{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O31539","uniProtkbId":"CALJ_BACSU","entryAudit":{"firstPublicDate":"2009-01-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-01-01","entryVersion":118,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Bacillus subtilis (strain 168)","taxonId":224308,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Bacillaceae","Bacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"pH-sensitive calcium channel"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24904158"}],"value":"BsYetJ"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"33208533"}],"value":"pH-dependent, voltage-gated calcium channel"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24904158"}],"value":"pH-sensitive calcium-leak channel"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"CAB12539.1"}],"value":"calJ"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9384377"}],"value":"yetJ"}],"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"CAB12539.1"}],"value":"BSU07200"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24904158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30930064"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33208533"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36948481"}],"value":"Calcium channel that probably plays a role in the regulation of calcium homeostasis (PubMed:30930064, PubMed:33208533, PubMed:36948481). Uptakes calcium ions and mediates calcium flux in proteoliposomes in a pH-dependent manner (PubMed:24904158, PubMed:30930064). When expressed in E.coli in the presence of high extracellular calcium concentrations, shows calcium-leak activity, increasing intracellular calcium concentration (PubMed:24904158). It can also mediate Ca(2+) flux from the endoplasmic reticulum (ER) when expressed in permeabilized mammalian cells (PubMed:30930064). Calcium transport activity is also detected in ER-like lipid vesicles (PubMed:36948481)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Ca(2+)(in) = Ca(2+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29671"},{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24904158"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30930064"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"36948481"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24904158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30930064"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33208533"}],"value":"The calcium-release activity is mediated by two factors: pH and transmembrane ion gradient (PubMed:33208533). It was proposed, based on an MD simulation, that the conserved aspartyl dyad (Asp-171-Asp-195) regulates Ca(2+) binding, pH sensing, and the channel pore opening and closing, and that protonation of Asp-171 probably weakens its interaction with Arg-60, facilitating the opening of the channel (PubMed:30930064). Another study using nanodiscs suggests that Asp-171 is not a pH sensor regulating the pore dynamics; instead, it is only involved in the gating of calcium ions (PubMed:33208533). When crystallized in detergents at different pH conditions, the transition between open and closed conformations is regulated by pH (PubMed:24904158). Ca(2+) binding is inhibited by Na(+), K(+), Li(+), Yb(3+) and Lu(3+), but not by Mg(2+) and Mn(2+) (PubMed:30930064)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24904158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25286840"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24904158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30930064"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33208533"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24904158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33208533"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36948481"}],"value":"BsYetJ in nanodiscs is structurally different from those crystallized in detergents (PubMed:33208533). In lipid nanodiscs, BsYetJ conformation is pH-sensitive in apo state (lacking calcium), whereas in a calcium-containing solution it is locked in an intermediate state, inert to pH changes (PubMed:33208533). When crystallized in detergents it shows a pH-sensitive conformational equilibrium between a rather flexible pore-open state seen at lower pH and a pore-closed state seen at higher pH (PubMed:24904158). BsYetJ appears to be a lipid-sensitive membrane protein: differences in membrane lipid composition lead to changes in functional sites (PubMed:36948481)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the BI1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"pH-sensitive calcium channel","featureId":"PRO_0000360560"},{"type":"Topological 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