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Conserved domains on  [gi|497610093|ref|WP_009924277|]
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bacteriocin immunity protein [Listeria monocytogenes]

Protein Classification

bacteriocin immunity protein( domain architecture ID 10556519)

bacteriocin immunity protein, similar to Lactococcus lactis lactococcin-A immunity protein, imparts immunity to specific bacteriocins to naturally sensitive host strains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EntA_Immun pfam08951
Enterocin A Immunity; Gram-positive lactobacilli produce bacteriocins to kill closely-related ...
14-85 5.41e-08

Enterocin A Immunity; Gram-positive lactobacilli produce bacteriocins to kill closely-related competitor species. To protect themselves from the bacteriocidal activity of this molecule they co-express an immunity protein (for discussion of this operon see Bacteriocin_IIc pfam10439). The immunity protein structure is a soluble, cytoplasmic, antiparallel four alpha-helical globular bundle with a fifth, more flexible and more divergent C-terminal helical hair-pin. The C-terminal hair-pin recognizes the C-terminus of the producer bacteriocin and this interaction is sufficient to dis-orient the bacteriocin within the membrane and close up the permeabilising pore that on its own the bacteriocin creates. These immunity proteins interact in the same way with other bacteriocins, family Bacteriocin_II, pfam01721. Since many enterococci can produce more than one bacteriocin it seems likely that the whole operon can be carried on transferable plasmids.


:

Pssm-ID: 430340  Cd Length: 68  Bit Score: 46.13  E-value: 5.41e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497610093   14 EELKNLFETDTSLNNqnsSQLQEILTTAIIRVKKASQtVELEARSVYQNIHTLCFVEKIHLNPEEANVLKEI 85
Cdd:pfam08951   1 NELYNLILNPEVKEN---EDLREVLLTAKNKLEKGKN-VEVVASRLEQALRPLALKNRIKLSPEVEDLYKEL 68
 
Name Accession Description Interval E-value
EntA_Immun pfam08951
Enterocin A Immunity; Gram-positive lactobacilli produce bacteriocins to kill closely-related ...
14-85 5.41e-08

Enterocin A Immunity; Gram-positive lactobacilli produce bacteriocins to kill closely-related competitor species. To protect themselves from the bacteriocidal activity of this molecule they co-express an immunity protein (for discussion of this operon see Bacteriocin_IIc pfam10439). The immunity protein structure is a soluble, cytoplasmic, antiparallel four alpha-helical globular bundle with a fifth, more flexible and more divergent C-terminal helical hair-pin. The C-terminal hair-pin recognizes the C-terminus of the producer bacteriocin and this interaction is sufficient to dis-orient the bacteriocin within the membrane and close up the permeabilising pore that on its own the bacteriocin creates. These immunity proteins interact in the same way with other bacteriocins, family Bacteriocin_II, pfam01721. Since many enterococci can produce more than one bacteriocin it seems likely that the whole operon can be carried on transferable plasmids.


Pssm-ID: 430340  Cd Length: 68  Bit Score: 46.13  E-value: 5.41e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497610093   14 EELKNLFETDTSLNNqnsSQLQEILTTAIIRVKKASQtVELEARSVYQNIHTLCFVEKIHLNPEEANVLKEI 85
Cdd:pfam08951   1 NELYNLILNPEVKEN---EDLREVLLTAKNKLEKGKN-VEVVASRLEQALRPLALKNRIKLSPEVEDLYKEL 68
 
Name Accession Description Interval E-value
EntA_Immun pfam08951
Enterocin A Immunity; Gram-positive lactobacilli produce bacteriocins to kill closely-related ...
14-85 5.41e-08

Enterocin A Immunity; Gram-positive lactobacilli produce bacteriocins to kill closely-related competitor species. To protect themselves from the bacteriocidal activity of this molecule they co-express an immunity protein (for discussion of this operon see Bacteriocin_IIc pfam10439). The immunity protein structure is a soluble, cytoplasmic, antiparallel four alpha-helical globular bundle with a fifth, more flexible and more divergent C-terminal helical hair-pin. The C-terminal hair-pin recognizes the C-terminus of the producer bacteriocin and this interaction is sufficient to dis-orient the bacteriocin within the membrane and close up the permeabilising pore that on its own the bacteriocin creates. These immunity proteins interact in the same way with other bacteriocins, family Bacteriocin_II, pfam01721. Since many enterococci can produce more than one bacteriocin it seems likely that the whole operon can be carried on transferable plasmids.


Pssm-ID: 430340  Cd Length: 68  Bit Score: 46.13  E-value: 5.41e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497610093   14 EELKNLFETDTSLNNqnsSQLQEILTTAIIRVKKASQtVELEARSVYQNIHTLCFVEKIHLNPEEANVLKEI 85
Cdd:pfam08951   1 NELYNLILNPEVKEN---EDLREVLLTAKNKLEKGKN-VEVVASRLEQALRPLALKNRIKLSPEVEDLYKEL 68
 
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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