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May also import phenylalanine (PubMed:29867812)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"29867812"}],"value":"The complex is probably composed of two ATP-binding proteins (CDR20291_0806), two transmembrane proteins (CDR20291_0807) and a solute-binding protein (CDR20291_0805)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}],"value":"Lipid-anchor","id":"SL-9901"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29867812"}],"value":"C.difficile isolates lacking CDR20291_0805 and CDR20291_0806 show reduced uptake of tyrosine (PubMed:29867812). Production of the tyrosine catabolic end product p-cresol is decreased by sixfold, and the intermediate fermentation product (4-hydroxyphenyl)acetate is not detectable at all (PubMed:29867812)"}],"commentType":"DISRUPTION PHENOTYPE"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Tyrosine-binding protein","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_0000458887"},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"id":"KW-0029","category":"Biological process","name":"Amino-acid transport"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0564","category":"PTM","name":"Palmitate"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"19781061","citationType":"journal article","authors":["Stabler R.A.","He M.","Dawson L.","Martin M.","Valiente E.","Corton C.","Lawley T.D.","Sebaihia M.","Quail M.A.","Rose G.","Gerding D.N.","Gibert M.","Popoff M.R.","Parkhill J.","Dougan G.","Wren B.W."],"citationCrossReferences":[{"database":"PubMed","id":"19781061"},{"database":"DOI","id":"10.1186/gb-2009-10-9-r102"}],"title":"Comparative genome and phenotypic analysis of Clostridium difficile 027 strains provides insight into the evolution of a hypervirulent bacterium.","publicationDate":"2009","journal":"Genome Biol.","firstPage":"R102.1","lastPage":"R102.15","volume":"10"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"R20291","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"29867812","citationType":"journal article","authors":["Steglich M.","Hofmann J.D.","Helmecke J.","Sikorski J.","Sproeer C.","Riedel T.","Bunk B.","Overmann J.","Neumann-Schaal M.","Nuebel U."],"citationCrossReferences":[{"database":"PubMed","id":"29867812"},{"database":"DOI","id":"10.3389/fmicb.2018.00901"}],"title":"Convergent loss of ABC transporter genes from Clostridioides difficile genomes is associated with impaired tyrosine uptake and p-cresol production.","publicationDate":"2018","journal":"Front. 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