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evolution
ROF2 encodes a peptidyl-prolyl cis-trans isomerase of the FK506-binding protein class
evolution
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the enzyme belongs to the FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases, PPIases, which share a canonical domain fold consisting of a beta-sheet composed of four large and two small -strands, opposed by a single main alpha-helix
evolution
the enzyme belongs to the FK506-binding protein (FKBP) family whose members are peptidyl-prolyl cis-trans isomerases with the enzymatic function attributed to the FKBP domain. Six members of this family localize to the mammalian endoplasmic reticulum. Four of them, FKBP22 (encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65 (FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. All FKBP-EFs contain an endoplasmic reticulum retention signal at the C-terminus
evolution
the enzyme belongs to the parvulin family of peptidyl-prolyl cis/trans isomerases, PPIases
evolution
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the enzyme belongs to the parvulin family of peptidyl-prolyl cis/trans isomerases, PPIases
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malfunction
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Pin1 blockade leads to Bax cleavage, mitochondrial translocation and caspase 9 and 3 activation, irrespective of the presence of cytokines, and Pin1 blockade accelerates eosinophil apoptosis
malfunction
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Pin1 is deregulated in many tumors
malfunction
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Pin1 plays a role in neurodegenerative disease such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
malfunction
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Pin1 plays a role in neurodegenerative disease such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
malfunction
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Bacillus subtilis cells depleted of the PrsA protein are able to grow in the presence of a high concentration of magnesium (20 mM). PrsA depletion destabilizes penicillin-binding proteins
malfunction
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knockdown of FKBP1B induces eye formation malfunction
malfunction
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knockdown of Pin1 does not prevent CK2alpha phosphorylation
malfunction
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Pin1 depletion is linked to a dysfunction of uncoating of human immunodeficiency virus type 1
malfunction
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Pin1 knock-out mice exhibit impaired insulin signaling with glucose intolerance. Pin1 knock-out mice are resistant to diet-induced obesity
malfunction
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silencing of Pin1 expression results in decrease of hepatitis C virus replication in both hepatitis C virus replicon cells and cell culture grown hepatitis C virus-infected cells
malfunction
a DELTAef0685/DELTAef1534 mutant is more resistant to oxidative stress, is able to grow under a high manganese concentration, and shows altered resistance to ampicillin and quinolone antibiotics
malfunction
loss of function of ROF2, and especially double mutation of ROF2 and the closely related gene ROF1, results in acid sensitivity, stress and development phenotypes of ROF mutants, overview
malfunction
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Bacillus subtilis cells depleted of the PrsA protein are able to grow in the presence of a high concentration of magnesium (20 mM). PrsA depletion destabilizes penicillin-binding proteins
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physiological function
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Arabidopsis thaliana PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SOC1 and AGL24. The Ser/Thr-Pro motifs are important for Pin1At function in promoting flowering through AGL24 and SOC1. Phosphorylation-dependent prolyl cis/trans isomerization of key transcription factors is an important flowering regulatory mechanism, overview
physiological function
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Cj0596 plays a role in interaction with host cells. Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization
physiological function
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cyclophilin A is an essential cofactor for hepatitis C virus infection and the intracellular target of cyclosporines anti-HCV effect, mechanism by which CyPA facilitates HCV replication, overview
physiological function
FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1, PPIase-dependent molecular mechanism, overview. PPIase-dependent regulation of netrin-1-induced Ca2+ influx by FKBP52. FKBP52 and its regulation of TRPC1 are essential for commissural axon guidance in vivo. The PPIase activity of FKBP52 is required for MAG-induced, but not for Sema3-induced, growth cone repulsion
physiological function
FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1, PPIase-dependent molecular mechanism, overview. PPIase-dependent regulation of netrin-1-induced Ca2+ influx by FKBP52. FKBP52 and its regulation of TRPC1 are essential for commissural axon guidance in vivo. The PPIase activity of FKBP52 is required for MAG-induced, but not for Sema3-induced, growth cone repulsion
physiological function
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peptidyl-prolyl isomerase, Pin1, is a critical regulator of NF-kappaB activation facilitating NF-kappaB binding in hepatocytes and protects against hepatic ischemia/reperfusion injury. Pin1 is required for full production of MIP-2, but not for production of TNFalpha
physiological function
peptidylprolyl isomerases play essential roles in protein folding and are implicated in immune response and cell cycle control. Bombyx mori PPIases may be involved in anti-Bombyx mori nucleopolyhedrovirus response, mechanism, overview
physiological function
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Pin1 is a key mediator of pro-survival signaling and a regulator of the pro-apoptotic Bcl-2-associated X protein, Bax, function. Pin1 likely functions as a downstream effector of GM-CSF and IL-5 signaling, and regulates cell death through the intrinsic, mitochondria- and caspase 9-dependent, apoptotic pathway, overview
physiological function
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Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, and with protein phosphatases, such as protein phosphatase 1A and 2B, in a wide range of cellular processes including cell division, DNA damage response, and gene transcription, and in susceptibility to cancer and neurogenerative diseases, detailed overview. Pin1 modulates excitotoxic and oxidative stress induced by perkaryal phosphorylation of NF-H. Pin1 mediates the neural-specific apoptosis machinery. Pin1 is involved in regulation of SMRT levels. Pin1 plays a post-phosphorylation role in regulating protein function, mechanisms, overview
physiological function
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Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, and with protein phosphatases, such as protein phosphatase 1A and 2B, in a wide range of cellular processes including cell division, DNA damage response, and gene transcription, and in susceptibilty to cancer and neurogenerative diseases, detailed overview. Pin1 modulates excitotoxic and oxidative stress induced by perkaryal phosphorylation of NF-H. Pin1 is involved in regulation of SMRT levels. Pin1 mediates the neural-specific apoptosis machinery. Pin1 plays a post-phosphorylation role in regulating protein function, mechanisms, overview
physiological function
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Pin1 is critical for the regulation of serine/threonine protein kinase B, PKB/Akt, stability and activation phosphorylation at S473 through the phosphorylated Thr-Pro motifs of Akt. Roles of Akt and Pin1 in oncogenesis, overview
physiological function
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Pin1 markedly enhances transformation in primary lymphocytes by the c-Rel protein and by viral Rel/NF-kappaB oncoprotein v-Rel, it enhances the nuclear translocation of the Rel proteins, overview
physiological function
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Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylation-dependent conformational changes relevant for protein function. In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis, signaling role of PP2A by Pin1, overview
physiological function
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Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylationdependent conformational changes relevant for protein function. In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis, signaling role of PP2A by Pin1, overview
physiological function
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Pin1 regulates the function and/or stability of phosphoproteins by altering the conformation of specific pSer/pThr-Pro peptide bonds
physiological function
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SurA may function to repair, or prevent damage to, the outer membrane upon exposure to PmB and may consequently limit damage to the inner-membrane
physiological function
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the Pin1 is located in the midbody ring in HeLa cells and regulates cell cycle progression and cytokinesis through centrosome protein Cep55, which is an essential component of the midbody ring
physiological function
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colicin M unfolds during transfer across the outer or cytoplasmic membrane and refolds to the active form in the periplasm assisted by prolyl cis-trans isomerase/chaperone FkpA
physiological function
Par45 is a phosphorylation-independent parvulin required for normal cell proliferation in a unicellular eukaryotic cell
physiological function
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peptidyl-prolyl isomerase Pin1 is required for CK2alpha mitotic spindle localization. Pin1 protects CK2alpha from dephosphorylation in vivo
physiological function
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peptidyl-prolyl isomerase SLyD controls the recombinant folding of bacteriophage T4 long tail fiber fragments
physiological function
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Pin1 is a host factor for hepatitis C virus propagation and may contribute to hepatitis C virus-induced liver pathogenesis. Both binding and isomerase activities of Pin1 are essential for hepatitis C virus replication
physiological function
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Pin1 plays a critical role in adipose differentiation. Pin1 binds to IRS-1 and thereby markedly enhances insulin action, essential for adipogenesis
physiological function
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Pin1 plays a critical role in adipose differentiation. Pin1 binds to IRS-1 and thereby markedly enhances insulin action, essential for adipogenesis
physiological function
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Pin1 prolyl isomerase activity is required for the disassembly of the human immunodeficiency virus type 1 core
physiological function
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PrsA catalyses the post-translocational folding of exported proteins and is essential for normal growth of Bacillus subtilis. PrsA is involved in the biosynthesis of the cylindrical lateral wall. PrsA is required for the folding of penicillin-binding protein 2a
physiological function
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Xenopus peptidyl-prolyl cis-trans isomerase FKBP1B induces ectopic secondary axis and is involved in eye formation during Xenopus embryogenesis
physiological function
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Fpr4 has been described as a histone chaperone, and is implicated in epigenetic function in part due to its mediation of cis-trans conversion of proline residues within histone tails
physiological function
peptidyl-prolyl cis-trans isomerase ROF2 modulates intracellular pH homeostasis. As ROF2 induction and intracellular acidification are common consequences of many stresses, this mechanism of pH homeostasis may be of general importance for stress tolerance. Chaperone ROF2 not only helps to refold proteins but also activates H+ extrusion to restore intracellular pH
physiological function
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peptidyl-prolyl isomerase activity of FKBP12 is essential for prevention of aggregation of tau, an Alzheimer's disease-related protein. Tau aggregates into neurofibrillary tangles when it is hyperphosphorylated, only the cis-isomer can aggregate. FKBP12 catalyzes isomerization of the tau R3 peptide peptide in both the monomeric and aggregative states, once the cis-isomer is converted into the trans-isomer in the aggregative state, the trans-isomer is quickly released from the aggregation because the trans-isomer cannot aggregate, inhibitory mechanism of R3 peptide aggregation by simple binding of FKBP12, overview. IC50 of FKBP12 is 0.003 mM. The aggregation inhibitory activity of FKBP12 is independent of the affinity between FKBP12 and the R3 peptide. Therefore, the aggregation inhibitory activity of FKBP12 depends only on the PPIase activity of FKBP12
physiological function
peptidylprolyl cis/trans isomerases are enzymes involved in protein folding. The parvulin family rotamase EF0685 and the cyclophilin family member EF1534 are important for virulence and resistance to NaCl, while EF2898 is not important for the Enterococcus faecalis stress response or virulence
physiological function
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CYPJ promotes the transition of cells from G1 phase to S phase by activating cyclin D1 promoter. CYPJ overexpression accelerates liver cell growth in vitro and in vivo. Inhibition of CYPJ by cyclosporin A or CYPJ-specific RNAi diminishes the growth of liver cancer cells in vitro and in vivo
physiological function
deletion of PrsA leads to a decrease in secreted protease and phospholipase activity. Deletion does not alter the growth characteristics of Staphylococcus aureus
physiological function
disruption of ppiB does not alter the growth characteristics of the strains but results in decreased activity of secreted virulence factor nuclease Nuc in culture supernatants, probably resulting from misfolding of Nuc in the absence of PpiB. Ppib directly interacts with Nuc in vitro
physiological function
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enzyme displays chaperone activity in a citrate synthase thermal aggregation activity assay
physiological function
enzyme interacts with calmodulin in vivo and in vitro. In vitro interaction is Ca2+-dependent, and the calmodulin-binding domain is localized to 35-70 amino acid residues in the N-terminus
physiological function
enzyme regulates lysyl hydroxylase LH2-mediated collagen cross-linking. FKBP65 deficiency diminishes hydroxylysine-aldehyde derived intermolecular collagen cross-links and increases the non-hydroxylated lysine-aldehyde-derived collagen cross-links
physiological function
expression of a wheat cyclophilin CypA-1 confers thermotolerance to Escherichia coli. Expression of deletion mutants that lack peptidyl-prolyl cis-trans isomerase activity, results in abrogation of thermotolerance. CypA-1 interacts with calmodulin, and the Calmodulin-binding domain is localized to amino acid residues 51-71 in the N-terminal region
physiological function
FkpA delays the aggregation of citrate synthase in vitro and has a positive effect on the activity and temperature range of citrate synthase in vitro. Deletion of FkpA causes a 50% reduced biomass yield compared to that of the wild type when grown at 37°C, whereas there is only a 10% reduced biomass yield at the optimal growth temperature of 30°C accompanied by accumulation of 7 mM L-glutamate and 22 mM 2-oxoglutarate
physiological function
HepG2 cells treated with recombinant isomerase protein exhibit a reduction in the formation of hydrogen peroxide-mediated reactive oxygen species. Treatment diminishes H2O2-mediated oxidative stress and restores both the expression and the activity of antioxidant enzymes, including superoxide dismutase, catalase, glutathione peroxidase and thioredoxin reductase. Superoxide dismutase, catalase and thioredoxin reductase activixadties are upregulated by treatment with the purified protein
physiological function
In response to genotoxic drug doxorubicin, Pin1 binds and decreases levels of the phosphorylated Foxo3, the positive transcription factor of P-glycoprotein (P-gp) gene. Thereby, Pin1 decreases the level of P-gp and signals the cell to pump the genotoxic drugs out
physiological function
loss of PinA leads to decreased growth rate, reduced spore formation and abnormal prespore-prestalk patterning. Expression of PinA complements the temperature sensitivity phenotype associated with a mutation in ESS1 in Saccharomyces cerevisiae
physiological function
mice lacking the Pin1 gene form more megakaryocytes than wild type mice, and the proplatelet formation of megakaryocytes is poorer in Pin1-/- mice than in wild-type mice. Treatment of megakaryoblastic floating cell line Meg-01 with shRNA against Pin1 suppresses the proplatelet formation. Expression of tau, a microtubule associated protein is induced in megakaryocytes during proplatelet formation. Pin1 binds tau and promotes microtubule polymerization
physiological function
overexpression lengthens the locomotor behavioral period. Dod associates preferentially with phosphorylated species of PERIOD, associated with the circadian clock machinery, which delays the phosphorylation-dependent degradation of PERIOD. PERIOD protein levels are higher in flies overexpressing Dod
physiological function
PIN1 directly interacts with hypoxia-inducible factor HIF-1alpha in human colon cancer cells. PIN1 binding occurs in a phosphorylation-dependent manner, and at both exogenous and endogenous levels. Binding stabilizes the HIF-1alpha protein, resulting in increased transcriptional activity, and upregulating expression of vascular endothelial growth factor. Silencing of PIN1 or pharmacologic inhibition of its activity abrogates the angiogenesis
physiological function
PIN1 inhibition dramatically reduces the tumor volume in a subcutaneous mouse xenograft model and angiogenesis as well as hypoxia-induced transcriptional activity of hypoxia-inducible factor HIF-1alpha
physiological function
Pin1 interacts with hypoxia-inducible transcription factor HIF-1alpha. The interaction is regulated through p42/p44 MAPK pathway activation, and Pin1 catalytic activity generates a conformational change in HIF-1alpha. Pin1 is required for gene-specific HIF-1 transcriptional activity
physiological function
Pin1 interacts with the cytoplasmic domain of tissue factor. Pin1 is able to bind wild-type and mutant forms of overexpressed tissue factor-tGFP fusion proteins. Pin1 coimmunoprecipitates with overexpressed wild-type tissue factor-tGFP but not Ser258Ala or Pro259Ala substituted mutants. Pin1 is capable of interfering with the ubiquitination and dephosphorylation of tissue factor-derived peptides
physiological function
recombinant expression in Escherichia coli increases its temperature and salinity tolerance´
physiological function
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PrsA catalyses the post-translocational folding of exported proteins and is essential for normal growth of Bacillus subtilis. PrsA is involved in the biosynthesis of the cylindrical lateral wall. PrsA is required for the folding of penicillin-binding protein 2a
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physiological function
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enzyme displays chaperone activity in a citrate synthase thermal aggregation activity assay
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physiological function
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FkpA delays the aggregation of citrate synthase in vitro and has a positive effect on the activity and temperature range of citrate synthase in vitro. Deletion of FkpA causes a 50% reduced biomass yield compared to that of the wild type when grown at 37°C, whereas there is only a 10% reduced biomass yield at the optimal growth temperature of 30°C accompanied by accumulation of 7 mM L-glutamate and 22 mM 2-oxoglutarate
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physiological function
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deletion of PrsA leads to a decrease in secreted protease and phospholipase activity. Deletion does not alter the growth characteristics of Staphylococcus aureus
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physiological function
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disruption of ppiB does not alter the growth characteristics of the strains but results in decreased activity of secreted virulence factor nuclease Nuc in culture supernatants, probably resulting from misfolding of Nuc in the absence of PpiB. Ppib directly interacts with Nuc in vitro
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physiological function
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peptidyl-prolyl isomerase SLyD controls the recombinant folding of bacteriophage T4 long tail fiber fragments
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physiological function
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Cj0596 plays a role in interaction with host cells. Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization
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physiological function
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colicin M unfolds during transfer across the outer or cytoplasmic membrane and refolds to the active form in the periplasm assisted by prolyl cis-trans isomerase/chaperone FkpA
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additional information
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SurA and FkpA are not involved in the starvation-stress response, SSR. Genes surA and fkpA appear to be dispensable for the cross-resistance of carbon-starved cells to oxidative stress
additional information
active site Cys113
additional information
EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
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EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
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length of helix alpha3 contributes significantly to the preservation of the structure, function, and stability of Escherichia coli FKBP22. Homology modeling of the three-dimensional enzyme structure, overview
additional information
ROF2 overexpressing plants show tolerance to toxic cations such as lithium, norspermidine and hygromycin B, whose uptake is driven by the membrane potential, due to activation of the electrogenic plasma membrane proton pump, ROF2 activates K+ transport, H+-ATPase, phenotypes, overview
additional information
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ROF2 overexpressing plants show tolerance to toxic cations such as lithium, norspermidine and hygromycin B, whose uptake is driven by the membrane potential, due to activation of the electrogenic plasma membrane proton pump, ROF2 activates K+ transport, H+-ATPase, phenotypes, overview
additional information
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the canonical FKBP catalytic domain actively increases the rate of isomerization of three decapeptides derived from the N-terminus of yeast histone H3, whereas maintaining intrinsic cis and trans populations. A notable feature of the FKBP catalytic domain is a prominent hydrophobic pocket that is thought to bind the proline. Specifically, Trp345 lies at the bottom of the hydrophobic pocket, with the additional residues Tyr313, Phe323, Phe332, Phe334, Val341, Ile342, Tyr368, and Phe384 forming the sides of the proline-binding cavity. The final residue, Asp324, provides a contrast to the largely hydrophic nature of the cavity. Asp324 along with the less-conserved Glu340 together comprise a small acidic region at the side of the hydrophobic pocket in Fpr4 that is otherwise surrounded by a large surface region enriched in positively charged amino acids
additional information
three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
additional information
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three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
additional information
Y100 is a key residue for the catalytic activity, catalytic mechanism of PvFKBP35-mediated cis-trans isomerization of substrate, overview
additional information
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Y100 is a key residue for the catalytic activity, catalytic mechanism of PvFKBP35-mediated cis-trans isomerization of substrate, overview
additional information
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three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
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