Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
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nDsbD reduces CcmG by fast, direct disulfide exchange; crystal structure of the disulfide-linked nDsbD-CcmG complex.
"we demonstrate fast (3.9 x 10(5) M(-1)s(-1)) and direct disulfide exchange between nDsbD and CcmG"
Membranome: a database for proteome-wide analysis of single-pass membrane proteins.
The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo.
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CcmG is membrane bound with a periplasmic C-terminal domain; deletion abolishes c-type cytochromes; thiol rescue of active-site mutants supports a reducing function.
"which is in agreement with a reducing function for CcmG"
The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly.
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CcmG oxidized form accumulates in dsbD/trxA and ccmF/ccmH mutants; chemical reductant does not bypass ccmG loss.
"The data support a model proposed by others in which CcmG catalyses one of the last reactions specific to cytochrome c assembly."
Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant.
Structural and redox properties of the leaderless DsbE (CcmG) protein: both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm.
The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochrome c maturation.
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R. capsulatus CcmG reduces apocytochrome disulfides and resolves CcmH-apocytochrome mixed disulfides.
"CcmG can efficiently reduce the disulfide bond of apocytochrome c and also resolve a mixed disulfide bond"
UniProtKB entry for E. coli DsbE/CcmG (P0AA86)
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Curated function (late reductive step of cytochrome c assembly, kept reduced by DsbD), inner-membrane location with periplasmic domain, DsbE subfamily of thioredoxins.