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Conserved domains on  [gi|516456544|ref|WP_017845384|]
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MULTISPECIES: Hpt domain-containing protein [Pseudomonas]

Protein Classification

Hpt domain-containing protein( domain architecture ID 10483122)

Hpt (histidine-containing phosphotransfer) domain-containing protein which may be involved in phosphotransfer signal transduction

CATH:  1.20.120.160
Gene Ontology:  GO:0000160|GO:0009927
PubMed:  9054511|11406410
SCOP:  4000835

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 24-102 1.36e-10

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


:

Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 53.12  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456544   24 KLLDTFLDDSQKRVEALRKA--RDDAKALALIAHSFKGSSGNLGAVRLAHLCQRLE-VESVEAAADLGALVDQIDHEFAL 100
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAldAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEdLLREGELPLDPELLEALRDLLEA 80


                  ..
gi 516456544  101 VK 102
Cdd:pfam01627  81 LR 82
 
Name Accession Description Interval E-value
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 24-102 1.36e-10

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 53.12  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456544   24 KLLDTFLDDSQKRVEALRKA--RDDAKALALIAHSFKGSSGNLGAVRLAHLCQRLE-VESVEAAADLGALVDQIDHEFAL 100
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAldAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEdLLREGELPLDPELLEALRDLLEA 80


                  ..
gi 516456544  101 VK 102
Cdd:pfam01627  81 LR 82
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 25-77 4.82e-08

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 46.99  E-value: 4.82e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516456544  25 LLDTFLDDSQKRVEALRKA------RDDAKALALIAHSFKGSSGNLGAVRLAHLCQRLE 77
Cdd:cd00088    4 LLELFLEEAEELLEELERAlleledAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLE 62
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 25-77 1.55e-07

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 45.32  E-value: 1.55e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 516456544    25 LLDTFLDDSQKRVEALRKARD--DAKALALIAHSFKGSSGNLGAVRLAHLCQRLE 77
Cdd:smart00073   9 ELAEFLQSLEEGLLELEKALDaqDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLE 63
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
21-77 1.17e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 42.48  E-value: 1.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516456544  21 EYPKLLDTFLDDSQKRVE-------ALRKARDDAKALALI---AHSFKGSSGNLGAVRLAHLCQRLE 77
Cdd:COG0643    2 DMDELLEIFLEEARELLEqleegllALEQDPDDPELLNAIfraAHTLKGSAGMLGLDALAELAHALE 68
 
Name Accession Description Interval E-value
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 24-102 1.36e-10

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 53.12  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456544   24 KLLDTFLDDSQKRVEALRKA--RDDAKALALIAHSFKGSSGNLGAVRLAHLCQRLE-VESVEAAADLGALVDQIDHEFAL 100
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAldAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEdLLREGELPLDPELLEALRDLLEA 80


                  ..
gi 516456544  101 VK 102
Cdd:pfam01627  81 LR 82
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 25-77 4.82e-08

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 46.99  E-value: 4.82e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516456544  25 LLDTFLDDSQKRVEALRKA------RDDAKALALIAHSFKGSSGNLGAVRLAHLCQRLE 77
Cdd:cd00088    4 LLELFLEEAEELLEELERAlleledAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLE 62
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 25-77 1.55e-07

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 45.32  E-value: 1.55e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 516456544    25 LLDTFLDDSQKRVEALRKARD--DAKALALIAHSFKGSSGNLGAVRLAHLCQRLE 77
Cdd:smart00073   9 ELAEFLQSLEEGLLELEKALDaqDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLE 63
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
21-77 1.17e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 42.48  E-value: 1.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516456544  21 EYPKLLDTFLDDSQKRVE-------ALRKARDDAKALALI---AHSFKGSSGNLGAVRLAHLCQRLE 77
Cdd:COG0643    2 DMDELLEIFLEEARELLEqleegllALEQDPDDPELLNAIfraAHTLKGSAGMLGLDALAELAHALE 68
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
19-111 3.51e-05

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 41.57  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456544  19 EGEYPKLLDTFLDDSQKRVEALRKA--RDDAKALALIAHSFKGSSGNLGAVRLAHLCQRLEVESVEA-AADLGALVDQID 95
Cdd:COG2198  775 PELLRELLELFLEELPELLAELRQAlaAGDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARAGdLEEAEELLAELE 854

                         90
                 ....*....|....*.
gi 516456544  96 HEFALVKPLYESERQR 111
Cdd:COG2198  855 AELERVLAALEALLAE 870
 
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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