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Conserved domains on  [gi|446314584|ref|WP_000392439|]
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MULTISPECIES: BhlA/UviB family holin-like peptide [Bacillus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Holin_BhlA super family cl12535
BhlA holin family; The Phage_holin_BhlA family is a family of holin-like proteins from both ...
1-66 3.51e-06

BhlA holin family; The Phage_holin_BhlA family is a family of holin-like proteins from both bacteriophages and bacterial chromosomes. In bacteriophage, holins are small membrane proteins that accumulate and oligomerise to form non-specific lesions in the cytoplasmic membrane allowing the release of the second protein, endolysins, to access the peptidoglycan. Most holins share common structural features: two or three transmembrane domains separated by a beta-turn, a short hydrophilic N-terminus, a highly charged C-terminus and a dual translational start motif. The BhlA holin of Bacillus is found to be toxic to the host cell where the site of action of is on the cell membrane and causes bacterial death by cell membrane disruption.


The actual alignment was detected with superfamily member pfam10960:

Pssm-ID: 431557  Cd Length: 66  Bit Score: 40.07  E-value: 3.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446314584   1 MEEQIFNSMIQQGAFAALFVWMLFTTQKKNEQREEQYQKVIEKNQAVIEEQAKAFGSLAKDVSDIK 66
Cdd:pfam10960  1 MENEIIKLASTQGIWAVLFVVLLFYILKTQEKRDLKQDEREKNYQEIISKLTEKLNVVEDVKKDVE 66
 
Name Accession Description Interval E-value
Holin_BhlA pfam10960
BhlA holin family; The Phage_holin_BhlA family is a family of holin-like proteins from both ...
1-66 3.51e-06

BhlA holin family; The Phage_holin_BhlA family is a family of holin-like proteins from both bacteriophages and bacterial chromosomes. In bacteriophage, holins are small membrane proteins that accumulate and oligomerise to form non-specific lesions in the cytoplasmic membrane allowing the release of the second protein, endolysins, to access the peptidoglycan. Most holins share common structural features: two or three transmembrane domains separated by a beta-turn, a short hydrophilic N-terminus, a highly charged C-terminus and a dual translational start motif. The BhlA holin of Bacillus is found to be toxic to the host cell where the site of action of is on the cell membrane and causes bacterial death by cell membrane disruption.


Pssm-ID: 431557  Cd Length: 66  Bit Score: 40.07  E-value: 3.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446314584   1 MEEQIFNSMIQQGAFAALFVWMLFTTQKKNEQREEQYQKVIEKNQAVIEEQAKAFGSLAKDVSDIK 66
Cdd:pfam10960  1 MENEIIKLASTQGIWAVLFVVLLFYILKTQEKRDLKQDEREKNYQEIISKLTEKLNVVEDVKKDVE 66
 
Name Accession Description Interval E-value
Holin_BhlA pfam10960
BhlA holin family; The Phage_holin_BhlA family is a family of holin-like proteins from both ...
1-66 3.51e-06

BhlA holin family; The Phage_holin_BhlA family is a family of holin-like proteins from both bacteriophages and bacterial chromosomes. In bacteriophage, holins are small membrane proteins that accumulate and oligomerise to form non-specific lesions in the cytoplasmic membrane allowing the release of the second protein, endolysins, to access the peptidoglycan. Most holins share common structural features: two or three transmembrane domains separated by a beta-turn, a short hydrophilic N-terminus, a highly charged C-terminus and a dual translational start motif. The BhlA holin of Bacillus is found to be toxic to the host cell where the site of action of is on the cell membrane and causes bacterial death by cell membrane disruption.


Pssm-ID: 431557  Cd Length: 66  Bit Score: 40.07  E-value: 3.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446314584   1 MEEQIFNSMIQQGAFAALFVWMLFTTQKKNEQREEQYQKVIEKNQAVIEEQAKAFGSLAKDVSDIK 66
Cdd:pfam10960  1 MENEIIKLASTQGIWAVLFVVLLFYILKTQEKRDLKQDEREKNYQEIISKLTEKLNVVEDVKKDVE 66
 
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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