Detailed information    

experimental Experimentally validated

Overview


Name   pknB   Type   Regulator
Locus tag   SMU_RS02325 Genome accession   NC_004350
Coordinates   452362..454212 (+) Length   616 a.a.
NCBI ID   WP_002263039.1    Uniprot ID   A0AAX1K050
Organism   Streptococcus mutans UA159     
Function   modulate the activity of ComDE; modulate the activity of VicKR   
Competence regulation

Function


A pknB mutant showed reduced expression of genes involved in bacteriocin production and genetic competence. PknB may modulate the activity of the two-component signal transduction systems VicKR and ComDE.


Genomic Context


Location: 447362..459212
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  SMU_RS02310 (SMU.481) fmt 449345..450280 (+) 936 WP_002263042.1 methionyl-tRNA formyltransferase -
  SMU_RS02315 (SMU.482) rsmB 450261..451583 (+) 1323 WP_002291122.1 16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB -
  SMU_RS02320 (SMU.483) - 451622..452365 (+) 744 WP_002263040.1 Stp1/IreP family PP2C-type Ser/Thr phosphatase -
  SMU_RS02325 (SMU.484) pknB 452362..454212 (+) 1851 WP_002263039.1 Stk1 family PASTA domain-containing Ser/Thr kinase Regulator
  SMU_RS02330 (SMU.485) liaF 454653..455348 (+) 696 WP_002263038.1 cell wall-active antibiotics response protein LiaF -
  SMU_RS02335 (SMU.486) - 455345..456349 (+) 1005 WP_002263037.1 sensor histidine kinase -
  SMU_RS02340 (SMU.487) - 456342..456983 (+) 642 WP_002263036.1 response regulator transcription factor -
  SMU_RS02345 (SMU.488) - 457027..458442 (+) 1416 WP_002263035.1 Cof-type HAD-IIB family hydrolase -
  SMU_RS02350 (SMU.489) - 458426..458812 (+) 387 WP_002263034.1 S1 RNA-binding domain-containing protein -

Sequence


Protein


Download         Length: 616 a.a.        Molecular weight: 66913.66 Da        Isoelectric Point: 9.4520

>NTDB_id=384 SMU_RS02325 WP_002263039.1 452362..454212(+) (pknB) [Streptococcus mutans UA159]
MIQIGKLFAGRYRILQSIGRGGMADVYLANDLILDNEEVAIKVLRTNYQTDQVAVTRFQREARAMAELNHPNIVAIRDIG
EEDGQQFLAMEYVDGADLKKYIQDHAPLSNAEVIRIMKEVLSAMTLAHQKGIIHRDLKPQNVLLTKDGTAKVTDFGIAVA
FAETSLTQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQKPLPSIIAENKNVP
QALENVVIKATAKRLTDRYHSTQEMLQDLRTSLQPNRSRERKLVFSDASDTKPLPKLEQAAANSLAAQSLKNKTSNQDKV
DHKSKPKTKPQPKPKKKRHFLARFFKIFFILVAIGIAVLTYLVLTKPSTVSVPDVSGDKLSTAKMIIRKSGLKVGDVQKI
EDDNVGAGKVVRTNPSAGSKKREGSSVDIFVASAKGFKMEDYTGQDYKDAIDNLTNNYGVSRDSIVLKEVSSDDYSGGTV
IGQSPKPGKTYHPSSDKKITLKVVKVTMPNLKNSTYEEAVSTLTAMGISSSRIKAYDASDYSSEISSPSSSSLVVGQSPY
YGNTVSLSSNDDIILYVSTSGGSHSGSSSSESSNSEGTTSSEASTDSSSSATTTSH

Nucleotide


Download         Length: 1851 bp        

>NTDB_id=384 SMU_RS02325 WP_002263039.1 452362..454212(+) (pknB) [Streptococcus mutans UA159]
ATGATTCAGATTGGCAAATTATTTGCTGGTCGTTATCGGATTCTCCAGTCTATCGGACGAGGTGGGATGGCGGATGTTTA
TTTAGCTAATGATTTGATTTTAGATAATGAGGAAGTGGCCATTAAGGTTCTACGTACGAATTATCAGACAGATCAGGTTG
CTGTGACACGTTTTCAGCGGGAAGCACGTGCCATGGCAGAACTTAATCATCCTAATATTGTAGCCATTCGTGACATTGGA
GAAGAAGACGGTCAGCAATTCCTTGCAATGGAATATGTTGATGGCGCCGACTTGAAGAAATACATTCAAGATCACGCTCC
TTTATCAAATGCTGAAGTCATTAGAATCATGAAAGAGGTTCTTTCTGCTATGACTCTTGCCCACCAAAAGGGCATTATTC
ATCGGGATTTAAAACCTCAAAATGTTTTACTGACCAAAGATGGAACGGCTAAAGTAACAGACTTTGGTATTGCTGTGGCT
TTTGCTGAAACGAGTTTGACCCAAACCAATTCAATGCTGGGTTCAGTACATTACTTATCTCCTGAACAGGCGCGTGGTTC
TAAGGCTACTGTTCAAAGTGATATCTATGCAATGGGGATTATGCTTTTTGAAATGCTGACAGGGCATATTCCCTATGATG
GCGATAGTGCTGTTACAATTGCTTTGCAGCATTTTCAAAAGCCTTTACCATCTATTATTGCTGAGAATAAAAATGTCCCT
CAAGCTCTTGAAAATGTTGTTATTAAAGCAACAGCTAAACGATTAACGGACCGCTATCATTCAACGCAGGAGATGTTGCA
GGATTTAAGAACGTCTCTGCAGCCGAATCGCAGCCGTGAAAGAAAGCTTGTTTTCAGTGATGCTTCAGATACAAAACCAC
TACCAAAACTGGAACAGGCAGCAGCAAACTCTTTAGCTGCTCAGTCCTTAAAAAACAAAACTTCCAATCAGGATAAAGTA
GATCATAAATCTAAGCCTAAAACCAAACCACAACCTAAGCCTAAGAAAAAAAGACATTTTTTAGCTCGTTTCTTTAAAAT
CTTCTTTATATTAGTTGCCATTGGTATTGCTGTTTTGACCTACCTGGTTCTGACAAAACCGAGTACTGTTTCAGTTCCTG
ACGTTTCAGGAGATAAATTATCAACGGCCAAGATGATTATTAGAAAATCGGGTCTTAAGGTGGGTGACGTTCAAAAAATT
GAGGATGATAACGTTGGTGCTGGAAAGGTCGTAAGAACTAATCCAAGTGCAGGCAGTAAAAAACGTGAAGGTTCTAGTGT
TGATATTTTTGTAGCTAGTGCTAAGGGATTTAAGATGGAGGACTATACCGGTCAAGATTACAAGGATGCTATTGATAATC
TGACTAATAATTATGGTGTTTCTAGGGACAGTATTGTTCTTAAGGAAGTTTCATCTGATGACTACAGTGGTGGAACTGTT
ATCGGTCAATCACCAAAACCCGGAAAGACCTATCATCCTAGCAGTGATAAAAAAATAACTCTCAAGGTTGTCAAAGTCAC
TATGCCAAATCTTAAAAATTCTACTTATGAAGAGGCTGTCAGTACTTTAACAGCTATGGGGATTTCTTCAAGCCGTATAA
AAGCTTATGATGCCAGCGATTACTCATCAGAAATTTCATCACCATCATCTTCGTCACTCGTTGTCGGTCAAAGTCCTTAT
TATGGTAATACTGTCAGTCTGTCATCTAATGATGATATTATCTTGTATGTTTCAACATCAGGTGGCTCTCATTCTGGTTC
GTCGTCGTCTGAATCTTCGAACAGTGAAGGAACAACATCAAGCGAAGCCTCGACAGACTCTAGTTCAAGTGCGACGACAA
CTTCACATTAA


Secondary structure


Protein secondary structures were predicted by S4PRED and visualized by seqviz.



3D structure


Source ID Structure

Transmembrane helices


Transmembrane helices of protein were predicted by TMHMM 2.0 and visualized by seqviz and ECharts.



Visualization of predicted probability:


Similar proteins


Only experimentally validated proteins are listed.

Protein Organism Identities (%) Coverage (%) Ha-value
  stkP/pknB Streptococcus salivarius strain HSISS4

62.919

96.753

0.609

  stkP Streptococcus pneumoniae TIGR4

52.381

98.864

0.518

  stkP Streptococcus pneumoniae D39

52.217

98.864

0.516

  stkP Streptococcus pneumoniae R6

52.217

98.864

0.516

  stkP Streptococcus pneumoniae Rx1

52.053

98.864

0.515


Multiple sequence alignment    



References


[1] Michael Reck et al. (2016) Carolacton Treatment Causes Delocalization of the Cell Division Proteins PknB and DivIVa in Streptococcus mutans in vivo. Frontiers in Microbiology 7:684. [PMID: 27242711]
[2] Michael Reck et al. (2011) The biofilm inhibitor carolacton disturbs membrane integrity and cell division of Streptococcus mutans through the serine/threonine protein kinase PknB. Journal of Bacteriology 193(20):5692-706. [PMID: 21840978]
[3] Liliana Danusia Banu et al. (2010) The Streptococcus mutans serine/threonine kinase, PknB, regulates competence development, bacteriocin production, and cell wall metabolism. Infection And Immunity 78(5):2209-20. [PMID: 20231406]
[4] Haitham Hussain et al. (2006) A eukaryotic-type serine/threonine protein kinase is required for biofilm formation, genetic competence, and acid resistance in Streptococcus mutans. Journal of Bacteriology 188(4):1628-32. [PMID: 16452447]