LBAT_0534 protein (Lactobacillus acetotolerans)

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[Homology]

Score

LBAT_0534

Thioredoxin. (106 aa)

Predicted Functional Partners:

msrA

0.880

dnaK

0.810

dnaJ

0.787

LBAT_0535

0.786

msrB

0.715

LBAT_0056

0.711

LBAT_1323

0.703

LBAT_0489

0.700

trxB

0.696

rbsK

0.649

Your Current Organism:

Lactobacillus acetotolerans

NCBI taxonomy Id: 1600
Other names: ATCC 43578, CCUG 32229, CIP 103180, DSM 20749, JCM 3825, L. acetotolerans, LMG 10751, LMG:10751, Lactobacillus acetitolerans, NBI 3014

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
LBAT_0056	LBAT_0534	LBAT_0056	LBAT_0534	Ribonucleoside triphosphate reductase.	Thioredoxin.	0.711
LBAT_0489	LBAT_0534	LBAT_0489	LBAT_0534	Thioredoxin reductase.	Thioredoxin.	0.700
LBAT_0489	trxB	LBAT_0489	LBAT_1152	Thioredoxin reductase.	Thioredoxin reductase.	0.443
LBAT_0534	LBAT_0056	LBAT_0534	LBAT_0056	Thioredoxin.	Ribonucleoside triphosphate reductase.	0.711
LBAT_0534	LBAT_0489	LBAT_0534	LBAT_0489	Thioredoxin.	Thioredoxin reductase.	0.700
LBAT_0534	LBAT_0535	LBAT_0534	LBAT_0535	Thioredoxin.	phenylalanyl-tRNA synthase; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.	0.786
LBAT_0534	LBAT_1323	LBAT_0534	LBAT_1323	Thioredoxin.	Conserved hypothetical protein.	0.703
LBAT_0534	dnaJ	LBAT_0534	LBAT_0714	Thioredoxin.	Chaperone protein DnaJ; 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 triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]	0.787
LBAT_0534	dnaK	LBAT_0534	LBAT_0713	Thioredoxin.	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.810
LBAT_0534	msrA	LBAT_0534	LBAT_0835	Thioredoxin.	Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.	0.880
LBAT_0534	msrB	LBAT_0534	LBAT_0834	Thioredoxin.	Methionine sulfoxide reductase.	0.715
LBAT_0534	rbsK	LBAT_0534	LBAT_1253	Thioredoxin.	Ribokinase; Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.	0.649
LBAT_0534	trxB	LBAT_0534	LBAT_1152	Thioredoxin.	Thioredoxin reductase.	0.696
LBAT_0535	LBAT_0534	LBAT_0535	LBAT_0534	phenylalanyl-tRNA synthase; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.	Thioredoxin.	0.786
LBAT_1323	LBAT_0534	LBAT_1323	LBAT_0534	Conserved hypothetical protein.	Thioredoxin.	0.703
LBAT_1323	dnaJ	LBAT_1323	LBAT_0714	Conserved hypothetical protein.	Chaperone protein DnaJ; 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 triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]	0.793
LBAT_1323	dnaK	LBAT_1323	LBAT_0713	Conserved hypothetical protein.	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.755
dnaJ	LBAT_0534	LBAT_0714	LBAT_0534	Chaperone protein DnaJ; 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 triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]	Thioredoxin.	0.787
dnaJ	LBAT_1323	LBAT_0714	LBAT_1323	Chaperone protein DnaJ; 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 triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]	Conserved hypothetical protein.	0.793
dnaJ	dnaK	LBAT_0714	LBAT_0713	Chaperone protein DnaJ; 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 triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.999

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