Detailed information    

experimental Experimentally validated

Overview

Name   pilQ   Type   Machinery gene
Locus tag   DR_RS03995 Genome accession   NC_001263
Coordinates   790281..791549 (+) Length   422 a.a.
NCBI ID   WP_227086002.1    Uniprot ID   -
Organism   Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539     
Function   assembly of type IV pilus   
DNA binding and uptake

Function

We identified the factors (PilQ, PilD, type IV pilins, PilB, PilT, ComEC-ComEA, and ComF) involved in DNA uptake and DNA translocation across the external and cytoplasmic membranes and showed that the DNA-uptake machinery is similar to that described in the Gram negative bacterium Vibrio cholerae.


Genomic Context

Location: 785281..796549
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  DR_RS03980 (DR_0771) - 786047..786763 (+) 717 WP_010887417.1 hypothetical protein -
  DR_RS03985 (DR_0772) pilO 786760..787419 (+) 660 WP_010887418.1 type 4a pilus biogenesis protein PilO -
  DR_RS03990 (DR_0773) - 787416..789323 (+) 1908 WP_010887419.1 hypothetical protein -
  DR_RS03995 pilQ 790281..791549 (+) 1269 WP_227086002.1 type II secretion system protein GspD Machinery gene
  DR_RS04005 (DR_0775) aroC 791813..792961 (+) 1149 WP_010887421.1 chorismate synthase -
  DR_RS04010 (DR_0776) - 793095..793685 (+) 591 WP_034350371.1 shikimate kinase -
  DR_RS04015 (DR_0777) aroB 793672..794724 (+) 1053 WP_010887423.1 3-dehydroquinate synthase -
  DR_RS04020 (DR_0778) aroQ 794873..795304 (+) 432 WP_010887424.1 type II 3-dehydroquinate dehydratase -
  DR_RS04030 (DR_0779) - 795301..796278 (+) 978 WP_027479984.1 alpha/beta hydrolase -

Sequence

Protein


Download         Length: 422 a.a.        Molecular weight: 44190.66 Da        Isoelectric Point: 5.4747

>NTDB_id=1304 DR_RS03995 WP_227086002.1 790281..791549(+) (pilQ) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
MQRIYTVRGQAADITALLAAQYPTLRVTPVGQTGQLVLNGAQAQLDTALALLEQVDRPAPVAESRTVQRVFQLVNASAEE
VKATLEGTLARDLTADSNNDVLPNVPVTATDANGNTTVVSVPNALGKTANQGTANAQAQTAQTPANTQQATLIADKRTNS
LIVRGTPEQVAQVAELVPQLDQVVPQINVQVRIQEVNERALQSLGLNWRATFGGFNVAVSGGTGLAATFNPTQSFLGFNI
FPTLTALETQGLTRRVYDGNVTMQSGQRSLSATGGAQNASSGAAASVKSGGRLEINIPSAAGNIVRQIDYGLNLDFFSPQ
VAPDGTITLRIRGQVNQPATAITADSLPNLIDFTNSEAQSTITFKNGQTILMSGLLGSTETTNRSGVPFLSSLPGVGAAF
GEKRTEKTQSQLLVIITGTVVK

Nucleotide


Download         Length: 1269 bp        

>NTDB_id=1304 DR_RS03995 WP_227086002.1 790281..791549(+) (pilQ) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
GTGCAGCGCATCTACACCGTGCGCGGCCAGGCCGCCGACATCACGGCGCTGCTCGCTGCCCAGTACCCTACCCTGCGCGT
GACCCCGGTGGGGCAGACCGGCCAACTGGTGCTCAACGGCGCTCAGGCCCAGCTCGACACGGCGCTCGCCCTGCTCGAAC
AGGTGGACCGCCCCGCCCCGGTGGCCGAGTCCCGTACCGTTCAGCGCGTCTTCCAGCTCGTCAACGCCAGCGCTGAGGAA
GTCAAGGCGACCCTGGAAGGCACCCTGGCGCGTGACCTGACCGCCGACAGCAATAACGACGTGCTGCCCAACGTGCCCGT
CACCGCCACCGACGCCAACGGCAACACGACCGTGGTGAGCGTGCCCAACGCGCTCGGCAAGACGGCGAACCAGGGCACGG
CGAATGCTCAGGCTCAGACTGCCCAGACTCCGGCCAACACCCAGCAGGCGACCCTGATCGCCGACAAGCGCACCAACAGC
CTGATCGTGCGCGGCACGCCCGAACAGGTGGCGCAGGTGGCCGAGCTGGTGCCGCAGCTCGATCAGGTGGTGCCGCAGAT
CAACGTGCAGGTGCGGATTCAGGAGGTCAACGAGCGAGCGCTGCAATCGCTGGGCCTCAACTGGCGGGCGACCTTCGGTG
GCTTCAACGTGGCGGTCTCGGGCGGCACCGGGCTGGCGGCCACCTTCAACCCCACCCAGAGCTTCCTCGGTTTCAACATT
TTCCCGACCCTCACGGCGCTCGAAACCCAGGGCCTGACCCGGCGCGTGTACGACGGCAACGTGACCATGCAAAGCGGCCA
GCGCTCGCTGAGTGCCACGGGCGGCGCCCAGAACGCTTCGAGCGGCGCGGCGGCCAGCGTCAAGAGTGGGGGCCGACTGG
AAATCAACATCCCCTCGGCGGCGGGCAACATCGTGCGGCAGATCGATTACGGTCTCAACCTCGATTTCTTCAGCCCGCAG
GTGGCGCCCGACGGCACCATCACCCTGCGTATTCGCGGTCAGGTCAACCAGCCGGCAACGGCGATCACCGCCGACAGCCT
GCCCAACCTCATCGACTTCACCAACAGCGAAGCGCAAAGCACCATCACCTTCAAGAACGGCCAGACCATCCTGATGAGCG
GCCTGCTCGGCAGCACCGAGACCACCAACCGCAGCGGCGTGCCCTTCCTGAGCAGCCTGCCCGGTGTGGGCGCGGCCTTC
GGGGAAAAACGCACCGAGAAGACCCAGTCGCAACTGCTCGTCATCATCACCGGCACCGTCGTCAAATAA

Domains

Predicted by InterproScan.

Bacterial type II and III secretion system protein (Secretin)

(279-422)

Bacterial type II/III secretion system short domain (Secretin_N)

(69-185)


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

References

[1] Solenne Ithurbide et al. (2020) Natural Transformation in Deinococcus radiodurans: A Genetic Analysis Reveals the Major Roles of DprA, DdrB, RecA, RecF, and RecO Proteins. Frontiers in Microbiology 11:1253. [PMID: 32625182]