type II toxin-antitoxin (TA) system HipA family toxin similar to Escherichia coli HipA, a serine/threonine-protein kinase that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu), and is also the toxin component of the HipA-HipB TA module
HipA-like C-terminal domain; The members of this family are similar to a region close to the ...
198-354
1.06e-20
HipA-like C-terminal domain; The members of this family are similar to a region close to the C-terminus of the HipA protein expressed by various bacterial species (for example Swiss:P23874). This protein is known to be involved in high-frequency persistence to the lethal effects of inhibition of either DNA or peptidoglycan synthesis. When expressed alone, it is toxic to bacterial cells, but it is usually tightly associated with HipB, and the HipA-HipB complex may be involved in autoregulation of the hip operon. The hip proteins may be involved in cell division control and may interact with cell division genes or their products.
Pssm-ID: 462271 [Multi-domain] Cd Length: 224 Bit Score: 90.05 E-value: 1.06e-20
serine/threonine-protein kinases similar to HipA and CtkA; This family contains serine ...
200-350
9.14e-11
serine/threonine-protein kinases similar to HipA and CtkA; This family contains serine/threonine-protein kinases similar to Escherichia coli HipA, a type II toxin-antitoxin (TA) system HipA family toxin that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu), and is the toxin component of the HipA-HipB TA module, as well as similar to the Helicobacter pylori serine/threonine-protein kinase CtkA (proinflammatory kinase), which has been shown to be secreted by the bacteria and to induce cytokines in gastric epithelial cells relevant to chronic gastric inflammation.
Pssm-ID: 341490 [Multi-domain] Cd Length: 284 Bit Score: 62.30 E-value: 9.14e-11
HipA-like C-terminal domain; The members of this family are similar to a region close to the ...
198-354
1.06e-20
HipA-like C-terminal domain; The members of this family are similar to a region close to the C-terminus of the HipA protein expressed by various bacterial species (for example Swiss:P23874). This protein is known to be involved in high-frequency persistence to the lethal effects of inhibition of either DNA or peptidoglycan synthesis. When expressed alone, it is toxic to bacterial cells, but it is usually tightly associated with HipB, and the HipA-HipB complex may be involved in autoregulation of the hip operon. The hip proteins may be involved in cell division control and may interact with cell division genes or their products.
Pssm-ID: 462271 [Multi-domain] Cd Length: 224 Bit Score: 90.05 E-value: 1.06e-20
serine/threonine-protein kinases similar to HipA and CtkA; This family contains serine ...
200-350
9.14e-11
serine/threonine-protein kinases similar to HipA and CtkA; This family contains serine/threonine-protein kinases similar to Escherichia coli HipA, a type II toxin-antitoxin (TA) system HipA family toxin that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu), and is the toxin component of the HipA-HipB TA module, as well as similar to the Helicobacter pylori serine/threonine-protein kinase CtkA (proinflammatory kinase), which has been shown to be secreted by the bacteria and to induce cytokines in gastric epithelial cells relevant to chronic gastric inflammation.
Pssm-ID: 341490 [Multi-domain] Cd Length: 284 Bit Score: 62.30 E-value: 9.14e-11
type II toxin-antitoxin sytem toxin HipA and similar proteins; This family contains type II ...
306-427
3.67e-06
type II toxin-antitoxin sytem toxin HipA and similar proteins; This family contains type II toxin-antitoxin (TA) system HipA family toxins similar to Escherichia coli and Shewanella oneidensis HipA, which is a serine/threonine-protein kinase that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance. HipA is the toxin component of the HipA-HipB TA module that is a major factor in persistence and bioflim formation; its toxic effect is neutralized by its cognate antitoxin HipB. HipA, with HipB, acts as a a corepressor for transcription of the hipBA promoter. Structures of HipAB:DNA complexes from both Escherichia coli and Shewanella oneidensis reveal distinct complex assembly.
Pssm-ID: 341492 [Multi-domain] Cd Length: 358 Bit Score: 48.74 E-value: 3.67e-06
type II toxin-antitoxin sytem toxin HipA from Shewanella oneidensis and similar proteins; This ...
319-350
1.01e-04
type II toxin-antitoxin sytem toxin HipA from Shewanella oneidensis and similar proteins; This family contains type II toxin-antitoxin (TA) system HipA family toxins similar to Shewanella oneidensis HipA, a serine/threonine-protein kinase that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance. HipA is the toxin component of the HipA-HipB TA module that is a major factor in persistence and bioflim formation; its toxic effect is neutralized by its cognate antitoxin HipB. HipA, with HipB, acts as a a corepressor for transcription of the hipBA promoter. In the Shewanella oneidensis HipAB:DNA promoter complex, HipB forms a dimer that binds the duplex operator DNA, with each HipB monomer interacting with separate HipA monomers. The HipAB component of the complex is composed of two HipA and two HipB subunits.
Pssm-ID: 341494 [Multi-domain] Cd Length: 405 Bit Score: 44.25 E-value: 1.01e-04
type II toxin-antitoxin sytem toxin HipA from Escherichia coli and similar proteins; This ...
291-406
2.04e-03
type II toxin-antitoxin sytem toxin HipA from Escherichia coli and similar proteins; This family contains type II toxin-antitoxin (TA) system HipA family toxins similar to Escherichia coli HipA, a serine/threonine-protein kinase that phosphorylates Glu-tRNA-ligase (GltX), preventing it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance. HipA is the toxin component of the HipA-HipB TA module that is a major factor in persistence and bioflim formation; its toxic effect is neutralized by its cognate antitoxin HipB. HipA, with HipB, acts as a a corepressor for transcription of the hipBA promoter. In the Escherichia coli HipAB:DNA promoter complex, HipA forms a dimer and each HipA monomer interacts with a HipB homodimer which binds DNA. The HipAB component of the complex is composed of two HipA and four HipB subunits.
Pssm-ID: 341493 [Multi-domain] Cd Length: 401 Bit Score: 40.26 E-value: 2.04e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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