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Dsba-like thioredoxin domain

WebThe formation of disulphide bonds is an essential step in the folding of many proteins that enter the secretory pathway; therefore, it is not surprising that eukaryotic and prokaryotic organisms have dedicated enzymatic systems to catalyse this process. In bacteria, one such enzyme is disulphide bond-forming protein A (DsbA), a thioredoxin-like thiol oxidase … WebDsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in ...

UniProt

WebDomain: IPR001853: DSBA-like thioredoxin domain: Family: IPR014371: Sterol O-acyltransferase, ACAT/DAG/ARE types: Family: IPR014440: HCCA isomerase/glutathione S-transferase kappa: Homologous_superfamily: IPR036249: Thioredoxin-like superfamily: Domain Details Per Protein . Protein Length WebMar 8, 2024 · The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox … bp systolic over diastolic https://paradiseusafashion.com

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WebDSBA-like thioredoxin domain Provide feedback. This family contains a diverse set of proteins with a thioredoxin-like structure 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]. ... WebDSBA-like thioredoxin domain (DSBA) DSBA-like thioredoxin domain: This family contains a diverse set of proteins with a thioredoxin-like structure Pfam:PF00085. This … WebMar 16, 2024 · They contain a CXXC motif in a DsbA-like thioredoxin domain. FrnE homologs are present in many bacteria, and many possess an additional conserved CXXXXC motif at the C-terminus. The name frnE was given for the first time to a gene present in a gene cluster ( frnA to frnU ) associated with the biosynthesis of the … bpt06wtb

NCBI Conserved Domain Search

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Dsba-like thioredoxin domain

NCBI Conserved Domain Search

WebDsbA_GSTK domain-containing protein (domain architecture ID 10122488) DsbA_GSTK domain-containing protein. Graphical summary. Zoom to residue level ... Refine search. List of domain hits. Name: Accession: Description: Interval: E-value: DsbA_GSTK: cd03021: DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a … WebDownload scientific diagram Thioredoxin-like, DsbA-like and redox domains in the ER from publication: Calnexin cycle ‐ structural features of the ER chaperone system The endoplasmic ...

Dsba-like thioredoxin domain

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WebDsbA introduces disulfide bonds into folding proteins, and is re-oxidized through interaction with its redox partner DsbB. Mycobacterium tuberculosis, a Gram-positive bacterium, … WebInterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

WebDec 6, 2005 · DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more … WebOct 18, 2013 · The X-ray crystal structure of Mt-DsbA reveals a two-domain structure, comprising a canonical thioredoxin domain with the conserved CXXC active site …

WebSep 1, 2024 · Aims: DsbA catalyzes disulfide bond formation in secreted and outer membrane proteins in bacteria. In pathogens, DsbA is a major facilitator of virulence … WebMar 1, 2016 · DsbA harbors a canonical thioredoxin-like fold that is characterized by an N-terminal βαβ motif and a C-terminal ββα motif . However, unlike thioredoxin, these motifs are separated by an extended α-helical domain. The DsbA active site is composed of a reactive disulfide bond found in a CXXC ...

WebDsbA (EC 1.8.4.15) introduces protein disulfide bonds in the periplasm and transfers the electrons via DsbB (EC 1.8.5.9) to ubiquinone and menaquinone. DsbA has a CPHC …

WebGene ID: 103641494, discontinued on 13-May-2024 Summary DISCONTINUED: This record has been withdrawn by NCBI staff. This record represented a gene that is not currently annotated by NCBI. Other designations DSBA-like thioredoxin domain containing protein gynecologist pooler gaWebIPR001853 DSBA-like_thioredoxin_dom IPR023205 DsbA/DsbL IPR036249 Thioredoxin-like_sf IPR017937 Thioredoxin_CS IPR013766 Thioredoxin_domain PIRSF PIRSF001488 Tdi_protein 1 hit PROSITE View protein in PROSITE PS00194 THIOREDOXIN_1 1 hit PS51352 THIOREDOXIN_2 1 hit Pfam View protein in Pfam … gynecologist pngWebDomain: 20-150: Thioredoxin PROSITE-ProRule annotation. BLAST Add. ... IPR001853 DSBA-like_thioredoxin_dom; IPR023205 DsbA/DsbL; IPR036249 Thioredoxin-like_sf; IPR017937 Thioredoxin_CS; IPR013766 Thioredoxin_domain; PANTHER. PTHR35891 THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA 1 hit; bpt10-34s40WebDsbA family protein (domain architecture ID 10122501) ... DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and ... bpt08wtbWebSep 29, 2024 · DSBA-like thioredoxin domain. This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in … bpt10-23h25-aWebThe thiol/disulfide oxidoreductase DsbA is the strongest oxidant of the thioredoxin superfamily and is required for efficient disulfide bond formation in the periplasm of Escherichia coli. bp sys and diagynecologist pmb