About Products Protein Database Contact

dsbG

Gene
dsbG
Protein
Thiol:disulfide interchange protein DsbG
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
256 amino acids
Function
Involved in disulfide bond formation. Functions probably as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD (By similarity).
Similarity
Belongs to the thioredoxin family. DsbC subfamily.
Mass
28.053 kDa
Sequence
MRLPRNLITLGLGLTLLNAGLATAAEELPAPIRMVQEKGARILGSFDAPDGLRGYAAEYQNQGMALYLTPDGKHVLTGHLFDAQGKDLSREPLERLVYAPLAKEMWQKMEQSAWIADGRADAPRVVYLFSDPNCPYCTMFWEQARPWVDAGKVQLRHIMVGIIREDSEAKSAALLASKDPQKALHDHEQAGKASTLKPLAKIPAAVRKQLAGNMELMESMGAAATPAIFYLNAEGRMQQQQGAPQPDQLAEILGPR

Gene
dsbG
Protein
Thiol:disulfide interchange protein DsbG
Organism
Escherichia coli O157:H7
Length
248 amino acids
Function
Involved in disulfide bond formation. Functions probably as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. In vitro, displays chaperone activity in both redox states (By similarity).
Similarity
Belongs to the thioredoxin family. DsbC subfamily.
Mass
27.496 kDa
Sequence
MLKKILLLALLPAIAFAEELPAPVKAIEKQGITIIKTFDAPGGMKGYLGKYQDMGVTIYLTPDGKHAISGYMYNEKGENLSNTLIEKEIYAPAGREMWQRMEQSHWLLDGKKDAPVIVYVFADPFCPYCKQFWQQARPWVDSGKVQLRTLLVGVIKPESPATAAAILASKDPAKTWQEYEASGGKLKLNVPANVSTEQMKVLSDNEKLMDDLGANVTPAIYYMSKENTLQQAVGLPDQKTLNIIMGNK

Gene
dsbG
Protein
Thiol:disulfide interchange protein DsbG
Organism
Escherichia coli (strain K12)
Length
248 amino acids
Function
Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.
Similarity
Belongs to the thioredoxin family. DsbC subfamily.
Mass
27.495 kDa
Sequence
MLKKILLLALLPAIAFAEELPAPVKAIEKQGITIIKTFDAPGGMKGYLGKYQDMGVTIYLTPDGKHAISGYMYNEKGENLSNTLIEKEIYAPAGREMWQRMEQSHWLLDGKKDAPVIVYVFADPFCPYCKQFWQQARPWVDSGKVQLRTLLVGVIKPESPATAAAILASKDPAKTWQQYEASGGKLKLNVPANVSTEQMKVLSDNEKLMDDLGANVTPAIYYMSKENTLQQAVGLPDQKTLNIIMGNK