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Conserved domains on  [gi|1831503256|pdb|6TXT|A]
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Chain A, Competence pilin-like protein ComGC

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
T2SSG super family cl46149
Type II secretion system (T2SS), protein G; The Type II secretion system, also called ...
1-60 3.38e-25

Type II secretion system (T2SS), protein G; The Type II secretion system, also called Secretion-dependent pathway (SDP), is responsible for the transport of proteins across the outer membrane first exported to the periplasm by the Sec or Tat translocon in Gram-negative (diderm) bacteria. The T2SG family includes proteins such as EpsG (P45773) in Vibrio cholera, XcpT also called PddA (Q00514) in Pseudomonas aeruginosa or PulG (P15746)in Klebsiella pneumoniae. The PulG is thought to be anchored in the inner membrane with its C-terminus directed towards the periplasme. Together with other members of the Type II secretion machinery, it is thought to assemble into a pilus-like structure that may function as a dynamic mechanism to push secreted proteins out of the cell. The polypeptide is organized into a long N-terminal alpha-helix followed by a loop region that separates it from a C-terminal anti-parallel beta-sheet.


The actual alignment was detected with superfamily member NF040999:

Pssm-ID: 480489  Cd Length: 84  Bit Score: 88.72  E-value: 3.38e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
6TXT_A        1 NLTKQKDAVSDTGTAAVVKVVESQAELYELKNtNEKASLSKLVSSGNISQKQADSYKAYY 60
Cdd:NF040999 26 NLSKQKESVQEKGCEAVVKVVESQVELYELDH-NKKPSLSELVSEGYITKKQCPNYKDYY 84
 
Name Accession Description Interval E-value
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
1-60 3.38e-25

competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major pilin of a type IV pilus involved in natural transformation of monoderm bacteria (those lacking an outer membrane) such as Bacillus subtilis and Streptococcus pneumoniae. In the seed alignment, Bacillus proteins have a pair of Cys residues likely to form a disulfide bond while Streptococcus proteins lack Cys residues.


Pssm-ID: 468929  Cd Length: 84  Bit Score: 88.72  E-value: 3.38e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
6TXT_A        1 NLTKQKDAVSDTGTAAVVKVVESQAELYELKNtNEKASLSKLVSSGNISQKQADSYKAYY 60
Cdd:NF040999 26 NLSKQKESVQEKGCEAVVKVVESQVELYELDH-NKKPSLSELVSEGYITKKQCPNYKDYY 84
 
Name Accession Description Interval E-value
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
1-60 3.38e-25

competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major pilin of a type IV pilus involved in natural transformation of monoderm bacteria (those lacking an outer membrane) such as Bacillus subtilis and Streptococcus pneumoniae. In the seed alignment, Bacillus proteins have a pair of Cys residues likely to form a disulfide bond while Streptococcus proteins lack Cys residues.


Pssm-ID: 468929  Cd Length: 84  Bit Score: 88.72  E-value: 3.38e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
6TXT_A        1 NLTKQKDAVSDTGTAAVVKVVESQAELYELKNtNEKASLSKLVSSGNISQKQADSYKAYY 60
Cdd:NF040999 26 NLSKQKESVQEKGCEAVVKVVESQVELYELDH-NKKPSLSELVSEGYITKKQCPNYKDYY 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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