MULTISPECIES: envelope stress response membrane protein PspB [Vibrio]
Protein Classification
phage shock protein B( domain architecture ID 10013244)
phage shock protein B is a cytoplasmic membrane protein that is part of a conserved extracytoplasmic stress response in bacteria
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| pspB | PRK09458 | envelope stress response membrane protein PspB; |
1-73 | 8.62e-38 | ||
envelope stress response membrane protein PspB; : Pssm-ID: 236526 Cd Length: 75 Bit Score: 120.37 E-value: 8.62e-38
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| Name | Accession | Description | Interval | E-value | ||
| pspB | PRK09458 | envelope stress response membrane protein PspB; |
1-73 | 8.62e-38 | ||
envelope stress response membrane protein PspB; Pssm-ID: 236526 Cd Length: 75 Bit Score: 120.37 E-value: 8.62e-38
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| PspB | pfam06667 | Phage shock protein B; This family consists of several bacterial phage shock protein B (PspB) ... |
5-73 | 5.72e-35 | ||
Phage shock protein B; This family consists of several bacterial phage shock protein B (PspB) sequences. The phage shock protein (psp) operon is induced in response to heat, ethanol, osmotic shock and infection by filamentous bacteriophages. Expression of the operon requires the alternative sigma factor sigma54 and the transcriptional activator PspF. In addition, PspA plays a negative regulatory role, and the integral-membrane proteins PspB and PspC play a positive one. Pssm-ID: 429060 Cd Length: 73 Bit Score: 113.07 E-value: 5.72e-35
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| phageshock_pspB | TIGR02976 | phage shock protein B; This model describes the PspB protein of the psp (phage shock protein) ... |
1-73 | 4.01e-28 | ||
phage shock protein B; This model describes the PspB protein of the psp (phage shock protein) operon, as found in Escherichia coli and many related species. Expression of a phage protein called secretin protein IV, and a number of other stresses including ethanol, heat shock, and defects in protein secretion trigger sigma-54-dependent expression of the phage shock regulon. PspB is both a regulator and an effector protein of the phage shock response. [Cellular processes, Adaptations to atypical conditions] Pssm-ID: 132021 Cd Length: 75 Bit Score: 95.90 E-value: 4.01e-28
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| 7tm_GPR137B | cd21476 | Integral membrane protein GPR137B, an orphan receptor member of the seven-transmembrane G ... |
3-30 | 5.14e-03 | ||
Integral membrane protein GPR137B, an orphan receptor member of the seven-transmembrane G protein-coupled receptor superfamily; GPR137B, also called transmembrane 7 superfamily member 1 (TM7SF1), is a lysosome integral membrane protein that is strongly expressed in the heart, liver, kidney, and brain. It is an orphan G protein-coupled receptor (GPCR) associated with M2 macrophage polarization, and has been shown to perform a regulatory function in controlling dynamic Rag and mTORC1 localization and activity, as well as lysosome morphology. It also plays a role in bone remodeling in mouse and zebrafish, functioning as a negative regulator of osteoclast activity essential for normal resorption and patterning of the skeleton. GPCRs transmit physiological signals from the outside of the cell to the inside via G proteins. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. Pssm-ID: 410553 Cd Length: 320 Bit Score: 33.63 E-value: 5.14e-03
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| Name | Accession | Description | Interval | E-value | ||
| pspB | PRK09458 | envelope stress response membrane protein PspB; |
1-73 | 8.62e-38 | ||
envelope stress response membrane protein PspB; Pssm-ID: 236526 Cd Length: 75 Bit Score: 120.37 E-value: 8.62e-38
|
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| PspB | pfam06667 | Phage shock protein B; This family consists of several bacterial phage shock protein B (PspB) ... |
5-73 | 5.72e-35 | ||
Phage shock protein B; This family consists of several bacterial phage shock protein B (PspB) sequences. The phage shock protein (psp) operon is induced in response to heat, ethanol, osmotic shock and infection by filamentous bacteriophages. Expression of the operon requires the alternative sigma factor sigma54 and the transcriptional activator PspF. In addition, PspA plays a negative regulatory role, and the integral-membrane proteins PspB and PspC play a positive one. Pssm-ID: 429060 Cd Length: 73 Bit Score: 113.07 E-value: 5.72e-35
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| phageshock_pspB | TIGR02976 | phage shock protein B; This model describes the PspB protein of the psp (phage shock protein) ... |
1-73 | 4.01e-28 | ||
phage shock protein B; This model describes the PspB protein of the psp (phage shock protein) operon, as found in Escherichia coli and many related species. Expression of a phage protein called secretin protein IV, and a number of other stresses including ethanol, heat shock, and defects in protein secretion trigger sigma-54-dependent expression of the phage shock regulon. PspB is both a regulator and an effector protein of the phage shock response. [Cellular processes, Adaptations to atypical conditions] Pssm-ID: 132021 Cd Length: 75 Bit Score: 95.90 E-value: 4.01e-28
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| 7tm_GPR137B | cd21476 | Integral membrane protein GPR137B, an orphan receptor member of the seven-transmembrane G ... |
3-30 | 5.14e-03 | ||
Integral membrane protein GPR137B, an orphan receptor member of the seven-transmembrane G protein-coupled receptor superfamily; GPR137B, also called transmembrane 7 superfamily member 1 (TM7SF1), is a lysosome integral membrane protein that is strongly expressed in the heart, liver, kidney, and brain. It is an orphan G protein-coupled receptor (GPCR) associated with M2 macrophage polarization, and has been shown to perform a regulatory function in controlling dynamic Rag and mTORC1 localization and activity, as well as lysosome morphology. It also plays a role in bone remodeling in mouse and zebrafish, functioning as a negative regulator of osteoclast activity essential for normal resorption and patterning of the skeleton. GPCRs transmit physiological signals from the outside of the cell to the inside via G proteins. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. Pssm-ID: 410553 Cd Length: 320 Bit Score: 33.63 E-value: 5.14e-03
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