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Q97PA9

- STKP2_STRPN

UniProt

Q97PA9 - STKP2_STRPN

Protein

Serine/threonine-protein kinase StkP

Gene

stkP

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Oct 2001)
      Previous versions | rss
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    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 – 421ATPPROSITE-ProRule annotation
    Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 269ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    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 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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 659659Serine/threonine-protein kinase StkPPRO_0000418144Add
    BLAST

    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.SP_1732.

    Structurei

    3D structure databases

    ProteinModelPortaliQ97PA9.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 342342CytoplasmicBy similarityAdd
    BLAST
    Topological domaini364 – 659296ExtracellularBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei343 – 36321HelicalBy similarityAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 273262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini366 – 43368PASTA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini434 – 50572PASTA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini506 – 57772PASTA 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini578 – 65174PASTA 4PROSITE-ProRule annotationAdd
    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.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

    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

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    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 100 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