{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"D3RPC0","uniProtkbId":"TUSA_ALLVD","entryAudit":{"firstPublicDate":"2017-03-15","lastAnnotationUpdateDate":"2025-04-09","lastSequenceUpdateDate":"2010-04-20","entryVersion":68,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)","commonName":"Chromatium vinosum","taxonId":572477,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Chromatiales","Chromatiaceae","Allochromatium"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24648525"}],"value":"Sulfur carrier protein TusA"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24648525"}],"value":"tusA"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ADC63510.1"}],"value":"Alvin_2600"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24648525"},{"evidenceCode":"ECO:0000305"}],"value":"Sulfur carrier protein involved in sulfur trafficking for oxidative dissimilatory sulfur metabolism. Component of a sulfur relay system that starts with the sulfur-mobilizing rhodanese-like protein Rhd_2599 (Alvin_2599), which transfers the sulfur from a low-molecular-weight thiol, maybe glutathione, to the TusA protein (Alvin_2600); TusA serves as the sulfur donor for DsrEFH, which persulfurates DsrC; persulfurated DsrC very probably serves as a direct substrate for reverse-acting sulfite reductase, DsrAB. TusA seems to be not exclusively dedicated to sulfur oxidation and may have other important roles in the cell. Might also act as a sulfur mediator required for 2-thiouridine formation of tRNA"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24648525"}],"value":"Energy metabolism; sulfur metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24648525"}],"value":"Mostly a monomer, a small portion forms homodimer via intermolecular disulfide bonds. Tightly interacts with DsrEFH"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24648525"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24487535"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24648525"}],"value":"Up-regulated under sulfur-oxidizing conditions (at mRNA level), i.e. when grown on reduced sulfur compounds such as sulfide, thiosulfate or elemental sulfur (PubMed:24648525). TusA is one of the major proteins in A.vinosum cells grown on malate or on reduced sulfur compounds (PubMed:24487535)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24648525"}],"value":"A mutant strain lacking rhd_2599, tusA and dsrE2, although not viable in liquid culture, is clearly sulfur oxidation negative upon growth on solid media containing sulfide, and shows massive accumulation of intercellular sulfur globules"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the sulfur carrier protein TusA family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"Sulfur carrier protein TusA","featureId":"PRO_0000439098"},{"type":"Active site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Cysteine persulfide intermediate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24648525"}]},{"type":"Mutagenesis","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Loss of sulfur binding in the presence of sulfide. Loss of interaction with DsrEFH proteins.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24648525"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}}],"keywords":[{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"22675582","citationType":"journal article","authors":["Weissgerber T.","Zigann R.","Bruce D.","Chang Y.J.","Detter J.C.","Han C.","Hauser L.","Jeffries C.D.","Land M.","Munk A.C.","Tapia R.","Dahl C."],"citationCrossReferences":[{"database":"PubMed","id":"22675582"},{"database":"DOI","id":"10.4056/sigs.2335270"}],"title":"Complete genome sequence of Allochromatium vinosum DSM 180(T).","publicationDate":"2011","journal":"Stand. Genomic Sci.","firstPage":"311","lastPage":"330","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"24487535","citationType":"journal article","authors":["Weissgerber T.","Sylvester M.","Kroeninger L.","Dahl C."],"citationCrossReferences":[{"database":"PubMed","id":"24487535"},{"database":"DOI","id":"10.1128/aem.04182-13"}],"title":"A comparative quantitative proteomic study identifies new proteins relevant for sulfur oxidation in the purple sulfur bacterium Allochromatium vinosum.","publicationDate":"2014","journal":"Appl. Environ. Microbiol.","firstPage":"2279","lastPage":"2292","volume":"80"},"referencePositions":["IDENTIFICATION BY MASS SPECTROMETRY","INDUCTION"],"referenceComments":[{"value":"ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"24648525","citationType":"journal article","authors":["Stockdreher Y.","Sturm M.","Josten M.","Sahl H.G.","Dobler N.","Zigann R.","Dahl C."],"citationCrossReferences":[{"database":"PubMed","id":"24648525"},{"database":"DOI","id":"10.1074/jbc.m113.536425"}],"title":"New proteins involved in sulfur trafficking in the cytoplasm of Allochromatium vinosum.","publicationDate":"2014","journal":"J. Biol. 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