flagellar motor switch phosphatase FliY [Bacillus wiedmannii]
Protein Classification
flagellar motor switch protein( domain architecture ID 11482415)
flagellar motor switch protein similar to FliN, one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| PRK06782 | PRK06782 | flagellar motor switch protein; Reviewed |
1-547 | 0e+00 | ||||||||
flagellar motor switch protein; Reviewed : Pssm-ID: 235861 [Multi-domain] Cd Length: 528 Bit Score: 757.06 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||
| PRK06782 | PRK06782 | flagellar motor switch protein; Reviewed |
1-547 | 0e+00 | ||||||||
flagellar motor switch protein; Reviewed Pssm-ID: 235861 [Multi-domain] Cd Length: 528 Bit Score: 757.06 E-value: 0e+00
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| FliY_FliN-Y | cd17907 | flagellar motor switch protein FliY; This family contains the flagellar rotor protein FliY, a ... |
22-213 | 1.81e-78 | ||||||||
flagellar motor switch protein FliY; This family contains the flagellar rotor protein FliY, a highly conserved and essential member of the CheC phosphatase family, that distinguishes flagellar architecture and function in different types of bacteria. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM, all present in many copies, and together corresponding structurally to the C-ring of the flagellar basal body. FliY structure resembles that of the rotor protein FliM but contains two active centers for CheY dephosphorylation. In bacteria such as Thermotogae and Bacilli, FliY is fused to FliN. It incorporates properties of the FliM/FliN rotor proteins and the CheC/CheX phosphatases to serve multiple functions in the flagellar switch. FliY seems to act on CheY-P constitutively, as compared to CheC and CheX that appear to be primarily involved in restoring normal CheY-P levels. Pssm-ID: 381735 [Multi-domain] Cd Length: 191 Bit Score: 244.70 E-value: 1.81e-78
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| CheC | COG1776 | Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]; |
22-214 | 4.25e-43 | ||||||||
Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]; Pssm-ID: 441382 [Multi-domain] Cd Length: 199 Bit Score: 152.29 E-value: 4.25e-43
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| FliMN_C | pfam01052 | Type III flagellar switch regulator (C-ring) FliN C-term; This family includes the C-terminal ... |
483-545 | 5.61e-13 | ||||||||
Type III flagellar switch regulator (C-ring) FliN C-term; This family includes the C-terminal region of flagellar motor switch proteins FliN and FliM. It is associated with family FliM, pfam02154 and family FliN_N pfam16973. Pssm-ID: 460043 [Multi-domain] Cd Length: 66 Bit Score: 63.90 E-value: 5.61e-13
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| fliN | TIGR02480 | flagellar motor switch protein FliN; Proteins that consist largely of the domain described by ... |
474-544 | 4.02e-11 | ||||||||
flagellar motor switch protein FliN; Proteins that consist largely of the domain described by this model for this protein family can be designated flagellar motor switch protein FliN. Longer proteins in which this region is a C-terminal domain typically are designated FliY. More distantly related sequences, outside the scope of this family, are associated with type III secretion and include the surface presentation of antigens protein SpaO required or invasion of host cells by Salmonella enterica. [Cellular processes, Chemotaxis and motility] Pssm-ID: 131533 [Multi-domain] Cd Length: 77 Bit Score: 58.76 E-value: 4.02e-11
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| CheX_Thtogales | NF041094 | CheY-P phosphatase CheX; |
252-377 | 1.56e-06 | ||||||||
CheY-P phosphatase CheX; Pssm-ID: 469020 [Multi-domain] Cd Length: 152 Bit Score: 48.07 E-value: 1.56e-06
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| CheX_Thtogales | NF041094 | CheY-P phosphatase CheX; |
32-165 | 1.96e-04 | ||||||||
CheY-P phosphatase CheX; Pssm-ID: 469020 [Multi-domain] Cd Length: 152 Bit Score: 41.91 E-value: 1.96e-04
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| Name | Accession | Description | Interval | E-value | ||||||||
| PRK06782 | PRK06782 | flagellar motor switch protein; Reviewed |
1-547 | 0e+00 | ||||||||
flagellar motor switch protein; Reviewed Pssm-ID: 235861 [Multi-domain] Cd Length: 528 Bit Score: 757.06 E-value: 0e+00
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| FliY_FliN-Y | cd17907 | flagellar motor switch protein FliY; This family contains the flagellar rotor protein FliY, a ... |
22-213 | 1.81e-78 | ||||||||
flagellar motor switch protein FliY; This family contains the flagellar rotor protein FliY, a highly conserved and essential member of the CheC phosphatase family, that distinguishes flagellar architecture and function in different types of bacteria. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM, all present in many copies, and together corresponding structurally to the C-ring of the flagellar basal body. FliY structure resembles that of the rotor protein FliM but contains two active centers for CheY dephosphorylation. In bacteria such as Thermotogae and Bacilli, FliY is fused to FliN. It incorporates properties of the FliM/FliN rotor proteins and the CheC/CheX phosphatases to serve multiple functions in the flagellar switch. FliY seems to act on CheY-P constitutively, as compared to CheC and CheX that appear to be primarily involved in restoring normal CheY-P levels. Pssm-ID: 381735 [Multi-domain] Cd Length: 191 Bit Score: 244.70 E-value: 1.81e-78
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| PRK08119 | PRK08119 | flagellar motor switch protein; Validated |
238-544 | 2.55e-78 | ||||||||
flagellar motor switch protein; Validated Pssm-ID: 236154 [Multi-domain] Cd Length: 382 Bit Score: 251.32 E-value: 2.55e-78
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| FliY_FliN-Y | cd17907 | flagellar motor switch protein FliY; This family contains the flagellar rotor protein FliY, a ... |
242-432 | 4.14e-75 | ||||||||
flagellar motor switch protein FliY; This family contains the flagellar rotor protein FliY, a highly conserved and essential member of the CheC phosphatase family, that distinguishes flagellar architecture and function in different types of bacteria. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM, all present in many copies, and together corresponding structurally to the C-ring of the flagellar basal body. FliY structure resembles that of the rotor protein FliM but contains two active centers for CheY dephosphorylation. In bacteria such as Thermotogae and Bacilli, FliY is fused to FliN. It incorporates properties of the FliM/FliN rotor proteins and the CheC/CheX phosphatases to serve multiple functions in the flagellar switch. FliY seems to act on CheY-P constitutively, as compared to CheC and CheX that appear to be primarily involved in restoring normal CheY-P levels. Pssm-ID: 381735 [Multi-domain] Cd Length: 191 Bit Score: 236.23 E-value: 4.14e-75
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| PRK08119 | PRK08119 | flagellar motor switch protein; Validated |
17-241 | 1.57e-73 | ||||||||
flagellar motor switch protein; Validated Pssm-ID: 236154 [Multi-domain] Cd Length: 382 Bit Score: 238.61 E-value: 1.57e-73
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| CheC | COG1776 | Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]; |
22-214 | 4.25e-43 | ||||||||
Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]; Pssm-ID: 441382 [Multi-domain] Cd Length: 199 Bit Score: 152.29 E-value: 4.25e-43
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| CheC | COG1776 | Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]; |
242-435 | 2.02e-42 | ||||||||
Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]; Pssm-ID: 441382 [Multi-domain] Cd Length: 199 Bit Score: 150.37 E-value: 2.02e-42
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| CheC_ClassI | cd17909 | chemotaxis protein CheC, Class I; This subfamily contains Class I CheC proteins with ... |
246-377 | 1.08e-17 | ||||||||
chemotaxis protein CheC, Class I; This subfamily contains Class I CheC proteins with phosphatase activity. The Class I cheC genes are generally found in firmicute and archaeal chemotaxis operons with cheD, usually translationally coupled. Class I CheCs interact with the CheD protein which is responsible for deamidation of certain glutamine residues to glutamates on the chemotaxis receptor proteins. This family contains two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site. The C-terminal helix of CheC acts as a mimic of the natural enzymatic target of CheD, the alpha-helical receptors, and serves as the binding site for CheD. The CheC/CheD heterodimerization increases CheY-P phosphatase activity five-fold. Class I CheCs are involved in adaptation of the chemotaxis system. Pssm-ID: 381737 [Multi-domain] Cd Length: 189 Bit Score: 81.32 E-value: 1.08e-17
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| CheC_CheX_FliY | cd16353 | CheC/CheX/FliY (CXY) family phosphatases; The CXY family includes CheY-P-hydrolyzing proteins ... |
251-377 | 1.75e-17 | ||||||||
CheC/CheX/FliY (CXY) family phosphatases; The CXY family includes CheY-P-hydrolyzing proteins that function in bacterial chemotaxis, which involves cellular processes that control the movement of organisms toward favorable environments via rotating flagella, which in turn determines the sense of rotation by the intracellular response regulator CheY. When phosphorylated, CheY-P interacts directly with the flagellar motor, and this signal is terminated by the CXY family of phosphatases (Escherichia coli uses CheZ). CheC acts as a weak CheY-P phosphatase but increases activity in the presence of CheD. Bacillus subtilis has only CheC and FliY while many systems also have CheX. CheC and CheX appear to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM. CheC, CheX, and FliY phosphatases share a consensus sequence ([DS]xxxExxNx(22)P) with four conserved residues thought to form the phosphatase active site. CheC class I and FliY each have two active sites, while CheC class II and III, and CheX have only one. This family also includes FliM, a component of the flagellar switch complex and a target of CheY, which lacks the phosphatase active site consensus sequence, and is not a CheY phosphatase. Pssm-ID: 381732 [Multi-domain] Cd Length: 162 Bit Score: 79.85 E-value: 1.75e-17
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| FliM | COG1868 | Flagellar motor switch protein FliM [Cell motility]; |
211-547 | 2.68e-17 | ||||||||
Flagellar motor switch protein FliM [Cell motility]; Pssm-ID: 441473 [Multi-domain] Cd Length: 326 Bit Score: 82.90 E-value: 2.68e-17
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| CheC_ClassI | cd17909 | chemotaxis protein CheC, Class I; This subfamily contains Class I CheC proteins with ... |
28-157 | 6.76e-17 | ||||||||
chemotaxis protein CheC, Class I; This subfamily contains Class I CheC proteins with phosphatase activity. The Class I cheC genes are generally found in firmicute and archaeal chemotaxis operons with cheD, usually translationally coupled. Class I CheCs interact with the CheD protein which is responsible for deamidation of certain glutamine residues to glutamates on the chemotaxis receptor proteins. This family contains two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site. The C-terminal helix of CheC acts as a mimic of the natural enzymatic target of CheD, the alpha-helical receptors, and serves as the binding site for CheD. The CheC/CheD heterodimerization increases CheY-P phosphatase activity five-fold. Class I CheCs are involved in adaptation of the chemotaxis system. Pssm-ID: 381737 [Multi-domain] Cd Length: 189 Bit Score: 79.00 E-value: 6.76e-17
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| FliN | COG1886 | Flagellar motor switch/type III secretory pathway protein FliN [Cell motility, Intracellular ... |
457-544 | 9.32e-17 | ||||||||
Flagellar motor switch/type III secretory pathway protein FliN [Cell motility, Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 441490 [Multi-domain] Cd Length: 172 Bit Score: 78.12 E-value: 9.32e-17
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| CheC | COG1776 | Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]; |
119-280 | 2.33e-16 | ||||||||
Phosphoaspartate phosphatase CheC, specific for CheY-P [Signal transduction mechanisms]; Pssm-ID: 441382 [Multi-domain] Cd Length: 199 Bit Score: 77.56 E-value: 2.33e-16
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| CheC_CheX_FliY | cd16353 | CheC/CheX/FliY (CXY) family phosphatases; The CXY family includes CheY-P-hydrolyzing proteins ... |
31-157 | 3.59e-16 | ||||||||
CheC/CheX/FliY (CXY) family phosphatases; The CXY family includes CheY-P-hydrolyzing proteins that function in bacterial chemotaxis, which involves cellular processes that control the movement of organisms toward favorable environments via rotating flagella, which in turn determines the sense of rotation by the intracellular response regulator CheY. When phosphorylated, CheY-P interacts directly with the flagellar motor, and this signal is terminated by the CXY family of phosphatases (Escherichia coli uses CheZ). CheC acts as a weak CheY-P phosphatase but increases activity in the presence of CheD. Bacillus subtilis has only CheC and FliY while many systems also have CheX. CheC and CheX appear to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM. CheC, CheX, and FliY phosphatases share a consensus sequence ([DS]xxxExxNx(22)P) with four conserved residues thought to form the phosphatase active site. CheC class I and FliY each have two active sites, while CheC class II and III, and CheX have only one. This family also includes FliM, a component of the flagellar switch complex and a target of CheY, which lacks the phosphatase active site consensus sequence, and is not a CheY phosphatase. Pssm-ID: 381732 [Multi-domain] Cd Length: 162 Bit Score: 76.00 E-value: 3.59e-16
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| CheC_ClassII | cd17910 | chemotaxis protein CheC, Class II; This family contains class II CheC proteins found in ... |
245-406 | 1.93e-13 | ||||||||
chemotaxis protein CheC, Class II; This family contains class II CheC proteins found in proteobacteria, which diverge from class I CheCs in sequence conservation and lack critical well-conserved residues for CheD binding. These proteins are likely to be dedicated phosphatases. The class II cheC genes are not found in chemotaxis operons, but in operons containing more archetypical two-component signaling components, non-signaling operons, or as orphans. Thus, class II CheCs appear to be involved in non-chemotactic two component systems. Class II CheCs lack the first of the two phosphatase active sites of class I CheCs, and retain the second active site of class I CheCs. Pssm-ID: 381738 [Multi-domain] Cd Length: 187 Bit Score: 68.67 E-value: 1.93e-13
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| FliMN_C | pfam01052 | Type III flagellar switch regulator (C-ring) FliN C-term; This family includes the C-terminal ... |
483-545 | 5.61e-13 | ||||||||
Type III flagellar switch regulator (C-ring) FliN C-term; This family includes the C-terminal region of flagellar motor switch proteins FliN and FliM. It is associated with family FliM, pfam02154 and family FliN_N pfam16973. Pssm-ID: 460043 [Multi-domain] Cd Length: 66 Bit Score: 63.90 E-value: 5.61e-13
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| CheC_ClassI | cd17909 | chemotaxis protein CheC, Class I; This subfamily contains Class I CheC proteins with ... |
123-280 | 8.70e-12 | ||||||||
chemotaxis protein CheC, Class I; This subfamily contains Class I CheC proteins with phosphatase activity. The Class I cheC genes are generally found in firmicute and archaeal chemotaxis operons with cheD, usually translationally coupled. Class I CheCs interact with the CheD protein which is responsible for deamidation of certain glutamine residues to glutamates on the chemotaxis receptor proteins. This family contains two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site. The C-terminal helix of CheC acts as a mimic of the natural enzymatic target of CheD, the alpha-helical receptors, and serves as the binding site for CheD. The CheC/CheD heterodimerization increases CheY-P phosphatase activity five-fold. Class I CheCs are involved in adaptation of the chemotaxis system. Pssm-ID: 381737 [Multi-domain] Cd Length: 189 Bit Score: 63.98 E-value: 8.70e-12
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| PRK08432 | PRK08432 | flagellar motor switch protein FliY; Validated |
289-544 | 8.98e-12 | ||||||||
flagellar motor switch protein FliY; Validated Pssm-ID: 236264 [Multi-domain] Cd Length: 283 Bit Score: 65.80 E-value: 8.98e-12
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| CheC_ClassII | cd17910 | chemotaxis protein CheC, Class II; This family contains class II CheC proteins found in ... |
28-186 | 2.59e-11 | ||||||||
chemotaxis protein CheC, Class II; This family contains class II CheC proteins found in proteobacteria, which diverge from class I CheCs in sequence conservation and lack critical well-conserved residues for CheD binding. These proteins are likely to be dedicated phosphatases. The class II cheC genes are not found in chemotaxis operons, but in operons containing more archetypical two-component signaling components, non-signaling operons, or as orphans. Thus, class II CheCs appear to be involved in non-chemotactic two component systems. Class II CheCs lack the first of the two phosphatase active sites of class I CheCs, and retain the second active site of class I CheCs. Pssm-ID: 381738 [Multi-domain] Cd Length: 187 Bit Score: 62.51 E-value: 2.59e-11
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| fliN | TIGR02480 | flagellar motor switch protein FliN; Proteins that consist largely of the domain described by ... |
474-544 | 4.02e-11 | ||||||||
flagellar motor switch protein FliN; Proteins that consist largely of the domain described by this model for this protein family can be designated flagellar motor switch protein FliN. Longer proteins in which this region is a C-terminal domain typically are designated FliY. More distantly related sequences, outside the scope of this family, are associated with type III secretion and include the surface presentation of antigens protein SpaO required or invasion of host cells by Salmonella enterica. [Cellular processes, Chemotaxis and motility] Pssm-ID: 131533 [Multi-domain] Cd Length: 77 Bit Score: 58.76 E-value: 4.02e-11
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| CheC_ClassI | cd17909 | chemotaxis protein CheC, Class I; This subfamily contains Class I CheC proteins with ... |
343-432 | 8.23e-11 | ||||||||
chemotaxis protein CheC, Class I; This subfamily contains Class I CheC proteins with phosphatase activity. The Class I cheC genes are generally found in firmicute and archaeal chemotaxis operons with cheD, usually translationally coupled. Class I CheCs interact with the CheD protein which is responsible for deamidation of certain glutamine residues to glutamates on the chemotaxis receptor proteins. This family contains two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site. The C-terminal helix of CheC acts as a mimic of the natural enzymatic target of CheD, the alpha-helical receptors, and serves as the binding site for CheD. The CheC/CheD heterodimerization increases CheY-P phosphatase activity five-fold. Class I CheCs are involved in adaptation of the chemotaxis system. Pssm-ID: 381737 [Multi-domain] Cd Length: 189 Bit Score: 61.29 E-value: 8.23e-11
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| CheC-like | cd17905 | chemotaxis protein CheC; includes CheC classes I, II, and III; This family contains chemotaxis ... |
32-159 | 1.08e-10 | ||||||||
chemotaxis protein CheC; includes CheC classes I, II, and III; This family contains chemotaxis protein CheC that acts as a weak CheY-P phosphatase but shows increased activity in the presence of CheD. This CheC family includes three classes: class I containing Bacillus subtilis CheC which might function as a regulator of CheD; class II CheCs that likely function as phosphatases in systems other than chemotaxis; and class III CheCs that are found chiefly in the archaeal class Halobacteria and might function similarly as class I CheCs. Class I CheCs contain two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site; class II and class III CheCs have only one actve site. Pssm-ID: 381733 [Multi-domain] Cd Length: 173 Bit Score: 60.66 E-value: 1.08e-10
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| CheC | pfam04509 | CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, ... |
122-159 | 2.37e-10 | ||||||||
CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, CheY-P, is important for allowing bacteria to respond to new environmental stimuli. The members of this family, CheC, CheX, CheA and FliY are CheY-P phosphatase. CheC appears to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. CheD enhances the activity of CheC 5-fold, which is normally relatively low. In some cases, the region represented by this entry is present as multiple copies. Pssm-ID: 398287 [Multi-domain] Cd Length: 38 Bit Score: 55.55 E-value: 2.37e-10
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| FliM | cd17908 | flagellar protein FliM; This family contains bacterial flagellar protein FliM which is ... |
260-409 | 4.44e-10 | ||||||||
flagellar protein FliM; This family contains bacterial flagellar protein FliM which is localized in the flagellar switch complex along with FliG and FliY; all are present in many copies, and together they correspond structurally to the C-ring of the flagellar basal body. FliM does not contain the CheC consensus sequence of the phosphatase active site ([DS]xxxExxNx(22)P) and is not a CheY-P phosphatase. FliM sits in the center of the rotor with the N-terminal region interacting with the signaling protein, phosphorylated CheY (CheY-P). The activated form of CheY destabilizes the parallel arrangement of FliM molecules, and perturbs FliG alignment in a process that may reflect the onset of rotation switching. This suggests a model of C-ring assembly in which intermolecular contacts among FliG domains provide a template for FliM assembly. Recent data show that binding of FliM to spermine synthase, SpeE, contributes to flagellar motility, an association that is unique to Helicobacter species. Pssm-ID: 381736 Cd Length: 181 Bit Score: 59.07 E-value: 4.44e-10
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| CheC-like | cd17905 | chemotaxis protein CheC; includes CheC classes I, II, and III; This family contains chemotaxis ... |
252-377 | 5.95e-10 | ||||||||
chemotaxis protein CheC; includes CheC classes I, II, and III; This family contains chemotaxis protein CheC that acts as a weak CheY-P phosphatase but shows increased activity in the presence of CheD. This CheC family includes three classes: class I containing Bacillus subtilis CheC which might function as a regulator of CheD; class II CheCs that likely function as phosphatases in systems other than chemotaxis; and class III CheCs that are found chiefly in the archaeal class Halobacteria and might function similarly as class I CheCs. Class I CheCs contain two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site; class II and class III CheCs have only one actve site. Pssm-ID: 381733 [Multi-domain] Cd Length: 173 Bit Score: 58.35 E-value: 5.95e-10
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| CheC | pfam04509 | CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, ... |
342-378 | 2.50e-09 | ||||||||
CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, CheY-P, is important for allowing bacteria to respond to new environmental stimuli. The members of this family, CheC, CheX, CheA and FliY are CheY-P phosphatase. CheC appears to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. CheD enhances the activity of CheC 5-fold, which is normally relatively low. In some cases, the region represented by this entry is present as multiple copies. Pssm-ID: 398287 [Multi-domain] Cd Length: 38 Bit Score: 52.85 E-value: 2.50e-09
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| CheX | cd17906 | chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very ... |
252-410 | 1.87e-08 | ||||||||
chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer. Pssm-ID: 381734 [Multi-domain] Cd Length: 148 Bit Score: 53.30 E-value: 1.87e-08
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| CheC_ClassII | cd17910 | chemotaxis protein CheC, Class II; This family contains class II CheC proteins found in ... |
122-292 | 2.81e-08 | ||||||||
chemotaxis protein CheC, Class II; This family contains class II CheC proteins found in proteobacteria, which diverge from class I CheCs in sequence conservation and lack critical well-conserved residues for CheD binding. These proteins are likely to be dedicated phosphatases. The class II cheC genes are not found in chemotaxis operons, but in operons containing more archetypical two-component signaling components, non-signaling operons, or as orphans. Thus, class II CheCs appear to be involved in non-chemotactic two component systems. Class II CheCs lack the first of the two phosphatase active sites of class I CheCs, and retain the second active site of class I CheCs. Pssm-ID: 381738 [Multi-domain] Cd Length: 187 Bit Score: 53.65 E-value: 2.81e-08
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| PRK08916 | PRK08916 | flagellar motor switch protein FliN; |
455-544 | 1.74e-07 | ||||||||
flagellar motor switch protein FliN; Pssm-ID: 236350 [Multi-domain] Cd Length: 116 Bit Score: 49.75 E-value: 1.74e-07
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| CheC | pfam04509 | CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, ... |
26-62 | 2.21e-07 | ||||||||
CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, CheY-P, is important for allowing bacteria to respond to new environmental stimuli. The members of this family, CheC, CheX, CheA and FliY are CheY-P phosphatase. CheC appears to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. CheD enhances the activity of CheC 5-fold, which is normally relatively low. In some cases, the region represented by this entry is present as multiple copies. Pssm-ID: 398287 [Multi-domain] Cd Length: 38 Bit Score: 47.08 E-value: 2.21e-07
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| CheC | pfam04509 | CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, ... |
245-282 | 6.50e-07 | ||||||||
CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, CheY-P, is important for allowing bacteria to respond to new environmental stimuli. The members of this family, CheC, CheX, CheA and FliY are CheY-P phosphatase. CheC appears to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. CheD enhances the activity of CheC 5-fold, which is normally relatively low. In some cases, the region represented by this entry is present as multiple copies. Pssm-ID: 398287 [Multi-domain] Cd Length: 38 Bit Score: 45.92 E-value: 6.50e-07
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| CheX_Thtogales | NF041094 | CheY-P phosphatase CheX; |
252-377 | 1.56e-06 | ||||||||
CheY-P phosphatase CheX; Pssm-ID: 469020 [Multi-domain] Cd Length: 152 Bit Score: 48.07 E-value: 1.56e-06
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| SpaO_YscQ | TIGR02551 | type III secretion system apparatus protein YscQ/HrcQ; Genes in this family are found in type ... |
478-544 | 1.99e-06 | ||||||||
type III secretion system apparatus protein YscQ/HrcQ; Genes in this family are found in type III secretion operons. The gene (YscQ) in Yersinia is essential for YOPs secretion, while SpaO in Shigella is involved in the Surface Presentation of Antigens apparatus found on the virulence plasmid, and HrcQ is involved in the Harpin secretory system in organisms like Pseudomonas syringae. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis] Pssm-ID: 274196 [Multi-domain] Cd Length: 298 Bit Score: 49.72 E-value: 1.99e-06
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| PRK06933 | PRK06933 | YscQ/HrcQ family type III secretion apparatus protein; |
478-545 | 5.10e-05 | ||||||||
YscQ/HrcQ family type III secretion apparatus protein; Pssm-ID: 235891 [Multi-domain] Cd Length: 308 Bit Score: 45.50 E-value: 5.10e-05
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| CheC_ClassIII | cd17911 | chemotactic protein CheC, Class III; This family contains class III CheC proteins, present ... |
75-156 | 1.31e-04 | ||||||||
chemotactic protein CheC, Class III; This family contains class III CheC proteins, present chiefly in the archaeal class Halobacteria. Sequence analysis shows that class III CheC proteins are structurally and functionally similar to class I CheCs, and not to CheX, despite the fact that both class III CheCs and CheX lack the first of the two phosphatase active sites of class I CheCs, and retain the second active site. Mutation analysis shows that the second active site is more important for function that the first one, suggesting that class III proteins arose by loss of the unnecessary first active site through mutational shift. All chemotactic archaea have a CheC homologue. Pssm-ID: 381739 [Multi-domain] Cd Length: 187 Bit Score: 42.92 E-value: 1.31e-04
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| CheX_Thtogales | NF041094 | CheY-P phosphatase CheX; |
32-165 | 1.96e-04 | ||||||||
CheY-P phosphatase CheX; Pssm-ID: 469020 [Multi-domain] Cd Length: 152 Bit Score: 41.91 E-value: 1.96e-04
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| fliN | PRK07963 | flagellar motor switch protein FliN; Validated |
473-544 | 2.33e-04 | ||||||||
flagellar motor switch protein FliN; Validated Pssm-ID: 181183 [Multi-domain] Cd Length: 137 Bit Score: 41.31 E-value: 2.33e-04
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| CheC-like | cd17905 | chemotaxis protein CheC; includes CheC classes I, II, and III; This family contains chemotaxis ... |
348-432 | 2.49e-04 | ||||||||
chemotaxis protein CheC; includes CheC classes I, II, and III; This family contains chemotaxis protein CheC that acts as a weak CheY-P phosphatase but shows increased activity in the presence of CheD. This CheC family includes three classes: class I containing Bacillus subtilis CheC which might function as a regulator of CheD; class II CheCs that likely function as phosphatases in systems other than chemotaxis; and class III CheCs that are found chiefly in the archaeal class Halobacteria and might function similarly as class I CheCs. Class I CheCs contain two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site; class II and class III CheCs have only one actve site. Pssm-ID: 381733 [Multi-domain] Cd Length: 173 Bit Score: 41.78 E-value: 2.49e-04
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| FliM | cd17908 | flagellar protein FliM; This family contains bacterial flagellar protein FliM which is ... |
40-189 | 2.62e-04 | ||||||||
flagellar protein FliM; This family contains bacterial flagellar protein FliM which is localized in the flagellar switch complex along with FliG and FliY; all are present in many copies, and together they correspond structurally to the C-ring of the flagellar basal body. FliM does not contain the CheC consensus sequence of the phosphatase active site ([DS]xxxExxNx(22)P) and is not a CheY-P phosphatase. FliM sits in the center of the rotor with the N-terminal region interacting with the signaling protein, phosphorylated CheY (CheY-P). The activated form of CheY destabilizes the parallel arrangement of FliM molecules, and perturbs FliG alignment in a process that may reflect the onset of rotation switching. This suggests a model of C-ring assembly in which intermolecular contacts among FliG domains provide a template for FliM assembly. Recent data show that binding of FliM to spermine synthase, SpeE, contributes to flagellar motility, an association that is unique to Helicobacter species. Pssm-ID: 381736 Cd Length: 181 Bit Score: 42.12 E-value: 2.62e-04
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| fliN | PRK05698 | flagellar motor switch protein FliN; |
490-544 | 2.92e-04 | ||||||||
flagellar motor switch protein FliN; Pssm-ID: 168189 [Multi-domain] Cd Length: 155 Bit Score: 41.32 E-value: 2.92e-04
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| FliM | pfam02154 | Flagellar motor switch protein FliM; |
262-410 | 4.90e-04 | ||||||||
Flagellar motor switch protein FliM; Pssm-ID: 111086 Cd Length: 192 Bit Score: 41.21 E-value: 4.90e-04
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| PRK08158 | PRK08158 | YscQ/HrcQ family type III secretion apparatus protein; |
478-547 | 6.96e-04 | ||||||||
YscQ/HrcQ family type III secretion apparatus protein; Pssm-ID: 181259 [Multi-domain] Cd Length: 303 Bit Score: 41.78 E-value: 6.96e-04
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| CheC_ClassIII | cd17911 | chemotactic protein CheC, Class III; This family contains class III CheC proteins, present ... |
295-377 | 8.26e-04 | ||||||||
chemotactic protein CheC, Class III; This family contains class III CheC proteins, present chiefly in the archaeal class Halobacteria. Sequence analysis shows that class III CheC proteins are structurally and functionally similar to class I CheCs, and not to CheX, despite the fact that both class III CheCs and CheX lack the first of the two phosphatase active sites of class I CheCs, and retain the second active site. Mutation analysis shows that the second active site is more important for function that the first one, suggesting that class III proteins arose by loss of the unnecessary first active site through mutational shift. All chemotactic archaea have a CheC homologue. Pssm-ID: 381739 [Multi-domain] Cd Length: 187 Bit Score: 40.61 E-value: 8.26e-04
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| fliM | PRK06666 | flagellar motor switch protein FliM; Validated |
262-545 | 1.15e-03 | ||||||||
flagellar motor switch protein FliM; Validated Pssm-ID: 235849 [Multi-domain] Cd Length: 337 Bit Score: 41.36 E-value: 1.15e-03
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| CheX | cd17906 | chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very ... |
32-157 | 1.16e-03 | ||||||||
chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer. Pssm-ID: 381734 [Multi-domain] Cd Length: 148 Bit Score: 39.43 E-value: 1.16e-03
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| CheC_CheX_FliY | cd16353 | CheC/CheX/FliY (CXY) family phosphatases; The CXY family includes CheY-P-hydrolyzing proteins ... |
128-284 | 3.11e-03 | ||||||||
CheC/CheX/FliY (CXY) family phosphatases; The CXY family includes CheY-P-hydrolyzing proteins that function in bacterial chemotaxis, which involves cellular processes that control the movement of organisms toward favorable environments via rotating flagella, which in turn determines the sense of rotation by the intracellular response regulator CheY. When phosphorylated, CheY-P interacts directly with the flagellar motor, and this signal is terminated by the CXY family of phosphatases (Escherichia coli uses CheZ). CheC acts as a weak CheY-P phosphatase but increases activity in the presence of CheD. Bacillus subtilis has only CheC and FliY while many systems also have CheX. CheC and CheX appear to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM. CheC, CheX, and FliY phosphatases share a consensus sequence ([DS]xxxExxNx(22)P) with four conserved residues thought to form the phosphatase active site. CheC class I and FliY each have two active sites, while CheC class II and III, and CheX have only one. This family also includes FliM, a component of the flagellar switch complex and a target of CheY, which lacks the phosphatase active site consensus sequence, and is not a CheY phosphatase. Pssm-ID: 381732 [Multi-domain] Cd Length: 162 Bit Score: 38.64 E-value: 3.11e-03
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