Detailed information    

experimental Experimentally validated

Overview

Name   pilW   Type   Machinery gene
Locus tag   TT_RS05140 Genome accession   NC_005835
Coordinates   994086..994964 (+) Length   292 a.a.
NCBI ID   WP_011173435.1    Uniprot ID   Q72IW5
Organism   Thermus thermophilus HB27     
Function   assembly of type IV pilus   
DNA binding and uptake

Function

PilW is essential for natural transformation and piliation and yeast twohybrid analyses revealed that PilW interacts with the N1 domain of PilQ and a combination of N0 and N1 domains of PilQ. PilW and PilQ form heteropolymeric macromolecular complexes and that PilW is essential for stability of PilQ monomers and PilQ complexes. A central disordered region in PilW is important for pilus dynamics.


Genomic Context

Location: 989086..999964
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 -

Sequence

Protein


Download         Length: 292 a.a.        Molecular weight: 29866.36 Da        Isoelectric Point: 4.6515

>NTDB_id=1026 TT_RS05140 WP_011173435.1 994086..994964(+) (pilW) [Thermus thermophilus HB27]
MKNAWQRLKEAWANLPRSTKLLLAALLLVGGVALWYVGLYLPAQVAEAPTPAPSTQVIEAPPIPPLASQEEAKPQAEAPA
QEEAQAPASSQEEAQAPPPAPVARAEPPPPNPFVPLVVETPPPPPASASRPTPVPEGPAVRVQTPAQAPQAAPATRPIPG
TSGALPAPKILSPALSAPLPQARETPPRVAVPTALVEAPLPGPEEKGAEKAPTPASPLERLVAEKGLRLSGTLLGPVSVA
ILESKEGYLVVPAGSPIPGTEAVVRQVEEGSVTLALKEETLNLSLVQAGGGQ

Nucleotide


Download         Length: 879 bp        

>NTDB_id=1026 TT_RS05140 WP_011173435.1 994086..994964(+) (pilW) [Thermus thermophilus HB27]
ATGAAGAACGCCTGGCAACGCCTGAAGGAAGCCTGGGCCAACCTGCCCAGGTCCACCAAGCTCCTCCTGGCGGCCCTCCT
TCTCGTGGGGGGCGTGGCCCTTTGGTACGTGGGCCTCTACCTCCCGGCCCAGGTGGCGGAAGCGCCCACCCCGGCCCCCT
CCACGCAGGTCATCGAGGCCCCCCCGATCCCGCCCCTCGCCTCCCAGGAAGAGGCCAAGCCACAGGCCGAAGCCCCGGCC
CAAGAGGAGGCCCAGGCGCCCGCTTCTTCCCAAGAGGAGGCCCAGGCGCCCCCGCCTGCCCCCGTGGCCCGGGCCGAGCC
CCCGCCCCCGAACCCCTTCGTCCCCCTGGTGGTGGAAACCCCACCCCCACCTCCGGCCTCCGCCTCCCGCCCCACGCCCG
TCCCCGAGGGGCCCGCCGTCCGGGTCCAGACCCCCGCCCAAGCCCCCCAGGCGGCCCCCGCCACCCGGCCCATCCCCGGG
ACCTCCGGCGCCCTCCCGGCGCCCAAGATCCTCTCCCCCGCGCTGTCCGCCCCCCTGCCCCAGGCCAGGGAGACGCCGCC
TAGGGTCGCCGTGCCCACGGCGCTCGTGGAGGCCCCCCTCCCCGGGCCCGAGGAAAAGGGGGCGGAGAAGGCCCCCACCC
CGGCCTCGCCGCTGGAGCGCCTGGTGGCGGAAAAGGGCCTCCGCCTCTCGGGGACCCTGCTCGGCCCCGTGAGCGTGGCC
ATCCTGGAGAGCAAGGAGGGCTACCTCGTCGTCCCGGCGGGAAGCCCCATCCCCGGCACGGAGGCCGTGGTGCGCCAGGT
GGAGGAAGGAAGCGTGACCCTGGCCTTGAAGGAGGAAACCTTGAACCTGTCCCTCGTCCAAGCTGGAGGTGGCCAATGA

Domains


No domain identified.



Secondary structure

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



3D structure

Source ID Structure
  AlphaFold DB Q72IW5

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] Deniz Yaman et al. (2021) Functional dissection of structural regions of the Thermus thermophilus competence protein PilW: Implication in secretin complex stability, natural transformation and pilus functions. Biochimica Et Biophysica Acta. Biomembranes 1863(10):183666. [PMID: 34143999]
[3] 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]
[4] Chengyun Li et al. (2013) Type IV pilus proteins form an integrated structure extending from the cytoplasm to the outer membrane. PloS One 8(7):e70144. [PMID: 23922942]
[5] 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]
[6] 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]
[7] 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]