Database Retrieval System V1.0

Name ddhC
Function
May transfer electrons to the iron-sulfur centers of DdhB.
Definition dimethylsulfide dehydrogenase subunit gamma.
AA seq
MPGFRFLLAATAAFLATSPALPLSADSLNAGNIRLVDPEETVPVIKIPDGIYLRTPNDPD DIIWARVPEFRVEMVMAPPVHPSVGLRYRDEYPEQDLVVQLARTSERFYVRLRWVDPTRD MSTLRDRFRDGAAIEFSESDDSVSYMMGTDAESPVNIWYWHPDGDRVESLAAGSPGSLTR LDRQPVTGASEYRTGHGPDDSQWIVVMSRPLASEGDHQVSFERDTIPVAFALWQGADAQR DGLKLVSLNWIFARMTPDAAPAPGN 270
Structure
Reference
PMIDTitle & AuthorAbstractYear
016820499Alteration of the rugose phenotype in waaG and ddhC mutants of Salmonella enterica serovar Typhimurium DT104 is associated with inverse production of curli and cellulose. Yuda Anriany , Surashri N Sahu, Kimberly R Wessels, Lindsay M McCann, Sam W JosephThe rugose (also known as wrinkled or rdar) phenotype in Salmonella enterica serovar Typhimurium DT104 Rv has been associated with cell aggregation and the ability, at low temperature under low-osmolarity conditions, to form pellicles and biofilms. Two Tn5 insertion mutations in genes that are involved in lipopolysaccharide (LPS) synthesis, ddhC (A1-8) and waaG (A1-9), of Rv resulted in diminished expression of colony rugosity. Scanning electron micrographs revealed that the ddhC mutant showed reduced amounts of extracellular matrix, while there was relatively more, profuse matrix production in the waaG mutant, compared to Rv. Both mutants appeared to produce decreased levels of curli, as judged by Western blot assays probed with anti-AgfA (curli) antibodies but, surprisingly, were observed to have increased amounts of cellulose relative to Rv. Comparison with a non-curli-producing mutant suggested that the alteration in curli production may have engendered the increased presence of cellulose. While both mutants had impaired biofilm formation when grown in rich medium with low osmolarity, they constitutively formed larger amounts of biofilms when the growth medium was supplemented with either glucose or a combination of glucose and NaCl. These observations indicated that LPS alterations may have opposing effects on biofilm formation in these mutants, depending upon either the presence or the absence of these osmolytes. The phenotypes of the waaG mutant were further confirmed in a constructed, nonpolar deletion mutant of S. enterica serovar Typhimurium LT2, where restoration to the wild-type phenotypes was accomplished by complementation. These results highlight the importance of an integral LPS, at both the O-antigen and core polysaccharide levels, in the modulation of curli protein and cellulose production, as well as in biofilm formation, thereby adding another potential component to the complex regulatory system which governs multicellular behaviors in S. enterica serovar Typhimurium.2006
112957948A gene cluster for chlorate metabolism in Ideonella dechloratans. Helena Danielsson Thorell , Katarina Stenklo, Jan Karlsson, Thomas NilssonChlorate reductase has been isolated from the chlorate-respiring bacterium Ideonella dechloratans, and the genes encoding the enzyme have been sequenced. The enzyme is composed of three different subunits and contains molybdopterin, iron, probably in iron-sulfur clusters, and heme b. The genes (clr) encoding chlorate reductase are arranged as clrABDC, where clrA, clrB, and clrC encode the subunits and clrD encodes a specific chaperone. Judging from the subunit composition, cofactor content, and sequence comparisons, chlorate reductase belongs to class II of the dimethyl sulfoxide reductase family. The clr genes are preceded by a novel insertion sequence (transposase gene surrounded by inverted repeats), denoted ISIde1. Further upstream, we find the previously characterized gene for chlorite dismutase (cld), oriented in the opposite direction. Chlorate metabolism in I. dechloratans starts with the reduction of chlorate, which is followed by the decomposition of the resulting chlorite to chloride and molecular oxygen. The present work reveals that the genes encoding the enzymes catalyzing both these reactions are in close proximity.2003

Thorell H D , Stenklo K , Karlsson J , et al. A gene cluster for chlorate metabolism in Ideonella dechloratans[J]. Applied & Environmental Microbiology, 2003, 69(9):5585.