{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9AD93","uniProtkbId":"CHPC_STRCO","entryAudit":{"firstPublicDate":"2018-10-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-06-01","entryVersion":90,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)","taxonId":100226,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces","Streptomyces albidoflavus group"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12832396"}],"value":"Chaplin-C"}},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12832396"}],"value":"chpC"},"orderedLocusNames":[{"value":"SCO1674"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15228525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17462011"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18586935"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19682261"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22296345"}],"value":"One of 8 partially redundant surface-active proteins required for efficient formation of aerial mycelium; the short chaplins assemble into a hydrophobic, amyloidal fibrillar surface layer that envelopes and protects aerial hyphae and spores, presumably anchored to the long chaplins (PubMed:12832396, PubMed:12832397, PubMed:15228525, PubMed:17462011). Chaplins have an overlapping function with the surface-active SapB peptide; chaplins are essential on minimal medium while on rich medium both chaplins and SapB are required for efficient aerial hyphae formation (PubMed:17462011). A minimal chaplin strain capable of forming aerial mycelium/hyphae on minimal medium contains ChpC, ChpE and ChpH. The strain also has restored rodlet formation on the hyphae surface (PubMed:18586935). The long chaplins (ChpA, ChpB, ChpC) are not absolutely necessary for short chaplin localization or rodlet formation, but probably play a role in initiating aerial hyphae development (PubMed:22296345). Chaplins are also involved in cell attachment to a hydrophobic surface (PubMed:19682261)"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22296345"}],"value":"Anchored to the cell wall by sortase SrtE2 and to a lesser extent by sortase SrtE1"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22296345"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00477"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22296345"}],"value":"Secreted, cell wall","id":"SL-0041"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00477"}],"value":"Peptidoglycan-anchor","id":"SL-9900"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832397"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12832396"}],"value":"Transcribed during aerial hyphae formation on minimal medium, about 10- to 25-fold lower expression than the short chaplins (Probable). Strongly induced during aerial hyphae formation and early sporulation on rich medium, under control of ECF sigma factor BldN (PubMed:12832397)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15228525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17462011"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19682261"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22296345"}],"value":"A single chpC disruption and double chpC-chpH knockout have no phenotype; a quadruple chpA-chpC-chpD-chpH knockout has delayed aerial hyphae formation and sporulation. A quintuple chpA-chpB-chpC-chpD-chpH knockout has a longer delay in aerial hyphae formation and an almost complete lack of sporulation. The quintuple knockout still expresses ChpE, ChpF and ChpG (PubMed:12832397). Quintuple knockout chpA-chpB-chpC-chpD-chpH has strongly delayed aerial hyphae formation, makes many fewer aerial hyphae but no effect on viability of the spores produced. Further deletion of chpE leads to more severe effects, and on rich media few aerial hyphae are produced after prolonged growth. Those few hyphae do differentiate into spores and have a rodlet layer (PubMed:12832396). Deletion of all 8 chaplin genes on minimal medium leads to severely disrupted aerial hyphae that collapse on the colony surface and are not hydrophobic. A few spore chains can still be made, but they have neither rodlets or amyloid-like fibers. rdlA and rdlB mRNA are down-regulated (PubMed:15228525, PubMed:17462011). Deletion of all 8 chaplin genes on rich medium leads to a reduced abundance of aerial hyphae without rodlets and occasional spore chains on surface hyphae. A complete chaplin-negative plus ram-negative strain (deletion of ramR or the ramC-ramS-ramA-ramB operon) leads to the complete loss of robust aerial hyphae (PubMed:17462011). Deletion of the 3 long chaplins (ChpA-ChpB-ChpC) results in a 24 hour delay in aerial hyphae formation, while rodlets are about 1.5-fold longer than wild-type (PubMed:22296345). Deletion of all 8 chaplin genes significantly reduces cellular attachment to a hydrophobic substrate; thin fibrils instead of fimbrae are detected. The long chaplins (ChpA, ChpB and ChpC, as seen by near wild-type attachment of the hextuple chpA-chpB-chpC-chpD-chpE-chpH knockout) are not essential but may contribute to cellular attachment (PubMed:19682261)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12832397"}],"value":"Belongs to the chaplin family. 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