Detailed information    

experimental Experimentally validated

Overview

Name   pilA/pilA2   Type   Machinery gene
Locus tag   TT_RS04320 Genome accession   NC_005835
Coordinates   831932..832513 (+) Length   193 a.a.
NCBI ID   WP_011173284.1    Uniprot ID   Q72JC3
Organism   Thermus thermophilus HB27     
Function   assembly of type IV pilus   
DNA binding and uptake

Function

A subcomplex in the IM comprising of PilMNOC forms the base for retraction and extension of the T4P structures comprising the major pilin PilA4 and the DNA translocator pseudopilus comprising PilA4 and the minor pilins PilA1–3.


Genomic Context

Location: 826932..837513
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  TT_RS04300 (TT_C0851) ilvN 827938..828450 (-) 513 WP_011173280.1 acetolactate synthase small subunit -
  TT_RS04305 (TT_C0852) ilvB 828447..830135 (-) 1689 WP_011173281.1 biosynthetic-type acetolactate synthase large subunit -
  TT_RS04310 (TT_C0853) - 830290..831270 (-) 981 WP_011173282.1 YpdA family putative bacillithiol disulfide reductase -
  TT_RS04315 (TT_C0854) pilA/pilA1 831428..831898 (+) 471 WP_011173283.1 GspH/FimT family protein Machinery gene
  TT_RS04320 (TT_C0855) pilA/pilA2 831932..832513 (+) 582 WP_011173284.1 type IV pilus modification PilV family protein Machinery gene
  TT_RS04325 (TT_C0856) pilA/pilA3 832510..833211 (+) 702 WP_011173285.1 PilW family protein Machinery gene
  TT_RS04330 (TT_C0857) comZ 833222..834886 (+) 1665 WP_011173286.1 pilus assembly PilX N-terminal domain-containing protein Machinery gene
  TT_RS11945 (TT_C0858) pilA/pilA4 835117..835512 (+) 396 WP_011173287.1 type IV wide pilus major component PilA4 Machinery gene
  TT_RS11645 - 835569..836861 (-) 1293 WP_143591263.1 O-antigen ligase family protein -

Sequence

Protein


Download         Length: 193 a.a.        Molecular weight: 20563.65 Da        Isoelectric Point: 9.1543

>NTDB_id=1031 TT_RS04320 WP_011173284.1 831932..832513(+) (pilA/pilA2) [Thermus thermophilus HB27]
MRKGLTLVEVLVTLVIMGIAFAALLTSQLANLRASAQARFATDAKAAAVQVLERRSAEVLKSEIVPALSPYKDAPLDPDN
PSGNWRSFYFVDYYFSCPTRVAPSPKQRGGSVANLRPGLTCSGTETIFGIPVAWDIRGENGILGEGVVTVVVTATHPRGP
KVTLGRRVTCYDVYPSPTQDQPAPCPPPGGGRP

Nucleotide


Download         Length: 582 bp        

>NTDB_id=1031 TT_RS04320 WP_011173284.1 831932..832513(+) (pilA/pilA2) [Thermus thermophilus HB27]
ATGAGAAAAGGGCTCACCCTCGTGGAAGTCCTCGTCACCTTGGTCATCATGGGTATCGCCTTTGCCGCCTTGTTGACGAG
CCAGCTTGCCAACCTCCGGGCGAGCGCCCAGGCCCGCTTCGCCACCGACGCCAAGGCCGCCGCCGTCCAGGTCCTGGAGC
GCCGCTCGGCCGAGGTGCTGAAAAGCGAAATCGTCCCGGCCTTAAGCCCCTACAAGGACGCCCCCTTGGACCCGGACAAC
CCTTCGGGAAACTGGCGGAGCTTTTACTTCGTGGACTACTACTTCTCCTGCCCCACCCGGGTGGCCCCTTCCCCTAAGCA
GAGGGGAGGGTCTGTAGCCAACCTTCGTCCCGGCCTCACCTGCTCGGGCACGGAGACGATCTTTGGCATCCCCGTGGCCT
GGGACATCCGCGGGGAAAACGGCATCCTGGGCGAGGGCGTGGTGACGGTGGTGGTCACGGCCACCCATCCCCGGGGGCCC
AAGGTCACCCTGGGCCGCCGGGTCACCTGCTACGACGTCTACCCTTCCCCCACCCAGGACCAGCCCGCCCCTTGCCCACC
TCCTGGAGGTGGTCGCCCATGA

Domains

Predicted by InterproScan.

Prokaryotic N-terminal methylation motif (N_methyl)

(2-25)


Secondary structure

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



3D structure

Source ID Structure
  AlphaFold DB Q72JC3

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] Lennart Kirchner et al. (2022) DNA binding by pilins and their interaction with the inner membrane platform of the DNA transporter in Thermus thermophilus. Biochimica Et Biophysica Acta. Biomembranes 1864(1):183818. [PMID: 34774498]
[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] 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]
[5] Alexandra Friedrich et al. (2003) Pilin-like proteins in the extremely thermophilic bacterium Thermus thermophilus HB27: implication in competence for natural transformation and links to type IV pilus biogenesis. Applied And Environmental Microbiology 69(7):3695-700. [PMID: 12839734]