CHPE_STRCO
ID CHPE_STRCO Reviewed; 82 AA.
AC Q9X9Z2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Chaplin-E {ECO:0000303|PubMed:12832396};
DE Flags: Precursor;
GN Name=chpE {ECO:0000303|PubMed:12832396}; OrderedLocusNames=SCO1800;
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, DEVELOPMENTAL STAGE, INDUCTION, AND MASS
RP SPECTROMETRY.
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 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, CREATION OF A MINIMAL CHAPLIN STRAIN, AND DISRUPTION PHENOTYPE.
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).
RN [11]
RP AMYLOID FORMATION, AND DOMAIN.
RX PubMed=28400129; DOI=10.1016/j.jsb.2017.04.004;
RA Dokouhaki M., Hung A., Day L., Gras S.L.;
RT "The pH-dependent assembly of chaplin E from Streptomyces coelicolor.";
RL J. Struct. Biol. 198:82-91(2017).
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, but does so less well
CC than other short chaplins (PubMed:21526199). A small chaplin extract
CC (ChpD, ChpE, ChpF, ChpG and ChpH) self-assembles into 2 different
CC amyloids; small fibrils at the air-water interface form an amphipathic
CC membrane that resembles spore-surface structures involved in aerial
CC hyphae formation, and hydrophilic fibrils in solution that resemble the
CC fibers that attach cells to a hydrophobic surface. At the air-water
CC interface the hydrophilic surface is in contact with water (probably
CC equivalent to the peptidoglycan layer), while the hydrophobic face is
CC exposed to the air, making the surface of the aerial hyphae hydrophobic
CC (PubMed:24012833). A minimal chaplin strain capable of forming aerial
CC mycelium/hyphae on minimal medium contains ChpC, ChpE and ChpH. The
CC strain also has restored rodlet formation on the hyphae surface. A
CC second strain with ChpA, ChpD and ChpE makes slightly less robust
CC hyphae. This essential chaplin may coordinate the assembly and/or
CC polymerization of the other chaplins (PubMed:18586935). A small chaplin
CC extract applied to a chaplin-deficient strain restores aerial hyphae
CC formation (PubMed:12832396, PubMed:12832397). The small chaplin extract
CC forms an amyloid-like structure similar to that seen on the surface of
CC cells without rodlets (rdlA-rdlB deletions), and is highly surface
CC active, reducing surface tension from 72 to 26 mJ/m(2), which probably
CC allows escape of hyphae from an aqueous environment into air
CC (PubMed:12832396). {ECO:0000269|PubMed:12832396,
CC ECO:0000269|PubMed:12832397, ECO:0000269|PubMed:15228525,
CC ECO:0000269|PubMed:17462011, ECO:0000269|PubMed:18586935,
CC ECO:0000269|PubMed:19682261, ECO:0000269|PubMed:21526199,
CC ECO:0000269|PubMed:24012833}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:12832396,
CC ECO:0000269|PubMed:12832397, ECO:0000269|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 (at protein level) (PubMed:12832396, PubMed:17462011). Strongest
CC expression in spores, with weaker expression in aerial hyphae.
CC {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:17462011,
CC ECO:0000305|PubMed:12832397}.
CC -!- INDUCTION: Highly expressed in 24 hour cultures while still submerged,
CC during aerial hyphae formation on minimal medium, decreases once aerial
CC growth ceases (PubMed:12832396). Strongly induced during aerial hyphae
CC formation and sporulation on rich medium, under control of ECF sigma
CC factor BldN; more strongly expressed when sporulation is blocked by
CC deletion of whiB, whiD or whiH (PubMed:12832397). Expression depends on
CC bldB but not bldA, bldD or bldH (at protein level) (PubMed:17462011).
CC {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397,
CC ECO:0000269|PubMed:17462011}.
CC -!- DOMAIN: The mature protein has a random coil structure at acidic pH,
CC rapidly changing to beta-sheet as the pH rises (examined from pH 3.0 to
CC 10.0); at pH 6.7 and higher forms amyloid fibrils visible by electron
CC microscopy. {ECO:0000269|PubMed:28400129, ECO:0000305|PubMed:21526199}.
CC -!- MASS SPECTROMETRY: Mass=5279; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12832396};
CC -!- MASS SPECTROMETRY: Mass=5271.65; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12832397};
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted individually in
CC a wild-type strain; the lethal effects of its disruption are suppressed
CC by loss of some other chaplins, the roldet protein (RdlA and RdlB) or
CC by inactivation of the tat secretion pathway (PubMed:18586935).
CC Quintuple knockout chpA-chpB-chpC-chpD-chpH has strongly delayed aerial
CC hyphae formation, makes many fewer aerial hyphae but no effect on
CC viability of the spores produced. Further deletion of chpE leads to
CC more severe effects, and on rich media few aerial hyphae are produced
CC after prolonged growth. Those few hyphae do differentiate into spores
CC and have a rodlet layer (PubMed:12832396). Deletion of all 8 chaplin
CC genes on minimal medium leads to severely disrupted aerial hyphae that
CC collapse on the colony surface and are not hydrophobic. A few spore
CC chains 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:15228525, ECO:0000269|PubMed:17462011,
CC ECO:0000269|PubMed:18586935, 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; AL939110; CAB45292.1; -; Genomic_DNA.
DR PIR; T36861; T36861.
DR RefSeq; NP_626070.1; NC_003888.3.
DR RefSeq; WP_003977022.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9X9Z2; -.
DR STRING; 100226.SCO1800; -.
DR GeneID; 1097234; -.
DR KEGG; sco:SCO1800; -.
DR PATRIC; fig|100226.15.peg.1821; -.
DR eggNOG; ENOG50348JU; Bacteria.
DR HOGENOM; CLU_145456_3_1_11; -.
DR OMA; QAPIHIP; -.
DR PhylomeDB; Q9X9Z2; -.
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; Fimbrium; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:12832396,
FT ECO:0000269|PubMed:12832397"
FT CHAIN 28..82
FT /note="Chaplin-E"
FT /id="PRO_5004336130"
FT DOMAIN 41..81
FT /note="Chaplin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
SQ SEQUENCE 82 AA; 7760 MW; 0400569E5A7E097C CRC64;
MKNLKKAAAV TMVAGGLIAA GAGMASATDG GAHAHGKAVG SPGVASGNLV QAPIHIPVNA
VGNSVNVIGV LNPAFGNLGV NH
