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There are several matches for 'molecular chaperone GrpE'.
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10631 matches
showing page 1 of 532
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organism
protein
1)
Homo sapiens
GRPEL1 - GrpE protein homolog 1, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner (By similarity). Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. Belongs to the GrpE family.
[a.k.a. AF087896, GREPEL1, 80273,
Molecular chaperone GrpE
]
2)
Homo sapiens
GRPEL2 - GrpE protein homolog 2, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity); Belongs to the GrpE family.
[a.k.a. UPI0001D3BA37, DKFZp451C205, OMIM:618545,
Molecular chaperone GrpE
]
3)
Mus musculus
Grpel1 - GrpE protein homolog 1, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity).
[a.k.a. GrpE-like 1, mitochondrial, GrpE protein homolog 1, mitochondrial, ENSMUSG00000029198,
Molecular chaperone GrpE
]
4)
Mus musculus
Grpel2 - GrpE protein homolog 2, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70; Belongs to the GrpE family.
[a.k.a. AAH68232.1, XR_385980, 17714,
Molecular chaperone GrpE
]
5)
Drosophila melanogaster
Roe1 - GrpE protein homolog, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity).
[a.k.a. FBgn0014877, Roe1-PA, 36508,
Molecular chaperone GrpE
]
6)
Caenorhabditis elegans
C34C12.8 - GrpE protein homolog, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity).
[a.k.a. CAA87101, UPI000012BB18, 175449,
Molecular chaperone GrpE
]
7)
Escherichia coli K12
grpE - Heat shock protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depen [...]
[a.k.a. b2614, AAC75663.1, NP_417104.1,
Molecular chaperone GrpE
]
8)
Saccharomyces cerevisiae
MGE1 - GrpE protein homolog, mitochondrial; Mitochondrial matrix cochaperone; nucleotide release factor for Ssc1p in protein translocation and folding; also acts as cochaperone for Ssq1p in folding of Fe-S cluster proteins; acts as oxidative sensor to regulate mitochondrial Ssc1p; in presence of oxidative stress, dimeric Mge1p becomes a monomer and unable to regulate Ssc1p function; homolog of E. coli GrpE and human Mge1 (GRPEL1), which also responds to oxidative stress; Belongs to the GrpE family.
[a.k.a. YOR232W, S000005758, P38523,
Molecular chaperone GrpE
]
9)
Escherichia coli K12
slyA - Global transcriptional regulator; Transcription regulator that can specifically activate or repress expression of target genes. Activates expression of genes such as
molecular
chaperones
(groL, groS, dnaK,
grpE
, and cbpA), proteins involved in acid resistance (hdeA, hdeB, and gadA), the starvation lipoprotein slp, virulence protein hlyE/clyA. Represses expression of genes involved in the histidine biosynthetic pathway such as hisA, hisB, hisD, hisF and hisG. Required for the activation of virulence genes; Belongs to the SlyA family.
[a.k.a. b1642, AAC74714.2, DNA-binding transcriptional dual regulator SlyA]
10)
Abiotrophia defectiva
grpE - Co-chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depend [...]
[a.k.a. ESK65280.1, GCWU000182_001441, adc:FOC79_08690,
Molecular chaperone GrpE
]
11)
Acaryochloris marina
grpE - Co-chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depend [...]
[a.k.a. AM1_0421, ABW25478.1, WP_012161085.1,
Molecular chaperone GrpE
]
12)
Accumulibacter phosphatis
grpE - GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...]
[a.k.a. CAP2UW1_0502, ACV33853.1, C7RL31,
Molecular chaperone GrpE
]
13)
Accumulibacter phosphatis
ACV34434.1 - GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...]
[a.k.a. CAP2UW1_1100, WP_015765671.1, C7RQT6,
Molecular chaperone GrpE
]
14)
Acetanaerobacterium elongatum
grpE -
Molecular
chaperone
GrpE
; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and
GrpE
. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex.
GrpE
releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...]
[a.k.a. SDN91782.1, SAMN05192585_1397, A0A1H0FBC5_9FIRM,
molecular chaperone GrpE
,
Molecular chaperone GrpE
, ...]
15)
Acetitomaculum ruminis
grpE -
Molecular
chaperone
GrpE
; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and
GrpE
. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex.
GrpE
releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...]
[a.k.a. SAMN05216249_1159, SFB24595.1, A0A1I0ZG20,
molecular chaperone GrpE
,
Molecular chaperone GrpE
, ...]
16)
Acetivibrio ethanolgignens
grpE -
Molecular
chaperone
GrpE
; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and
GrpE
. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex.
GrpE
releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...]
[a.k.a. ASU35_07920, KSV59793.1, NZ_LNAM01000090.1,
molecular chaperone GrpE
,
Molecular chaperone GrpE
, ...]
17)
Acetoanaerobium sticklandii
grpE - GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interacti [...]
[a.k.a. CLOST_1794, CBH21914.1, GrpE,
Molecular chaperone GrpE
]
18)
Acetobacter aceti
grpE - Nucleotide exchange factor GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds [...]
[a.k.a. A0U92_16440, AQS86074.1, nucleotide exchange factor GrpE,
Molecular chaperone GrpE
]
19)
Acetobacter ascendens
grpE - Nucleotide exchange factor GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds [...]
[a.k.a. A4S02_11140, AOW47231.1, AOW47231,
Molecular chaperone GrpE
]
20)
Acetobacter ghanensis
grpE -
Molecular
chaperone
GrpE
; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and
GrpE
. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex.
GrpE
releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...]
[a.k.a. AGA_803, CEF54481.1, A0A0U5F2J5,
molecular chaperone GrpE
,
Molecular chaperone GrpE
, ...]
10631 matches
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