CHPH_STRCO
ID CHPH_STRCO Reviewed; 77 AA.
AC Q9AD92;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Chaplin-H {ECO:0000303|PubMed:12832396};
DE Flags: Precursor;
GN Name=chpH {ECO:0000303|PubMed:12832396}; OrderedLocusNames=SCO1675;
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, MASS
RP SPECTROMETRY, AND 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, CREATION OF A MINIMAL CHAPLIN STRAIN, AND MUTAGENESIS OF CYS-56
RP AND CYS-74.
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, AMYLOID FORMATION, SUBUNIT, SUBCELLULAR LOCATION, AND DISULFIDE
RP BOND.
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 AMYLOID FORMATION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP 30-GLN--VAL-51; 62-VAL--LEU-66 AND VAL-62.
RC STRAIN=A3(2) / M600;
RX PubMed=21628577; DOI=10.1073/pnas.1018715108;
RA Capstick D.S., Jomaa A., Hanke C., Ortega J., Elliot M.A.;
RT "Dual amyloid domains promote differential functioning of the chaplin
RT proteins during Streptomyces aerial morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9821-9826(2011).
RN [10]
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 [11]
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
CC (PubMed:21526199). A small chaplin extract (ChpD, ChpE, ChpF, ChpG and
CC ChpH) self-assembles into 2 different amyloids; small fibrils at the
CC air-water interface form an amphipathic membrane that resembles spore-
CC surface structures involved in aerial hyphae formation, and hydrophilic
CC fibrils in solution that resemble the fibers that attach cells to a
CC hydrophobic surface. At the air-water interface the hydrophilic surface
CC is in contact with water (probably equivalent to the peptidoglycan
CC layer), while the hydrophobic face is exposed to the air, making the
CC surface of the aerial hyphae hydrophobic (PubMed:24012833). A minimal
CC chaplin strain capable of forming aerial mycelium/hyphae on minimal
CC medium contains ChpC, ChpE and ChpH. The strain also has restored
CC rodlet formation on the hyphae surface (PubMed:18586935). A small
CC chaplin extract applied to a chaplin-deficient strain restores aerial
CC hyphae formation (PubMed:12832396, PubMed:12832397). The small chaplin
CC extract forms an amyloid-like structure similar to that seen on the
CC surface of cells without rodlets (rdlA-rdlB deletions), and is highly
CC surface active, reducing surface tension from 72 to 26 mJ/m(2), which
CC probably 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 -!- SUBUNIT: Homodimer; disulfide linked. About 10% of ChpH isolated from
CC cell wall forms disulfide-bonded homodimers.
CC {ECO:0000269|PubMed:21526199}.
CC -!- INTERACTION:
CC Q9AD92; Q9AD92: chpH; NbExp=2; IntAct=EBI-15929047, EBI-15929047;
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 ECO:0000269|PubMed:21526199, ECO:0000269|PubMed:21628577}. Fimbrium
CC {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 (PubMed:12832397). {ECO:0000269|PubMed:12832396,
CC ECO:0000269|PubMed:12832397, ECO:0000269|PubMed:17462011}.
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. Strongly expressed in aerial hyphae (at protein level)
CC (PubMed:12832396). During aerial hyphae formation and sporulation on
CC rich medium, under control of ECF sigma factor BldN; more strongly
CC expressed when sporulation is blocked by deletion of whiB, whiD or whiH
CC (PubMed:12832397). Expression depends on bldB but not bldA, bldD or
CC bldH (at protein level) (PubMed:17462011).
CC {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397,
CC ECO:0000269|PubMed:17462011}.
CC -!- DOMAIN: Has 2 domains capable of forming beta amyloid structures, both
CC of which are required for aerial hyphae formation while the N-terminal
CC region is not required for rodlet formation.
CC {ECO:0000269|PubMed:21628577}.
CC -!- MASS SPECTROMETRY: Mass=5122; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12832396};
CC -!- MASS SPECTROMETRY: Mass=5116.61; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12832397};
CC -!- DISRUPTION PHENOTYPE: A single chpH disruption and double chpC-chpH
CC knockout have no visible or sporulation phenotype; a quadruple chpA-
CC chpC-chpD-chpH knockout has delayed aerial hyphae formation and
CC sporulation. A quintuple chpA-chpB-chpC-chpD-chpH knockout has a longer
CC delay in aerial hyphae formation and an almost complete lack of
CC sporulation. The quintuple knockout still expresses ChpE, ChpF and ChpG
CC (PubMed:12832397). Quintuple knockout chpA-chpB-chpC-chpD-chpH has
CC strongly delayed aerial hyphae formation, makes many fewer aerial
CC hyphae but no effect on viability of the spores produced. Further
CC deletion of chpE leads to more severe effects, and on rich media few
CC aerial hyphae are produced after prolonged growth. Those few hyphae do
CC differentiate into spores and have a rodlet layer (PubMed:12832396).
CC Deletion of all 8 chaplin genes on minimal medium leads to severely
CC disrupted aerial hyphae that collapse on the colony surface and are not
CC hydrophobic. A few spore chains can still be made, but they have
CC neither rodlets or amyloid-like fibers. rdlA and rdlB mRNA are down-
CC regulated (PubMed:15228525, PubMed:17462011). Deletion of all 8 chaplin
CC genes on rich medium leads to a reduced abundance of aerial hyphae
CC without rodlets and occasional spore chains on surface hyphae. A
CC complete chaplin-negative plus ram-negative strain (deletion of ramR or
CC the ramC-ramS-ramA-ramB operon) leads to the complete loss of robust
CC aerial hyphae (PubMed:17462011). Deletion of all 8 chaplin genes
CC significantly reduces cellular attachment to a hydrophobic substrate;
CC thin fibrils instead of fimbrae are detected. The long chaplins (ChpA,
CC ChpB and ChpC, as seen by near wild-type attachment of the hextuple
CC chpA-chpB-chpC-chpD-chpE-chpH knockout) are not essential but may
CC contribute to attachment (PubMed:19682261).
CC {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397,
CC ECO:0000269|PubMed:15228525, ECO:0000269|PubMed:17462011,
CC 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; AL939109; CAC36378.1; -; Genomic_DNA.
DR RefSeq; NP_625950.1; NC_003888.3.
DR RefSeq; WP_003977150.1; NZ_VNID01000018.1.
DR AlphaFoldDB; Q9AD92; -.
DR DIP; DIP-60401N; -.
DR STRING; 100226.SCO1675; -.
DR DNASU; 1097106; -.
DR GeneID; 1097106; -.
DR KEGG; sco:SCO1675; -.
DR PATRIC; fig|100226.15.peg.1692; -.
DR eggNOG; ENOG50348JU; Bacteria.
DR HOGENOM; CLU_145456_3_1_11; -.
DR OMA; VHSPGVV; -.
DR PhylomeDB; Q9AD92; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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..25
FT /evidence="ECO:0000269|PubMed:12832396,
FT ECO:0000269|PubMed:12832397"
FT CHAIN 26..77
FT /note="Chaplin-H"
FT /evidence="ECO:0000255"
FT /id="PRO_5004323940"
FT DOMAIN 36..76
FT /note="Chaplin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT REGION 38..54
FT /note="Forms amyloid fibrils in vitro"
FT /evidence="ECO:0000269|PubMed:21628577"
FT REGION 57..72
FT /note="Forms amyloid fibrils in vitro"
FT /evidence="ECO:0000269|PubMed:21628577"
FT DISULFID 56..74
FT /evidence="ECO:0000305|PubMed:12832397,
FT ECO:0000305|PubMed:21526199"
FT MUTAGEN 30..51
FT /note="Missing: Very decreased formation of aerial hyphae,
FT no spore chains formed, no effect on rodlet formation."
FT /evidence="ECO:0000269|PubMed:21628577"
FT MUTAGEN 56
FT /note="C->V: In minimal chaplin strain, forms very sparse
FT aerial hyphae, no rodlets form; when associated with G-74,
FT loss of disulfide bond."
FT /evidence="ECO:0000269|PubMed:18586935"
FT MUTAGEN 62..66
FT /note="VIGLL->AAAAA: Severely reduced ability to form
FT amyloid fibers in vitro, very decreased formation of aerial
FT hyphae, very few rodlets, no spore chains formed."
FT /evidence="ECO:0000269|PubMed:21628577"
FT MUTAGEN 62
FT /note="V->A: Significantly reduced ability to form amyloid
FT fibers in vitro, decreased formation of aerial hyphae and
FT rodlets, no change in spore chain formation."
FT /evidence="ECO:0000269|PubMed:21628577"
FT MUTAGEN 74
FT /note="C->G: In minimal chaplin strain, forms very sparse
FT aerial hyphae, no rodlets form; when associated with V-56,
FT loss of disulfide bond."
FT /evidence="ECO:0000269|PubMed:18586935"
SQ SEQUENCE 77 AA; 7345 MW; 34FAD03DBE797735 CRC64;
MLKKVVAAAA ATGGLVLAGA GMAVADSGAQ GAAVHSPGVL SGNVVQVPVH VPVNVCGNTI
SVIGLLNPAF GNVCINK
