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Conserved domains on  [gi|1613518834|emb|VHB43893|]
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Lantibiotic macedocin [Streptococcus pyogenes]

Protein Classification

similar to lantibiotic nukacin( domain architecture ID 10519119)

protein similar to lantibiotic nukacin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
L_biotic_typeA pfam04604
Type-A lantibiotic; Lantibiotics are antibiotic peptides distinguished by the presence of the ...
1-50 4.79e-21

Type-A lantibiotic; Lantibiotics are antibiotic peptides distinguished by the presence of the rare thioether amino acids lanthionine and/or methyl-lanthionine. They are produced by Gram-positive bacteria as gene-encoded precursor peptides and undergo post-translational modification to generate the mature peptide. Based on their structural and functional features lantibiotics are currently divided into two major groups: the flexible amphiphilic type-A and the rather rigid and globular type-B. Type-A lantibiotics act primarily by pore formation in the bacterial membrane by a mechanism involving the interaction with specific docking molecules such as the membrane precursor lipid II.


:

Pssm-ID: 368018  Cd Length: 51  Bit Score: 76.28  E-value: 4.79e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1613518834  1 MEKNNEVINSIQEVSLEELDQIIGAGKNGVFKTISHECHLNTWAFLATCC 50
Cdd:pfam04604  2 KNSNDEALNSLQEVSEEELDQILGGKGSGVIKTISHECRMNSWQFVFTCC 51
 
Name Accession Description Interval E-value
L_biotic_typeA pfam04604
Type-A lantibiotic; Lantibiotics are antibiotic peptides distinguished by the presence of the ...
1-50 4.79e-21

Type-A lantibiotic; Lantibiotics are antibiotic peptides distinguished by the presence of the rare thioether amino acids lanthionine and/or methyl-lanthionine. They are produced by Gram-positive bacteria as gene-encoded precursor peptides and undergo post-translational modification to generate the mature peptide. Based on their structural and functional features lantibiotics are currently divided into two major groups: the flexible amphiphilic type-A and the rather rigid and globular type-B. Type-A lantibiotics act primarily by pore formation in the bacterial membrane by a mechanism involving the interaction with specific docking molecules such as the membrane precursor lipid II.


Pssm-ID: 368018  Cd Length: 51  Bit Score: 76.28  E-value: 4.79e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1613518834  1 MEKNNEVINSIQEVSLEELDQIIGAGKNGVFKTISHECHLNTWAFLATCC 50
Cdd:pfam04604  2 KNSNDEALNSLQEVSEEELDQILGGKGSGVIKTISHECRMNSWQFVFTCC 51
HEC_x9_TCC_lant NF040664
lacticin 481 family lantibiotic; The lacticin 481 group exert their antimicrobial action by ...
12-50 5.56e-20

lacticin 481 family lantibiotic; The lacticin 481 group exert their antimicrobial action by disrupting the cytoplasmic membrane. This model contains a lipid II-binding motif. The docking of the lantibiotic with lipid II is part of the mechanism by which family members form a membrane-disrupting structure. The lacticin 481 group includes lacticin 481, mutacin H-29B, variacin, nukacin ISK-1, butyrivibriocin OR79A, streptococcin A-FF2, ruminococcin A, mutacin II, and salivaricin A.


Pssm-ID: 468630  Cd Length: 39  Bit Score: 73.50  E-value: 5.56e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 1613518834 12 QEVSLEELDQIIGAGKNGVFKTISHECHLNTWAFLATCC 50
Cdd:NF040664   1 QEVSDEELDQILGAGGNGVIKTISHECHMNSWQFLFTCC 39
 
Name Accession Description Interval E-value
L_biotic_typeA pfam04604
Type-A lantibiotic; Lantibiotics are antibiotic peptides distinguished by the presence of the ...
1-50 4.79e-21

Type-A lantibiotic; Lantibiotics are antibiotic peptides distinguished by the presence of the rare thioether amino acids lanthionine and/or methyl-lanthionine. They are produced by Gram-positive bacteria as gene-encoded precursor peptides and undergo post-translational modification to generate the mature peptide. Based on their structural and functional features lantibiotics are currently divided into two major groups: the flexible amphiphilic type-A and the rather rigid and globular type-B. Type-A lantibiotics act primarily by pore formation in the bacterial membrane by a mechanism involving the interaction with specific docking molecules such as the membrane precursor lipid II.


Pssm-ID: 368018  Cd Length: 51  Bit Score: 76.28  E-value: 4.79e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1613518834  1 MEKNNEVINSIQEVSLEELDQIIGAGKNGVFKTISHECHLNTWAFLATCC 50
Cdd:pfam04604  2 KNSNDEALNSLQEVSEEELDQILGGKGSGVIKTISHECRMNSWQFVFTCC 51
HEC_x9_TCC_lant NF040664
lacticin 481 family lantibiotic; The lacticin 481 group exert their antimicrobial action by ...
12-50 5.56e-20

lacticin 481 family lantibiotic; The lacticin 481 group exert their antimicrobial action by disrupting the cytoplasmic membrane. This model contains a lipid II-binding motif. The docking of the lantibiotic with lipid II is part of the mechanism by which family members form a membrane-disrupting structure. The lacticin 481 group includes lacticin 481, mutacin H-29B, variacin, nukacin ISK-1, butyrivibriocin OR79A, streptococcin A-FF2, ruminococcin A, mutacin II, and salivaricin A.


Pssm-ID: 468630  Cd Length: 39  Bit Score: 73.50  E-value: 5.56e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 1613518834 12 QEVSLEELDQIIGAGKNGVFKTISHECHLNTWAFLATCC 50
Cdd:NF040664   1 QEVSDEELDQILGAGGNGVIKTISHECHMNSWQFLFTCC 39
 
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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