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Conserved domains on  [gi|489307467|ref|WP_003214902|]
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MULTISPECIES: uberolysin/carnocyclin family circular bacteriocin [Bacillus]

Protein Classification

uberolysin/carnocyclin family circular bacteriocin( domain architecture ID 10022736)

uberolysin/carnocyclin family circular bacteriocin similar to Streptococcus uberis bacteriocin uberolysin, a cyclopeptide antibiotic with bacteriolytic activity against most streptococci

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
circ_ocin_uber TIGR03651
circular bacteriocin, circularin A/uberolysin family; Circular bacteriocins are antibiotic ...
31-84 4.58e-06

circular bacteriocin, circularin A/uberolysin family; Circular bacteriocins are antibiotic proteins made by ribosomal translation of a precursor molecular, followed by cleavage and circularization. Members of this subclass of the circular bacteriocins include circularin A from Clostridium beijerinckii, bacteriocin AS-48 from Enterococcus faecalis, uberolysin from Streptococcus uberis, and carnocyclin A from Carnobacterium maltaromaticum. The mature circularized peptides average about 70 amino acids in size. [Cellular processes, Toxin production and resistance]


:

Pssm-ID: 274700  Cd Length: 73  Bit Score: 40.55  E-value: 4.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489307467  31 SLIAANLGVSTATAATVVNFLDTWSSVATVITIVGVFTGVGTISSGVAAAILAI 84
Cdd:TIGR03651  1 AEVAGTLGISTATATTVVNIIDTGSTIVTIISIIAAIVGSGGLSVLLAAGIDAI 54
 
Name Accession Description Interval E-value
circ_ocin_uber TIGR03651
circular bacteriocin, circularin A/uberolysin family; Circular bacteriocins are antibiotic ...
31-84 4.58e-06

circular bacteriocin, circularin A/uberolysin family; Circular bacteriocins are antibiotic proteins made by ribosomal translation of a precursor molecular, followed by cleavage and circularization. Members of this subclass of the circular bacteriocins include circularin A from Clostridium beijerinckii, bacteriocin AS-48 from Enterococcus faecalis, uberolysin from Streptococcus uberis, and carnocyclin A from Carnobacterium maltaromaticum. The mature circularized peptides average about 70 amino acids in size. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274700  Cd Length: 73  Bit Score: 40.55  E-value: 4.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489307467  31 SLIAANLGVSTATAATVVNFLDTWSSVATVITIVGVFTGVGTISSGVAAAILAI 84
Cdd:TIGR03651  1 AEVAGTLGISTATATTVVNIIDTGSTIVTIISIIAAIVGSGGLSVLLAAGIDAI 54
Bacteriocin_IId pfam09221
Bacteriocin class IId cyclical uberolysin-like; Members of this family are ...
34-83 3.47e-05

Bacteriocin class IId cyclical uberolysin-like; Members of this family are membrane-interacting peptides, produced by Firmicutes that display a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. They adopt a helical structure, with four or five alpha helices forming a Saposin-like fold. The structure has been found to be cyclical. It should be pointed out that one reference implies that both circularin A and gassericin A are class V or IIc-type bacteriocins; however we find that these two proteins fall into different Pfam families families, this one and BacteriocIIc_cy, pfam12173.


Pssm-ID: 401240  Cd Length: 67  Bit Score: 38.22  E-value: 3.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489307467  34 AANLGVSTATAATVVNFLDTWSSVATVITIVGVFTGVGTISSGVAAAILA 83
Cdd:pfam09221  1 AGTLGISKGTATKVVDIVDTGSTAATIISIIGAILSAGAISAIGASAIVA 50
 
Name Accession Description Interval E-value
circ_ocin_uber TIGR03651
circular bacteriocin, circularin A/uberolysin family; Circular bacteriocins are antibiotic ...
31-84 4.58e-06

circular bacteriocin, circularin A/uberolysin family; Circular bacteriocins are antibiotic proteins made by ribosomal translation of a precursor molecular, followed by cleavage and circularization. Members of this subclass of the circular bacteriocins include circularin A from Clostridium beijerinckii, bacteriocin AS-48 from Enterococcus faecalis, uberolysin from Streptococcus uberis, and carnocyclin A from Carnobacterium maltaromaticum. The mature circularized peptides average about 70 amino acids in size. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274700  Cd Length: 73  Bit Score: 40.55  E-value: 4.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489307467  31 SLIAANLGVSTATAATVVNFLDTWSSVATVITIVGVFTGVGTISSGVAAAILAI 84
Cdd:TIGR03651  1 AEVAGTLGISTATATTVVNIIDTGSTIVTIISIIAAIVGSGGLSVLLAAGIDAI 54
Bacteriocin_IId pfam09221
Bacteriocin class IId cyclical uberolysin-like; Members of this family are ...
34-83 3.47e-05

Bacteriocin class IId cyclical uberolysin-like; Members of this family are membrane-interacting peptides, produced by Firmicutes that display a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. They adopt a helical structure, with four or five alpha helices forming a Saposin-like fold. The structure has been found to be cyclical. It should be pointed out that one reference implies that both circularin A and gassericin A are class V or IIc-type bacteriocins; however we find that these two proteins fall into different Pfam families families, this one and BacteriocIIc_cy, pfam12173.


Pssm-ID: 401240  Cd Length: 67  Bit Score: 38.22  E-value: 3.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489307467  34 AANLGVSTATAATVVNFLDTWSSVATVITIVGVFTGVGTISSGVAAAILA 83
Cdd:pfam09221  1 AGTLGISKGTATKVVDIVDTGSTAATIISIIGAILSAGAISAIGASAIVA 50
 
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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