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Conserved domains on  [gi|556388852|ref|WP_023303149|]
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MULTISPECIES: TA system toxin CbtA family protein [Enterobacterales]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CbtA_toxin super family cl06013
CbtA_toxin of type IV toxin-antitoxin system; CbtA is a family of bacterial and archaeal ...
 1-105 2.95e-69

CbtA_toxin of type IV toxin-antitoxin system; CbtA is a family of bacterial and archaeal toxins of type IV toxin-antitoxin system. Toxins from such systems in free-living bacteria inhibit cell growth by targeting essential functions of cellular metabolism. In this case the toxin inhibits cell-division leading to changes in morphology and finally lysis, by interacting with two essential cytoskeletal proteins, FtsZ and MreB. For FtsZ it inhibits its GTPase activity and GTP-dependent polymerization, and for MreB it inhibits its ATP-dependent polymerization. These actions of CbtA appear to occur simultaneously. he cognate antitoxin family is represented by pfam06154.


The actual alignment was detected with superfamily member pfam06755:

Pssm-ID: 369065  Cd Length: 108  Bit Score: 203.25  E-value: 2.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556388852    1 MKNLPATISRAAKPCLSPVAVWQMLLTRLLEQHYGLTLNDTPFSDETVIKEHIDAGIILADAVNFLVDKYELVRIDRRGF 80
Cdd:pfam06755   1 MNTLPATHVRAAKPCLSPVAVWQMLLTRLLEQHYGLTLNDTPFADERVIKEHIDAGITLADAVNFLVEKYELVRIDQPGF 80

                          90       100
                  ....*....|....*....|....*
gi 556388852   81 SSQGQVPYLTVTDILHARRACGLMK 105
Cdd:pfam06755  81 SWQTQSPYINSIDILRARRVTGLLT 105
 
Name Accession Description Interval E-value
CbtA_toxin pfam06755
CbtA_toxin of type IV toxin-antitoxin system; CbtA is a family of bacterial and archaeal ...
 1-105 2.95e-69

CbtA_toxin of type IV toxin-antitoxin system; CbtA is a family of bacterial and archaeal toxins of type IV toxin-antitoxin system. Toxins from such systems in free-living bacteria inhibit cell growth by targeting essential functions of cellular metabolism. In this case the toxin inhibits cell-division leading to changes in morphology and finally lysis, by interacting with two essential cytoskeletal proteins, FtsZ and MreB. For FtsZ it inhibits its GTPase activity and GTP-dependent polymerization, and for MreB it inhibits its ATP-dependent polymerization. These actions of CbtA appear to occur simultaneously. he cognate antitoxin family is represented by pfam06154.


Pssm-ID: 369065  Cd Length: 108  Bit Score: 203.25  E-value: 2.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556388852    1 MKNLPATISRAAKPCLSPVAVWQMLLTRLLEQHYGLTLNDTPFSDETVIKEHIDAGIILADAVNFLVDKYELVRIDRRGF 80
Cdd:pfam06755   1 MNTLPATHVRAAKPCLSPVAVWQMLLTRLLEQHYGLTLNDTPFADERVIKEHIDAGITLADAVNFLVEKYELVRIDQPGF 80

                          90       100
                  ....*....|....*....|....*
gi 556388852   81 SSQGQVPYLTVTDILHARRACGLMK 105
Cdd:pfam06755  81 SWQTQSPYINSIDILRARRVTGLLT 105
 
Name Accession Description Interval E-value
CbtA_toxin pfam06755
CbtA_toxin of type IV toxin-antitoxin system; CbtA is a family of bacterial and archaeal ...
 1-105 2.95e-69

CbtA_toxin of type IV toxin-antitoxin system; CbtA is a family of bacterial and archaeal toxins of type IV toxin-antitoxin system. Toxins from such systems in free-living bacteria inhibit cell growth by targeting essential functions of cellular metabolism. In this case the toxin inhibits cell-division leading to changes in morphology and finally lysis, by interacting with two essential cytoskeletal proteins, FtsZ and MreB. For FtsZ it inhibits its GTPase activity and GTP-dependent polymerization, and for MreB it inhibits its ATP-dependent polymerization. These actions of CbtA appear to occur simultaneously. he cognate antitoxin family is represented by pfam06154.


Pssm-ID: 369065  Cd Length: 108  Bit Score: 203.25  E-value: 2.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556388852    1 MKNLPATISRAAKPCLSPVAVWQMLLTRLLEQHYGLTLNDTPFSDETVIKEHIDAGIILADAVNFLVDKYELVRIDRRGF 80
Cdd:pfam06755   1 MNTLPATHVRAAKPCLSPVAVWQMLLTRLLEQHYGLTLNDTPFADERVIKEHIDAGITLADAVNFLVEKYELVRIDQPGF 80

                          90       100
                  ....*....|....*....|....*
gi 556388852   81 SSQGQVPYLTVTDILHARRACGLMK 105
Cdd:pfam06755  81 SWQTQSPYINSIDILRARRVTGLLT 105
 
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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