{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9KYG7","uniProtkbId":"CHPF_STRCO","entryAudit":{"firstPublicDate":"2018-10-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2000-10-01","entryVersion":81,"sequenceVersion":1},"annotationScore":5.0,"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-F"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12832397"}],"value":"Chaplin-G"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12832396"}],"value":"chpF"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12832397"}],"value":"chpG"}],"orderedLocusNames":[{"value":"SCO2705"}]}],"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":"19682261"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21526199"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24012833"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28925983"}],"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). Chaplins are also involved in cell attachment to a hydrophobic surface (PubMed:19682261). Forms amyloid fibrils in vitro probably composed of stacked beta-sheets, at low extracellular concentrations individually restores the ability to form aerial hyphae to a chaplin-deficient strain (PubMed:21526199). A small chaplin extract (ChpD, ChpE, ChpF, ChpG and ChpH) self-assembles into 2 different amyloids; small fibrils at the air-water interface form an amphipathic membrane that resembles spore-surface structures involved in aerial hyphae formation, and hydrophilic fibrils in solution that resemble the fibers that attach cells to a hydrophobic surface. At the air-water interface the hydrophilic surface is in contact with water (probably equivalent to the peptidoglycan layer), while the hydrophobic face is exposed to the air, making the surface of the aerial hyphae hydrophobic (PubMed:24012833). A small chaplin extract applied to a chaplin-deficient strain restores aerial hyphae formation (PubMed:12832396, PubMed:12832397). The small chaplin extract forms an amyloid-like structure similar to that seen on the surface of cells without rodlets (rdlA-rdlB deletions), and is highly surface active, reducing surface tension from 72 to 26 mJ/m(2), which probably allows escape of hyphae from an aqueous environment into air (PubMed:12832396). ChpF alone is less surface active at pH 3.0 than at pH 10.0, it reduces the surface tension of water from 72.8 mN/m to 50 mN/m at pH 3.0 or to 37 mN/m at pH 10.0 (PubMed:28925983). ChpF and ChpG are sufficient to restore the rodlet layer and hydrophobicity to a strain deleted for the other 6 chaplin genes (PubMed:15228525)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21526199"}],"value":"Homodimer; disulfide linked. About 20% of ChpF isolated from cell wall forms disulfide-bonded homodimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19682261"}],"value":"Considerably more ChpF is seen in fimbrae than in aerial hyphae"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832397"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17462011"}],"value":"Cell surface","id":"SL-0310"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21526199"}],"value":"Secreted, cell wall","id":"SL-0041"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19682261"}],"value":"Fimbrium","id":"SL-0113"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832396"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17462011"}],"value":"Present in aerial hyphae of sporulating cultures (at protein level)"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17462011"}],"value":"Not expressed while still submerged, accumulates during aerial hyphae formation on minimal medium, no transcript detected during sporulation (PubMed:12832396). During aerial hyphae formation and early sporulation on rich medium, under control of ECF sigma factor BldN (PubMed:12832397). Expression depends on bldB but not bldA, bldD or bldH (at protein level) (PubMed:17462011)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28925983"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21526199"}],"value":"The mature protein rapidly forms a predominantly amyloid fibril beta-sheet structure at pH 3.0 and 4.2, with less beta-sheet and more random coil at pH 10 (Probable) (PubMed:28925983). Reduced and non-reduced peptide have the same secondary structures at all pH tested, suggesting the disulfide bond is not required for fibril formation (PubMed:28925983)"}],"commentType":"DOMAIN"},{"commentType":"MASS SPECTROMETRY","method":"MALDI","molWeight":5182.0,"molWeightError":0.0,"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832396"}]},{"commentType":"MASS SPECTROMETRY","method":"MALDI","molWeight":5177.48,"molWeightError":0.0,"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832397"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15228525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17462011"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19682261"}],"value":"A strain deleted of chpF and chpG makes rodlets (PubMed:15228525). 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 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 attachment (PubMed:19682261)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24413917"}],"value":"The small chaplin mixture (a cell wall extract of an rdlA-rdlB knockout) forms a stable coat on a number of surfaces (including Teflon and cotton) and emulsifies oil-water mixtures, which could be useful in medical and technical applications"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12832397"}],"value":"Belongs to the chaplin family. Short chaplin subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832397"}]},{"type":"Chain","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Chaplin-F","featureId":"PRO_5004329169"},{"type":"Domain","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Chaplin","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01232"}]},{"type":"Disulfide bond","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12832397"}]}],"keywords":[{"id":"KW-0034","category":"Cellular component","name":"Amyloid"},{"id":"KW-0130","category":"Biological process","name":"Cell adhesion"},{"id":"KW-0134","category":"Cellular component","name":"Cell wall"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0281","category":"Cellular component","name":"Fimbrium"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"12000953","citationType":"journal article","authors":["Bentley S.D.","Chater K.F.","Cerdeno-Tarraga A.-M.","Challis G.L.","Thomson N.R.","James K.D.","Harris D.E.","Quail M.A.","Kieser H.","Harper D.","Bateman A.","Brown S.","Chandra G.","Chen C.W.","Collins M.","Cronin A.","Fraser A.","Goble A.","Hidalgo J.","Hornsby T.","Howarth S.","Huang C.-H.","Kieser T.","Larke L.","Murphy L.D.","Oliver K.","O'Neil S.","Rabbinowitsch E.","Rajandream M.A.","Rutherford K.M.","Rutter S.","Seeger K.","Saunders D.","Sharp S.","Squares R.","Squares S.","Taylor K.","Warren T.","Wietzorrek A.","Woodward J.R.","Barrell B.G.","Parkhill J.","Hopwood D.A."],"citationCrossReferences":[{"database":"PubMed","id":"12000953"},{"database":"DOI","id":"10.1038/417141a"}],"title":"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2).","publicationDate":"2002","journal":"Nature","firstPage":"141","lastPage":"147","volume":"417"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC BAA-471 / A3(2) / M145","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"12832396","citationType":"journal article","authors":["Claessen D.","Rink R.","de Jong W.","Siebring J.","de Vreugd P.","Boersma F.G.","Dijkhuizen L.","Wosten H.A."],"citationCrossReferences":[{"database":"PubMed","id":"12832396"},{"database":"DOI","id":"10.1101/gad.264303"}],"title":"A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils.","publicationDate":"2003","journal":"Genes Dev.","firstPage":"1714","lastPage":"1726","volume":"17"},"referencePositions":["FUNCTION","AMYLOID FORMATION","SUBCELLULAR LOCATION","DEVELOPMENTAL STAGE","INDUCTION","MASS SPECTROMETRY"],"referenceComments":[{"value":"ATCC BAA-471 / A3(2) / M145","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"12832397","citationType":"journal article","authors":["Elliot M.A.","Karoonuthaisiri N.","Huang J.","Bibb M.J.","Cohen S.N.","Kao C.M.","Buttner M.J."],"citationCrossReferences":[{"database":"PubMed","id":"12832397"},{"database":"DOI","id":"10.1101/gad.264403"}],"title":"The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor.","publicationDate":"2003","journal":"Genes Dev.","firstPage":"1727","lastPage":"1740","volume":"17"},"referencePositions":["FUNCTION","SUBCELLULAR LOCATION","INDUCTION","MASS SPECTROMETRY"],"referenceComments":[{"value":"A3(2) / M600","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"15228525","citationType":"journal article","authors":["Claessen D.","Stokroos I.","Deelstra H.J.","Penninga N.A.","Bormann C.","Salas J.A.","Dijkhuizen L.","Woesten H.A."],"citationCrossReferences":[{"database":"PubMed","id":"15228525"},{"database":"DOI","id":"10.1111/j.1365-2958.2004.04143.x"}],"title":"The formation of the rodlet layer of streptomycetes is the result of the interplay between rodlins and chaplins.","publicationDate":"2004","journal":"Mol. 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