhpP By similarity.1 Publication

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.1 Publication

Protein-protein interaction databases

STRINGi170187.SP_1732.

Structurei

3D structure databases

ProteinModelPortaliQ97PA9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 273262Protein kinase
Add
BLAST
Domaini366 – 43368PASTA 1
Add
BLAST
Domaini434 – 50572PASTA 2
Add
BLAST
Domaini506 – 57772PASTA 3
Add
BLAST
Domaini578 – 65174PASTA 4
Add
BLAST

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.

Sequence similaritiesi

Contains 4 PASTA domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000037186.
KOiK08884.
OMAiMQIPIVN.
OrthoDBiEOG6B35XT.

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.
[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

MIQIGKIFAG RYRIVKQIGR GGMADVYLAK DLILDGEEVA VKVLRTNYQT    50
DPIAVARFQR EARAMADLDH PHIVRITDIG EEDGQQYLAM EYVAGLDLKR 100
YIKEHYPLSN EEAVRIMGQI LLAMRLAHTR GIVHRDLKPQ NILLTPDGTA 150
KVTDFGIAVA FAETSLTQTN SMLGSVHYLS PEQARGSKAT VQSDIYAMGI 200
IFYEMLTGHI PYDGDSAVTI ALQHFQKPLP SVIAENPSVP QALENVIIKA 250
TAKKLTNRYR SVSEMYVDLS SSLSYNRRNE SKLIFDETSK ADTKTLPKVS 300
QSTLTSIPKV QAQTEHKSIK NPSQAVTEET YQPQAPKKHR FKMRYLILLA 350
SLVLVAASLI WILSRTPATI AIPDVAGQTV AEAKATLKKA NFEIGEEKTE 400
ASEKVEEGRI IRTDPGAGTG RKEGTKINLV VSSGKQSFQI SNYVGRKSSD 450
VIAELKEKKV PDNLIKIEEE ESNESEAGTV LKQSLPEGTT YDLSKATQIV 500
LTVAKKATTI QLGNYIGRNS TEVISELKQK KVPENLIKIE EEESSESEPG 550
TIMKQSPGAG TTYDVSKPTQ IVLTVAKKVT SVAMPSYIGS SLEFTKNNLI 600
QIVGIKEANI EVVEVTTAPA GSAEGMVVEQ SPRAGEKVDL NKTRVKISIY 650
KPKTTSATP 659
Length:659
Mass (Da):72,289
Last modified:October 1, 2001 - v1
Checksum:i4723AE1001BCE4CF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005672 Genomic DNA. Translation: AAK75808.1.
PIRiG95201.
RefSeqiNP_346168.1. NC_003028.3.

Genome annotation databases

EnsemblBacteriaiAAK75808; AAK75808; SP_1732.
GeneIDi931099.
KEGGispn:SP_1732.
PATRICi19707915. VBIStrPne105772_1800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005672 Genomic DNA. Translation: AAK75808.1 .
PIRi G95201.
RefSeqi NP_346168.1. NC_003028.3.

3D structure databases

ProteinModelPortali Q97PA9.
ModBasei Search...

Protein-protein interaction databases

STRINGi 170187.SP_1732.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK75808 ; AAK75808 ; SP_1732 .
GeneIDi 931099.
KEGGi spn:SP_1732.
PATRICi 19707915. VBIStrPne105772_1800.

Phylogenomic databases

HOGENOMi HOG000037186.
KOi K08884.
OMAi MQIPIVN.
OrthoDBi EOG6B35XT.

Enzyme and pathway databases

BioCyci SPNE170187:GHGN-1739-MONOMER.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR005543. PASTA_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00740. PASTA. 4 hits.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiSTKP2_STRPN
AccessioniPrimary (citable) accession number: Q97PA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: October 1, 2001
Last modified: September 3, 2014
This is version 99 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

External Data

Dasty 3

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