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There are several matches for 'co-chaperone GrpE'.
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815 matches
showing page 1 of 41
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organism
protein
1)
Escherichia coli K12
dnaJ -
Chaperone
Hsp40, DnaK
co
-
chaperone
; Interacts with DnaK and
GrpE
to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 t [...]
[a.k.a. b0015, AAC73126.1, P08622]
2)
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,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
3)
Absiella dolichum
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. EUBDOL_01828, EDP10577.1, A8REL9_9FIRM,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
4)
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,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
5)
Acetobacteraceae bacterium AT5844
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. HMPREF9946_05072, EHL95810.1, EHL95810,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
6)
Acetomicrobium hydrogeniformans
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. HMPREF1705_02923, KRT35680.1, KRT35680,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
7)
Acetonema longum
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. ALO_13654, EGO63305.1,
co-chaperone grpe
,
Co-chaperone grpe
]
8)
Acidithiobacillus ferrooxidans
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. AFE_2666, ACK80271.1, ACK80271,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
9)
Acidobacterium capsulatum
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. ACP_2087, ACO31724.1, WP_015897188.1,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
10)
Actinobaculum sp. F0552
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. ERH19053.1, HMPREF0043_00912, U1RHD2,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
11)
Actinomyces sp. F0311
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. ERH28817.1, HMPREF1980_01182, U1SDS0_9ACTO,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
12)
Actinomyces sp. F0330
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. EHM95403.1, HMPREF0975_00516, EHM95403,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
13)
Actinomyces sp. F0386
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. HMPREF9056_01134, EGF55805.1,
co-chaperone GrpE
,
Co-chaperone GrpE
]
14)
Actinomyces sp. ICM47
grpE_1 -
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. HMPREF1136_0063, EJG15102.1, J1LNI3_9ACTO,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
15)
Actinomyces sp. ICM47
grpE_2 -
Co
-
chaperone
GrpE
; An automated process has identified a potential problem with this gene model; the current end5 and/or the end3 may need to extended or the current gene model may need to be merged with a neighboring gene model; the current gene model (or a revised gene model) may contain a frame shift.
[a.k.a. EJG14268.1, HMPREF1136_0431, NZ_ALCA01000127.1,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
16)
Aerococcus urinae
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. HMPREF9243_1127, AEA00584.1, F2I4Z5,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
17)
Aeromicrobium marinum
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. HMPREF0063_12696, EFQ82172.1, E2SF87_9ACTN,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
18)
Aeromonas hydrophila
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. AHA_2984, ABK37883.1, YP_857488.1,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
19)
Aggregatibacter sp. W10330
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. HMPREF9065_00242, ERH28974.1, U1R5X1,
co-chaperone GrpE
,
Co-chaperone GrpE
, ...]
20)
Ahrensia sp. R2A130
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. EFL89734.1, R2A130_2344,
co-chaperone GrpE
,
Co-chaperone GrpE
]
815 matches
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