CHPD_STRCO
ID CHPD_STRCO Reviewed; 75 AA.
AC Q9L1J9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Chaplin-D {ECO:0000303|PubMed:12832396};
DE Flags: Precursor;
GN Name=chpD {ECO:0000303|PubMed:12832396}; OrderedLocusNames=SCO2717;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, AMYLOID FORMATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP INDUCTION, MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12832396; DOI=10.1101/gad.264303;
RA Claessen D., Rink R., de Jong W., Siebring J., de Vreugd P., Boersma F.G.,
RA Dijkhuizen L., Wosten H.A.;
RT "A novel class of secreted hydrophobic proteins is involved in aerial
RT hyphae formation in Streptomyces coelicolor by forming amyloid-like
RT fibrils.";
RL Genes Dev. 17:1714-1726(2003).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, MASS SPECTROMETRY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=A3(2) / M600;
RX PubMed=12832397; DOI=10.1101/gad.264403;
RA Elliot M.A., Karoonuthaisiri N., Huang J., Bibb M.J., Cohen S.N., Kao C.M.,
RA Buttner M.J.;
RT "The chaplins: a family of hydrophobic cell-surface proteins involved in
RT aerial mycelium formation in Streptomyces coelicolor.";
RL Genes Dev. 17:1727-1740(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=15228525; DOI=10.1111/j.1365-2958.2004.04143.x;
RA Claessen D., Stokroos I., Deelstra H.J., Penninga N.A., Bormann C.,
RA Salas J.A., Dijkhuizen L., Woesten H.A.;
RT "The formation of the rodlet layer of streptomycetes is the result of the
RT interplay between rodlins and chaplins.";
RL Mol. Microbiol. 53:433-443(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=A3(2) / M600;
RX PubMed=17462011; DOI=10.1111/j.1365-2958.2007.05674.x;
RA Capstick D.S., Willey J.M., Buttner M.J., Elliot M.A.;
RT "SapB and the chaplins: connections between morphogenetic proteins in
RT Streptomyces coelicolor.";
RL Mol. Microbiol. 64:602-613(2007).
RN [6]
RP FUNCTION, AND CREATION OF A MINIMAL CHAPLIN STRAIN.
RC STRAIN=A3(2) / M600;
RX PubMed=18586935; DOI=10.1128/jb.00685-08;
RA Di Berardo C., Capstick D.S., Bibb M.J., Findlay K.C., Buttner M.J.,
RA Elliot M.A.;
RT "Function and redundancy of the chaplin cell surface proteins in aerial
RT hypha formation, rodlet assembly, and viability in Streptomyces
RT coelicolor.";
RL J. Bacteriol. 190:5879-5889(2008).
RN [7]
RP FUNCTION IN GROWTH SUBSTRATE ATTACHMENT, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=19682261; DOI=10.1111/j.1365-2958.2009.06838.x;
RA de Jong W., Woesten H.A., Dijkhuizen L., Claessen D.;
RT "Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae
RT that are anchored to the cell surface via cellulose.";
RL Mol. Microbiol. 73:1128-1140(2009).
RN [8]
RP FUNCTION, AND AMYLOID FORMATION.
RX PubMed=21526199; DOI=10.1371/journal.pone.0018839;
RA Sawyer E.B., Claessen D., Haas M., Hurgobin B., Gras S.L.;
RT "The assembly of individual chaplin peptides from Streptomyces coelicolor
RT into functional amyloid fibrils.";
RL PLoS ONE 6:E18839-E18839(2011).
RN [9]
RP FUNCTION, AND AMYLOID FORMATION.
RX PubMed=24012833; DOI=10.1016/j.jsb.2013.08.013;
RA Bokhove M., Claessen D., de Jong W., Dijkhuizen L., Boekema E.J.,
RA Oostergetel G.T.;
RT "Chaplins of Streptomyces coelicolor self-assemble into two distinct
RT functional amyloids.";
RL J. Struct. Biol. 184:301-309(2013).
RN [10]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=24413917; DOI=10.1007/s00253-013-5463-z;
RA Ekkers D.M., Claessen D., Galli F., Stamhuis E.;
RT "Surface modification using interfacial assembly of the Streptomyces
RT chaplin proteins.";
RL Appl. Microbiol. Biotechnol. 98:4491-4501(2014).
CC -!- FUNCTION: One of 8 partially redundant surface-active proteins required
CC for efficient formation of aerial mycelium; the short chaplins assemble
CC into a hydrophobic, amyloidal fibrillar surface layer that envelopes
CC and protects aerial hyphae and spores, presumably anchored to the long
CC chaplins (PubMed:12832396, PubMed:12832397, PubMed:15228525,
CC PubMed:17462011). Chaplins have an overlapping function with the
CC surface-active SapB peptide; chaplins are essential on minimal medium
CC while on rich medium both chaplins and SapB are required for efficient
CC aerial hyphae formation (PubMed:17462011). Chaplins are also involved
CC in cell attachment to a hydrophobic surface (PubMed:19682261). Forms
CC amyloid fibrils in vitro probably composed of stacked beta-sheets, at
CC low extracellular concentrations individually restores the ability to
CC form aerial hyphae to a chaplin-deficient strain (PubMed:21526199). A
CC small chaplin extract (ChpD, ChpE, ChpF, ChpG and ChpH) self-assembles
CC into 2 different amyloids; small fibrils at the air-water interface
CC form an amphipathic membrane that resembles spore-surface structures
CC involved in aerial hyphae formation, and hydrophilic fibrils in
CC solution that resemble the fibers that attach cells to a hydrophobic
CC surface. At the air-water interface the hydrophilic surface is in
CC contact with water (probably equivalent to the peptidoglycan layer),
CC while the hydrophobic face is exposed to the air, making the surface of
CC the aerial hyphae hydrophobic (PubMed:24012833). A minimal chaplin
CC strain capable of forming aerial mycelium/hyphae on minimal medium
CC contains ChpC, ChpE and ChpH. The strain also has restored rodlet
CC formation on the hyphae surface. A second minimal chaplin strain with
CC ChpA, ChpD and ChpE makes slightly less robust hyphae
CC (PubMed:18586935). A small chaplin extract applied to a chaplin-
CC deficient strain restores aerial hyphae formation (PubMed:12832396,
CC PubMed:12832397). The small chaplin extract forms an amyloid-like
CC structure similar to that seen on the surface of cells without rodlets
CC (rdlA-rdlB deletions), and is highly surface active, reducing surface
CC tension from 72 to 26 mJ/m(2), which probably allows escape of hyphae
CC from an aqueous environment into air (PubMed:12832396).
CC {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397,
CC ECO:0000269|PubMed:15228525, ECO:0000269|PubMed:17462011,
CC ECO:0000269|PubMed:18586935, ECO:0000269|PubMed:19682261,
CC ECO:0000269|PubMed:21526199, ECO:0000269|PubMed:24012833}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:12832396,
CC ECO:0000269|PubMed:12832397, ECO:0000305|PubMed:17462011}. Secreted,
CC cell wall {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397}.
CC Fimbrium {ECO:0000269|PubMed:19682261}.
CC -!- DEVELOPMENTAL STAGE: Present in aerial hyphae of sporulating cultures;
CC it is probably directly underneath the rodlet layer formed by RdlA and
CC RdlB (at protein level). {ECO:0000269|PubMed:12832396,
CC ECO:0000305|PubMed:17462011}.
CC -!- INDUCTION: Not expressed while still submerged, accumulates during
CC aerial hyphae formation on minimal medium, no transcript detected
CC during sporulation (Probable). During aerial hyphae formation and early
CC sporulation on rich medium, under control of ECF sigma factor BldN
CC (PubMed:12832397). Expression depends on bldB but not bldA, bldD or
CC bldH (at protein level) (PubMed:17462011).
CC {ECO:0000269|PubMed:12832397, ECO:0000269|PubMed:17462011,
CC ECO:0000305|PubMed:12832396}.
CC -!- MASS SPECTROMETRY: Mass=5071; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12832396};
CC -!- MASS SPECTROMETRY: Mass=5066.49; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12832397};
CC -!- DISRUPTION PHENOTYPE: A double chpA-chpD knockout has no phenotype; a
CC quadruple chpA-chpC-chpD-chpH knockout has delayed aerial hyphae
CC formation and sporulation. A quintuple chpA-chpB-chpC-chpD-chpH
CC knockout has a longer delay in aerial hyphae formation and an almost
CC complete lack of sporulation. The quintuple knockout still expresses
CC ChpE, ChpEF and ChpG (PubMed:12832397). Quintuple knockout chpA-chpB-
CC chpC-chpD-chpH has strongly delayed aerial hyphae formation, makes many
CC fewer aerial hyphae but no effect on viability of the spores produced.
CC Further deletion of chpE leads to more severe effects, and on rich
CC media few aerial hyphae are produced after prolonged growth. Those few
CC hyphae do differentiate into spores and have a rodlet layer
CC (PubMed:12832396). Deletion of all 8 chaplin genes on minimal medium
CC leads to severely disrupted aerial hyphae that collapse on the colony
CC surface and are not hydrophobic on minimal medium. A few spore chains
CC can still be made, but they have neither rodlets or amyloid-like
CC fibers. rdlA and rdlB mRNA are down-regulated (PubMed:15228525,
CC PubMed:17462011). Deletion of all 8 chaplin genes on rich medium leads
CC to a reduced abundance of aerial hyphae without rodlets and occasional
CC spore chains on surface hyphae. A complete chaplin-negative plus ram-
CC negative strain (deletion of ramR or the ramC-ramS-ramA-ramB operon)
CC leads to the complete loss of robust aerial hyphae (PubMed:17462011).
CC Deletion of all 8 chaplin genes significantly reduces cellular
CC attachment to a hydrophobic substrate; thin fibrils instead of fimbrae
CC are detected. The long chaplins (ChpA, ChpB and ChpC, as seen by near
CC wild-type attachment of the hextuple chpA-chpB-chpC-chpD-chpE-chpH
CC knockout) are not essential but may contribute to attachment
CC (PubMed:19682261). {ECO:0000269|PubMed:12832396,
CC ECO:0000269|PubMed:12832397, ECO:0000269|PubMed:15228525,
CC ECO:0000269|PubMed:17462011, ECO:0000269|PubMed:19682261}.
CC -!- BIOTECHNOLOGY: The small chaplin mixture (a cell wall extract of an
CC rdlA-rdlB knockout) forms a stable coat on a number of surfaces
CC (including Teflon and cotton) and emulsifies oil-water mixtures, which
CC could be useful in medical and technical applications.
CC {ECO:0000269|PubMed:24413917}.
CC -!- SIMILARITY: Belongs to the chaplin family. Short chaplin subfamily.
CC {ECO:0000305|PubMed:12832397}.
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DR EMBL; AL939113; CAB75306.1; -; Genomic_DNA.
DR RefSeq; NP_626950.1; NC_003888.3.
DR RefSeq; WP_011028536.1; NZ_VNID01000020.1.
DR AlphaFoldDB; Q9L1J9; -.
DR STRING; 100226.SCO2717; -.
DR DNASU; 1098151; -.
DR GeneID; 1098151; -.
DR KEGG; sco:SCO2717; -.
DR PATRIC; fig|100226.15.peg.2772; -.
DR eggNOG; ENOG50348JU; Bacteria.
DR HOGENOM; CLU_145456_3_1_11; -.
DR OMA; HVPINAC; -.
DR PhylomeDB; Q9L1J9; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR005528; ChpA-H.
DR Pfam; PF03777; ChpA-C; 1.
DR PROSITE; PS51884; CHAPLIN; 1.
PE 1: Evidence at protein level;
KW Amyloid; Cell adhesion; Cell wall; Disulfide bond; Fimbrium;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:12832396,
FT ECO:0000269|PubMed:12832397"
FT CHAIN 24..75
FT /note="Chaplin-D"
FT /id="PRO_5004329893"
FT DOMAIN 34..74
FT /note="Chaplin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT DISULFID 54..72
FT /evidence="ECO:0000305|PubMed:12832397"
SQ SEQUENCE 75 AA; 7230 MW; 6C7F7D3C0116D9D9 CRC64;
MKKSAAVVAG AIMALGMAAP AFADAGAEGA AVGSPGVLSG NVIQVPVHVP VNVCGNSINV
VGLLNPAFGN KCEND
