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In response to oxidative stress, interacts with the ECF sigma factor SigH and, in conjunction with SigH, binds to an auxiliary promoter upstream of mec-cysO-cysM, leading to the transcriptional activation of these genes encoding a non-canonical actinomycete-specific cysteine biosynthesis pathway (PubMed:34018220). Increased transcription of mec-cysO-cysM results in enhanced production of L-cysteine and cysteine-derived antioxidant molecules (PubMed:34018220). Increased production of cysteine protects mycobacteria cells from host phagocyte-derived oxidative and nitrosative stress, thus facilitating the mycobacterial growth in the host (PubMed:34018220)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34018220"}],"value":"Activity is modulated by the formation of a disulfide bound within the N-terminal Cys-X-X-X-Cys (CXXXC) motif (PubMed:34018220). This intramolecular disulfide bond is formed in response to oxidative stress, and results in oxidative stress-dependent interaction with the sigma factor SigH (PubMed:34018220)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34018220"}],"value":"Homodimer (PubMed:34018220). Under oxidative stress, interacts with the extracytoplasmic-function (ECF) RNA polymerase sigma factor SigH (PubMed:34018220)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34018220"}],"value":"Deletion mutant shows no growth difference in vitro in nutrient rich or limiting media, but its survival is compromised within peritoneal macrophages at day 4 post-infection (PubMed:34018220). Mutant shows a marginal decrease in the survival upon exposure to nitrosative stress and markedly compromised survival upon exposure to peroxide radicals (PubMed:34018220). Failure of the mutant to up-regulate cysteine biosynthesis during oxidative stress generates a domino effect, causing differential expression of 6% of M.tuberculosis genes, resulting in attenuated survival (PubMed:34018220)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the AosR family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Oxidative stress regulator AosR","featureId":"PRO_0000103805"},{"type":"Motif","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"CXXXC","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34018220"}]},{"type":"Disulfide bond","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"Redox-active","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34018220"}]},{"type":"Mutagenesis","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"Forms dimers independent of the oxidizing nature of the environment, but cannot interact with SigH and cannot rescue the growth defects of the deletion mutant; when associated with A-9.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34018220"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"Forms dimers independent of the oxidizing nature of the environment, but cannot interact with SigH and cannot rescue the growth defects of the deletion mutant; when associated with A-5.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34018220"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}}],"keywords":[{"id":"KW-0010","category":"Molecular function","name":"Activator"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0676","category":"Domain","name":"Redox-active center"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0346","category":"Biological process","name":"Stress response"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"9634230","citationType":"journal article","authors":["Cole S.T.","Brosch R.","Parkhill J.","Garnier T.","Churcher C.M.","Harris D.E.","Gordon S.V.","Eiglmeier K.","Gas S.","Barry C.E. 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