Detailed information    

experimental Experimentally validated

Overview


Name   pilQ   Type   Machinery gene
Locus tag   TT_RS05145 Genome accession   NC_005835
Coordinates   994961..997234 (+) Length   757 a.a.
NCBI ID   WP_011173436.1    Uniprot ID   -
Organism   Thermus thermophilus HB27     
Function   assembly of type IV pilus   
DNA binding and uptake

Function


PilQ forms macromolecular complexes which consist of 13 protomers forming a stable cone and a cup structure and six stacked rings (N0–N5) with a large central channel. The PilQ complex is highly dynamic and undergoes major conformational changes by opening and closing of two periplasmic gates, thereby making way for pilus extrusion.


Genomic Context


Location: 989961..1002234
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  TT_RS05115 (TT_C1011) - 990085..990576 (+) 492 WP_011173430.1 DUF5317 domain-containing protein -
  TT_RS05120 (TT_C1012) - 990630..991634 (+) 1005 WP_011173431.1 homoisocitrate dehydrogenase -
  TT_RS05125 (TT_C1013) pilM 991769..992902 (+) 1134 WP_011173432.1 type IV pilus assembly protein PilM Machinery gene
  TT_RS05130 (TT_C1014) pilN 992895..993518 (+) 624 WP_011173433.1 competence protein Machinery gene
  TT_RS05135 (TT_C1015) pilO 993508..994089 (+) 582 WP_011173434.1 type 4a pilus biogenesis protein PilO Machinery gene
  TT_RS05140 (TT_C1016) pilW 994086..994964 (+) 879 WP_011173435.1 hypothetical protein Machinery gene
  TT_RS05145 (TT_C1017) pilQ 994961..997234 (+) 2274 WP_011173436.1 secretin N-terminal domain-containing protein Machinery gene
  TT_RS05150 (TT_C1018) aroC 997293..998444 (+) 1152 WP_011173437.1 chorismate synthase -
  TT_RS05155 (TT_C1019) - 998469..999023 (+) 555 WP_011173438.1 shikimate kinase -
  TT_RS05160 (TT_C1020) - 999001..1000047 (+) 1047 WP_011173439.1 3-dehydroquinate synthase -
  TT_RS05165 (TT_C1021) rsmF 1000093..1001463 (-) 1371 WP_041443492.1 16S rRNA (cytosine(1407)-C(5))-methyltransferase RsmF -
  TT_RS05170 (TT_C1022) - 1001516..1001893 (+) 378 WP_011173441.1 4'-phosphopantetheinyl transferase superfamily protein -
  TT_RS05175 (TT_C1023) - 1001871..1002224 (-) 354 WP_011173442.1 DUF4870 domain-containing protein -

Sequence


Protein


Download         Length: 757 a.a.        Molecular weight: 82637.62 Da        Isoelectric Point: 5.1292

>NTDB_id=1027 TT_RS05145 WP_011173436.1 994961..997234(+) (pilQ) [Thermus thermophilus HB27]
MKSAWIRAAVIALAGLGAFALAGSFPEEPRFQAPVNLKVSESQVKAGQTLPLDVVLEALARSVGLQPLIYRAYDPSGDPA
TAQPPLPNVKLDFQGKPFREVWDLLFATYGNQYSLDYLFLPPDVVVVAPTQVITALVDAPSRTGAMERRPYIVGVPEIAY
KRTETDAQGQPRTVVNIEGAKAWVQNDLLPFLSREAAGLNVNWIVVEEGGRLKAVLSVLATPEQHARFSDILQRAGIDFR
PLPALAQPKPRVEKTYTLTYATFPDLLAFLQSRLPEAQIGVVPTNPQRAIVLATEEDHARLSELLKTADVPKTVRRVYTL
QNLTFAEAQERLKPLLEKDLKGARLESLPGNPKALLLEAPEAEHALFAEILKALDVPPQAPQAPQEATLRRLYPLHYANA
EQVAPFLAREVPGIVVQTVPGQPLLSVRGTEAQLREVESLLAQIDRPPEQGPPVFQRAYQLSNAKAVELAQVLQEALKAR
QAQNQGQQNQAPPTREATVVADPRTNTLIVTGTQEDLALVEGLIPKLDQPVPQVNLRVRIQEVQSNLTRSLGLKWNSIAG
GNVAASILDSGLSLIFDSTRSLAALNIMATLDALQQQGLSRALRDVNQTVLNNQTARLQSGETFFIRRVVNDQVERVPFD
VGLIVEVTPQITADGQILLNIKAEVSGNVQRNPVDGDVDRFTKQVVTTTLRVKDGETVVLGGLTSQESNQSQQGVPLLMD
IPLIGELFKQRTNESTDKELLVVITADILKEAASANP

Nucleotide


Download         Length: 2274 bp        

>NTDB_id=1027 TT_RS05145 WP_011173436.1 994961..997234(+) (pilQ) [Thermus thermophilus HB27]
ATGAAGAGCGCGTGGATCCGTGCGGCCGTGATCGCCCTCGCAGGGCTAGGGGCTTTTGCCCTTGCGGGGAGCTTTCCCGA
GGAGCCCCGCTTCCAGGCCCCGGTGAACCTCAAGGTCTCGGAATCCCAGGTCAAGGCGGGCCAGACCCTGCCCTTGGACG
TGGTCCTCGAGGCCCTGGCGCGAAGCGTGGGGCTCCAGCCCCTCATCTACCGGGCCTACGACCCGAGCGGGGACCCCGCC
ACGGCCCAGCCCCCCCTGCCCAACGTCAAGCTGGACTTCCAGGGCAAGCCCTTCCGGGAGGTCTGGGACCTCCTCTTCGC
CACCTACGGCAACCAGTACAGCCTGGACTACCTCTTCCTGCCCCCCGACGTGGTGGTGGTGGCCCCCACCCAGGTGATCA
CCGCCCTGGTGGACGCCCCGAGCCGCACGGGGGCCATGGAGCGCAGGCCCTACATCGTGGGCGTCCCCGAGATCGCCTAC
AAGCGCACGGAGACGGACGCCCAGGGCCAGCCCCGCACGGTCGTCAACATCGAGGGCGCCAAGGCCTGGGTCCAGAACGA
TCTCCTCCCCTTCCTCTCCCGGGAGGCGGCGGGGCTCAACGTGAACTGGATCGTGGTGGAGGAAGGGGGTAGGCTCAAGG
CCGTCCTCTCCGTCCTCGCCACCCCCGAGCAGCACGCCCGCTTCTCCGATATCCTGCAGCGGGCCGGGATTGACTTCCGC
CCCCTCCCCGCCCTGGCCCAGCCTAAGCCCCGGGTGGAGAAGACCTACACCCTCACCTACGCCACCTTCCCCGACCTCCT
CGCCTTCCTCCAGTCCCGTCTCCCCGAGGCCCAGATCGGCGTGGTCCCCACCAACCCCCAAAGGGCCATCGTCCTCGCCA
CCGAGGAGGACCACGCCCGCTTGAGCGAGCTTCTGAAGACGGCCGACGTCCCCAAGACCGTCCGCCGGGTCTACACCCTG
CAGAACCTCACCTTCGCCGAGGCCCAGGAGCGCCTAAAGCCCCTCCTGGAGAAGGACCTCAAGGGGGCCCGCCTGGAAAG
CCTCCCCGGCAACCCCAAGGCCCTCCTCCTCGAGGCCCCCGAGGCTGAGCACGCCCTCTTCGCCGAGATCCTGAAGGCCC
TGGACGTCCCCCCCCAGGCCCCCCAAGCCCCCCAGGAGGCCACCTTGCGGCGCCTCTACCCCCTGCACTACGCCAACGCC
GAGCAGGTGGCCCCCTTCCTCGCCCGGGAGGTGCCGGGGATCGTGGTCCAGACCGTCCCCGGCCAACCCCTCCTCTCGGT
GAGGGGCACGGAAGCGCAGCTTAGGGAGGTGGAAAGCCTCCTCGCCCAGATTGACCGCCCCCCGGAGCAGGGCCCTCCCG
TGTTCCAGCGGGCCTACCAGCTCTCCAACGCCAAGGCGGTGGAGCTCGCCCAGGTGCTCCAGGAGGCGCTCAAGGCCCGG
CAGGCCCAGAACCAGGGCCAGCAGAACCAGGCCCCCCCCACCCGGGAGGCCACGGTGGTGGCCGACCCCAGGACCAACAC
CCTCATCGTCACCGGCACCCAGGAGGACCTCGCCCTGGTGGAGGGCCTCATCCCCAAGCTGGACCAGCCCGTGCCCCAGG
TGAACCTCAGGGTGCGCATCCAGGAGGTCCAGTCCAACCTGACCCGCAGCCTCGGCCTCAAGTGGAACAGCATCGCCGGC
GGCAACGTGGCGGCCAGCATCCTGGACTCGGGCCTTTCCCTCATCTTTGACTCCACGCGAAGCCTCGCCGCCCTCAACAT
CATGGCCACCCTGGACGCCCTGCAGCAACAGGGCCTCTCCCGGGCCCTCCGGGACGTGAACCAGACCGTCCTCAACAACC
AAACCGCCCGCCTGCAGTCCGGCGAGACCTTCTTCATCCGGCGGGTGGTGAACGACCAGGTGGAACGGGTCCCCTTTGAC
GTGGGGCTCATCGTGGAGGTCACGCCCCAGATCACCGCCGACGGCCAGATCCTCCTCAACATCAAGGCCGAGGTCTCGGG
GAACGTGCAGCGCAACCCCGTGGACGGGGACGTGGACCGCTTCACCAAGCAGGTGGTGACCACCACCCTCAGGGTCAAAG
ACGGGGAGACCGTGGTCCTCGGGGGCCTCACCTCCCAGGAGTCCAACCAGAGCCAGCAGGGGGTGCCCCTCCTCATGGAC
ATCCCCCTGATCGGCGAGCTCTTCAAGCAGCGGACGAACGAGAGCACCGACAAGGAGCTTTTGGTGGTGATCACCGCCGA
CATCCTCAAGGAGGCGGCCTCGGCGAACCCCTAA


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] Deniz Yaman et al. (2024) Identification of subcomplexes and protein-protein interactions in the DNA transporter of Thermus thermophilus HB27. Biochimica Et Biophysica Acta. Biomembranes 1866(7):184363. [PMID: 38909880]
[2] Beate Averhoff et al. (2021) Natural transformation in Gram-negative bacteria thriving in extreme environments: from genes and genomes to proteins, structures and regulation. Extremophiles : Life Under Extreme Conditions 25(5-6):425-436. [PMID: 34542714]
[3] Edoardo D'Imprima et al. (2017) Cryo-EM structure of the bifunctional secretin complex of Thermus thermophilus. ELife 6:e30483. [PMID: 29280731]
[4] Ralf Salzer et al. (2016) Topology and Structure/Function Correlation of Ring- and Gate-forming Domains in the Dynamic Secretin Complex of Thermus thermophilus. The Journal of Biological Chemistry 291(28):14448-56. [PMID: 27226590]
[5] Vicki A M Gold et al. (2015) Structure of a type IV pilus machinery in the open and closed state. ELife 4:e07380. [PMID: 25997099]
[6] Janin Burkhardt et al. (2012) Unusual N-terminal ααβαββα fold of PilQ from Thermus thermophilus mediates ring formation and is essential for piliation. The Journal of Biological Chemistry 287(11):8484-94. [PMID: 22253437]
[7] Janin Burkhardt et al. (2011) Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27. The Journal of Biological Chemistry 286(12):9977-84. [PMID: 21285351]
[8] Cornelia Schwarzenlander et al. (2009) The role of single subunits of the DNA transport machinery of Thermus thermophilus HB27 in DNA binding and transport. Environmental Microbiology 11(4):801-8. [PMID: 19396940]
[9] Judit Rumszauer et al. (2006) Identification, subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27. The FEBS Journal 273(14):3261-72. [PMID: 16857013]
[10] Alexandra Friedrich et al. (2002) Molecular analyses of the natural transformation machinery and identification of pilus structures in the extremely thermophilic bacterium Thermus thermophilus strain HB27. Applied And Environmental Microbiology 68(2):745-55. [PMID: 11823215]