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Conserved domains on  [gi|1090990655|gb|OHP28172|]
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transcriptional regulator, partial [Enterococcus sp. HMSC060D07]

Protein Classification

CopG family transcriptional regulator( domain architecture ID 15348592)

CopG family transcriptional regulator is a ribbon-helix-helix (RHH) protein similar to Mycobacterium VapB antitoxins and Streptococcus agalactiae protein CopG, which regulates plasmid copy number by binding to the RepAB promoter

Gene Ontology:  GO:0006276|GO:0006355|GO:0032993

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RHH_CopG_NikR-like cd21631
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ...
7-36 2.83e-04

ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins; This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.


:

Pssm-ID: 409020  Cd Length: 42  Bit Score: 33.64  E-value: 2.83e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 1090990655  7 KRVVVTLTKEVADNLDKIAKQMGLSKSGLI 36
Cdd:cd21631    1 KRVTIKLDDELLERLDELARKRGVSRSELI 30
 
Name Accession Description Interval E-value
RHH_CopG_NikR-like cd21631
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ...
7-36 2.83e-04

ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins; This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.


Pssm-ID: 409020  Cd Length: 42  Bit Score: 33.64  E-value: 2.83e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 1090990655  7 KRVVVTLTKEVADNLDKIAKQMGLSKSGLI 36
Cdd:cd21631    1 KRVTIKLDDELLERLDELARKRGVSRSELI 30
 
Name Accession Description Interval E-value
RHH_CopG_NikR-like cd21631
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ...
7-36 2.83e-04

ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins; This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.


Pssm-ID: 409020  Cd Length: 42  Bit Score: 33.64  E-value: 2.83e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 1090990655  7 KRVVVTLTKEVADNLDKIAKQMGLSKSGLI 36
Cdd:cd21631    1 KRVTIKLDDELLERLDELARKRGVSRSELI 30
RHH_CopG_Cop6-like cd22232
ribbon-helix-helix family transcriptional repressor protein CopG, uncharacterized Cop6, and ...
5-36 3.54e-03

ribbon-helix-helix family transcriptional repressor protein CopG, uncharacterized Cop6, and similar proteins; This family includes the ribbon-helix-helix (RHH) family transcriptional repressor CopG, which is involved in the control of plasmid copy number, as well as uncharacterized proteins such as Cop6, which is found in a small plasmid that has been identified in methicillin-resistant Staphylococcus aureus (MRSA). CopG, a homodimeric protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It binds to and represses the single Pcr promoter that directs the synthesis of a bicistronic mRNA for CopG and the RepB initiator of replication, thereby regulating its own synthesis and that of RepB.


Pssm-ID: 409022  Cd Length: 45  Bit Score: 30.80  E-value: 3.54e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 1090990655  5 EKKRVVVTLTKEVADNLDKIAKQMGLSKSGLI 36
Cdd:cd22232    1 MKKQLTIRLPEEENENLNKIKEKYGISKSDQI 32
 
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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