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Q97PA9

- STKP2_STRPN

UniProt

Q97PA9 - STKP2_STRPN

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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: 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 – 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
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 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 342342CytoplasmicBy similarityAdd
BLAST
Transmembranei343 – 36321HelicalBy similarityAdd
BLAST
Topological domaini364 – 659296ExtracellularBy similarityAdd
BLAST

GO - Cellular componenti

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

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

« 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.
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:
EMBLi
GenBanki
DDBJi
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

« 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: October 29, 2014
This is version 101 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