Detailed information    

experimental Experimentally validated

Overview

Name   rcrP   Type   Regulator
Locus tag   SMU_RS04255 Genome accession   NC_004350
Coordinates   875028..876830 (+) Length   600 a.a.
NCBI ID   WP_002263293.1    Uniprot ID   Q8DUK5
Organism   Streptococcus mutans UA159     
Function   regulate competence   
Competence regulation

Function

Mutations in the RcrR binding site impacted expression from the rcrR promoter in vivo and elicited changes in transformation efficiency, competence gene expression, and growth inhibition by competence-stimulating peptide; even when the changes in rcrRPQ transcription were minor. An additional mechanistic linkage of RcrR with competence and (p)ppGpp metabolism was identified by showing that the rRcrR protein could bind to the promoter regions of comX, comYA and relP, although the binding was not as efficient as to the rcrRPQ promoter under the conditions tested.


Related MGE

Note: This gene co-localizes with putative mobile genetic elements (MGEs) in the genome predicted by VRprofile2, as detailed below.

Gene-MGE association summary

MGE type MGE coordinates Gene coordinates Relative position Distance (bp)
Prophage 855756..878574 875028..876830 within 0


Gene organization within MGE regions


Location: 855756..878574
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  SMU_RS04185 (SMU.901) - 855756..856961 (+) 1206 WP_002262894.1 CCA tRNA nucleotidyltransferase -
  SMU_RS04190 (SMU.902) - 856964..858832 (+) 1869 WP_002262895.1 ABC-F family ATP-binding cassette domain-containing protein -
  SMU_RS04195 (SMU.905) - 859289..861025 (+) 1737 WP_002262897.1 ABC transporter ATP-binding protein -
  SMU_RS04200 (SMU.906) - 861036..862808 (+) 1773 WP_002262898.1 ABC transporter ATP-binding protein -
  SMU_RS04205 (SMU.909) - 862924..863844 (+) 921 WP_002262899.1 AEC family transporter -
  SMU_RS04210 (SMU.910) gtfD 864064..868452 (+) 4389 WP_002352262.1 glucosyltransferase-S -
  SMU_RS04215 (SMU.911c) - 868627..869136 (-) 510 WP_002262901.1 DUF308 domain-containing protein -
  SMU_RS04220 (SMU.913) gdhA 869772..871121 (+) 1350 WP_002263849.1 NADP-specific glutamate dehydrogenase -
  SMU_RS04225 (SMU.914c) - 871233..871616 (-) 384 WP_002263287.1 DUF3021 family protein -
  SMU_RS04230 (SMU.915c) queF 871725..872213 (-) 489 WP_002263288.1 preQ(1) synthase -
  SMU_RS04235 (SMU.916c) queE 872226..872942 (-) 717 WP_002263289.1 7-carboxy-7-deazaguanine synthase QueE -
  SMU_RS04240 (SMU.917c) queD 872939..873385 (-) 447 WP_002263290.1 6-carboxytetrahydropterin synthase QueD -
  SMU_RS04245 (SMU.919c) queC 873385..874038 (-) 654 WP_002263291.1 7-cyano-7-deazaguanine synthase QueC -
  SMU_RS04250 (SMU.921) rcrR 874590..875024 (+) 435 WP_002263292.1 MarR family winged helix-turn-helix transcriptional regulator Regulator
  SMU_RS04255 (SMU.922) rcrP 875028..876830 (+) 1803 WP_002263293.1 ABC transporter ATP-binding protein Regulator
  SMU_RS04260 (SMU.923) rcrQ 876820..878574 (+) 1755 WP_002263294.1 ABC transporter ATP-binding protein Regulator

Sequence

Protein


Download         Length: 600 a.a.        Molecular weight: 66968.76 Da        Isoelectric Point: 9.6602

>NTDB_id=369 SMU_RS04255 WP_002263293.1 875028..876830(+) (rcrP) [Streptococcus mutans UA159]
MFKIFKRLNAKEWGMVLLSTAFICLAVWMDLKTPEYMSNITTLLQTKGTTASDIMDPGSKMLMFSFGSFFMAVLVGFLAS
RTAASFTTRLRSDIFNRVMDYSEAEIKKFSIPSLLTRTTNDLTQLQIMIVMGMQVVTRGPIMAVWALTKIWGKSDEWTGA
VGVAVLIVFIMLSVLMFVAFPRQRQVQSLTDALNSTTRESLTGVRVVRAYNAEDYQDTKFKRENKNLTKLNLLVYRLMSL
MNPVMTVVSSGLTLAIYWIGAYLLNDIKIPMTSVTAAKGAIADRISVFSDMVVFSSYAMQVVVGFMMMVAIFIILPRALV
SAKRINEVLALNSSVHFKEYSKADNARKGEVEFHDVSFRYSKNSRAVIEHVSFSAKAGETVAFIGSTGSGKSTLVNLIPR
FYDATEGWIKIDGIKVQDYSHDDLNNKVGYIPQRAVLFSGTIRSNIAFGQSDQAPLDDAKIWEALELAQAKNFVEEKEKG
LDTEVAQGGTNFSGGQKQRLAIARALARKPEILIFDDSFSALDYKTDRILRNDLAKKTKEMTKLIVAQRISTIMDADHIL
VLDQGKVVGQGTHKELLANNDIYQEIAYSQLSKEELENGK

Nucleotide


Download         Length: 1803 bp        

>NTDB_id=369 SMU_RS04255 WP_002263293.1 875028..876830(+) (rcrP) [Streptococcus mutans UA159]
ATGTTTAAAATTTTTAAACGTCTAAATGCTAAAGAATGGGGCATGGTTCTCCTTAGTACTGCCTTTATCTGTTTGGCTGT
CTGGATGGATTTGAAGACGCCCGAATATATGTCCAACATTACAACCTTGCTGCAGACTAAGGGAACGACCGCCTCAGATA
TTATGGATCCGGGATCTAAGATGCTCATGTTTTCATTTGGGAGCTTTTTTATGGCCGTTCTAGTTGGTTTTTTAGCTTCA
AGAACAGCTGCTAGCTTTACGACCCGTCTTCGATCTGATATTTTCAATCGGGTTATGGATTATTCAGAGGCGGAAATCAA
GAAATTTTCCATTCCCAGCCTTCTAACGCGTACGACTAATGATTTGACACAGTTGCAAATCATGATCGTTATGGGAATGC
AAGTGGTGACACGCGGTCCAATCATGGCTGTTTGGGCCTTGACTAAAATCTGGGGTAAAAGCGATGAATGGACAGGAGCA
GTCGGTGTTGCCGTTTTAATTGTCTTTATTATGCTGTCTGTTTTGATGTTTGTCGCTTTTCCAAGACAGCGTCAGGTGCA
GAGCTTGACGGATGCTCTAAATTCTACAACCCGTGAATCTCTGACTGGTGTTCGTGTTGTTCGGGCTTACAATGCAGAAG
ATTATCAGGACACTAAATTTAAGCGGGAAAATAAAAACCTGACGAAATTGAATTTATTGGTCTATCGTCTGATGTCGCTA
ATGAATCCTGTCATGACAGTTGTTTCCAGTGGTCTAACTTTAGCTATTTATTGGATTGGAGCTTACCTGCTCAATGATAT
TAAAATTCCTATGACGAGTGTGACAGCTGCTAAAGGAGCTATTGCTGATCGTATCAGTGTTTTTAGTGATATGGTTGTCT
TTTCATCTTATGCCATGCAGGTTGTTGTCGGTTTTATGATGATGGTCGCTATCTTTATCATTTTACCGCGTGCTTTAGTT
TCTGCCAAACGAATTAATGAAGTATTGGCGCTTAACTCATCTGTACACTTCAAAGAATATTCTAAAGCAGACAATGCTCG
AAAAGGAGAAGTCGAATTTCATGATGTATCGTTTCGTTACAGTAAAAATTCTCGTGCGGTTATTGAGCATGTGTCTTTCA
GTGCTAAAGCTGGTGAGACAGTTGCTTTTATTGGTTCCACTGGCTCAGGAAAATCAACTCTTGTTAATCTGATTCCTCGT
TTTTATGATGCTACAGAAGGTTGGATTAAGATAGATGGAATCAAAGTGCAAGATTACAGCCATGATGACCTCAACAATAA
AGTCGGCTATATTCCGCAAAGGGCAGTGCTTTTTAGTGGGACCATTCGTTCTAATATTGCATTTGGGCAAAGCGATCAAG
CGCCGCTTGATGATGCTAAAATTTGGGAGGCTCTTGAACTAGCCCAAGCCAAAAACTTTGTTGAAGAAAAAGAAAAGGGT
CTGGATACCGAGGTAGCTCAAGGCGGTACCAACTTCTCTGGCGGTCAAAAGCAGCGCTTAGCTATTGCCCGTGCACTTGC
ACGCAAACCAGAAATTCTTATTTTTGATGACTCCTTCTCAGCTCTTGATTATAAGACGGATCGCATTCTGCGAAATGATT
TGGCAAAGAAAACCAAAGAAATGACTAAGTTGATTGTAGCCCAACGTATTTCAACTATTATGGATGCTGATCATATTTTG
GTCTTAGATCAGGGAAAGGTTGTTGGTCAAGGAACACACAAGGAATTACTGGCTAATAACGATATTTATCAAGAAATTGC
TTATTCACAACTATCTAAGGAGGAGTTAGAAAATGGAAAATAA

Domains

Predicted by InterproScan.

ABC transporter (ABC_tran)

(369-518)

ABC transporter transmembrane region (ABC_membrane)

(17-266)


Secondary structure

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



3D structure

Source ID Structure
  AlphaFold DB Q8DUK5

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

References

[1] Robert C Shields et al. (2020) Peptides encoded in the Streptococcus mutans RcrRPQ operon are essential for thermotolerance. Microbiology (Reading, England) 166(3):306-317. [PMID: 31935187]
[2] Kinda Seaton et al. (2015) Regulation of competence and gene expression in Streptococcus mutans by the RcrR transcriptional regulator. Molecular Oral Microbiology 30(2):147-159. [PMID: 25146832]
[3] Robert C Shields et al. (2015) Conserved and divergent functions of RcrRPQ in Streptococcus gordonii and S. mutans. FEMS Microbiology Letters 362(16):fnv119. [PMID: 26229070]
[4] Sang-Joon Ahn et al. (2014) Discovery of novel peptides regulating competence development in Streptococcus mutans. Journal of Bacteriology 196(21):3735-45. [PMID: 25135217]
[5] Kinda Seaton et al. (2011) A transcriptional regulator and ABC transporters link stress tolerance, (p)ppGpp, and genetic competence in Streptococcus mutans. Journal of Bacteriology 193(4):862-74. [PMID: 21148727]