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Copper resistance protein ScsC N-terminal domain
This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (Pfam:PF13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity [1]. [1]. 28722010. A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance. Furlong EJ, Lo AW, Kurth F, Premkumar L, Totsika M, Achard MES, Halili MA, Heras B, Whitten AE, Choudhury HG, Schembri MA, Martin JL;. Nat Commun. 2017;8:16065. (from Pfam)
thioredoxin domain-containing protein
DsbA family protein
This family contains a diverse set of proteins with a thioredoxin-like structure Pfam:PF00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyse one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways [2,3,4]. This family also contains members with functions other than HCCA isomerisation, such as Kappa family GSTs (e.g. Swiss:P24473), whose similarity to HCCA isomerases was not previously recognised. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme (see [5]). [1]. 9149147. Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. Hu SH, Peek JA, Rattigan E, Taylor RK, Martin JL;. J Mol Biol 1997;268:137-146. [2]. 8226631. Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway. Denome SA, Stanley DC, Olson ES, Young KD;. J Bacteriol 1993;175:6890-6901. [3]. 8002605. Organization and evolution of naphthalene catabolic pathways: sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from the NAH7 plasmid. Eaton RW;. J Bacteriol 1994;176:7757-7762. [4]. 9882667. The phn genes of Burkholderia sp. strain RP007 constitute a dive. TRUNCATED at 1650 bytes (from Pfam)
DsbA family protein such as Proteus mirabilis suppressor of copper sensitivity protein C ScaC (PmScsC), a homotrimeric disulfide isomerase that plays a role in copper tolerance
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