CHPF_STRCO
ID CHPF_STRCO Reviewed; 88 AA.
AC Q9KYG7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Chaplin-F {ECO:0000303|PubMed:12832396};
DE AltName: Full=Chaplin-G {ECO:0000303|PubMed:12832397};
DE Flags: Precursor;
GN Name=chpF {ECO:0000303|PubMed:12832396};
GN Synonyms=chpG {ECO:0000303|PubMed:12832397}; OrderedLocusNames=SCO2705;
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, AND MASS SPECTROMETRY.
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, AND MASS 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 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 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 [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, AMYLOID FORMATION, AND DOMAIN.
RX PubMed=28925983; DOI=10.3390/biom7030068;
RA Dokouhaki M., Prime E.L., Hung A., Qiao G.G., Day L., Gras S.L.;
RT "Structure-dependent interfacial properties of chaplin F from Streptomyces
RT coelicolor.";
RL Biomolecules 7:0-0(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 (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 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). ChpF alone is less surface active at pH 3.0 than at
CC pH 10.0, it reduces the surface tension of water from 72.8 mN/m to 50
CC mN/m at pH 3.0 or to 37 mN/m at pH 10.0 (PubMed:28925983). ChpF and
CC ChpG are sufficient to restore the rodlet layer and hydrophobicity to a
CC strain deleted for the other 6 chaplin genes (PubMed:15228525).
CC {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397,
CC ECO:0000269|PubMed:15228525, ECO:0000269|PubMed:17462011,
CC ECO:0000269|PubMed:19682261, ECO:0000269|PubMed:21526199,
CC ECO:0000269|PubMed:24012833, ECO:0000269|PubMed:28925983}.
CC -!- SUBUNIT: Homodimer; disulfide linked. About 20% of ChpF isolated from
CC cell wall forms disulfide-bonded homodimers.
CC {ECO:0000269|PubMed:21526199}.
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}. Fimbrium {ECO:0000269|PubMed:19682261}.
CC Note=Considerably more ChpF is seen in fimbrae than in aerial hyphae.
CC {ECO:0000269|PubMed:19682261}.
CC -!- DEVELOPMENTAL STAGE: Present in aerial hyphae of sporulating cultures
CC (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 (PubMed:12832396). During aerial hyphae formation
CC and early sporulation on rich medium, under control of ECF sigma factor
CC BldN (PubMed:12832397). Expression depends on bldB but not bldA, bldD
CC 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 rapidly forms a predominantly amyloid fibril
CC beta-sheet structure at pH 3.0 and 4.2, with less beta-sheet and more
CC random coil at pH 10 (Probable) (PubMed:28925983). Reduced and non-
CC reduced peptide have the same secondary structures at all pH tested,
CC suggesting the disulfide bond is not required for fibril formation
CC (PubMed:28925983). {ECO:0000269|PubMed:28925983,
CC ECO:0000305|PubMed:21526199}.
CC -!- MASS SPECTROMETRY: Mass=5182; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12832396};
CC -!- MASS SPECTROMETRY: Mass=5177.48; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12832397};
CC -!- DISRUPTION PHENOTYPE: A strain deleted of chpF and chpG makes rodlets
CC (PubMed:15228525). 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. A few spore chains can still be made,
CC but they have neither rodlets or amyloid-like fibers. rdlA and rdlB
CC mRNA are down-regulated (PubMed:15228525, PubMed:17462011). Deletion of
CC all 8 chaplin genes on rich medium leads to a reduced abundance of
CC aerial hyphae without rodlets and occasional spore chains on surface
CC hyphae. A complete chaplin-negative plus ram-negative strain (deletion
CC of ramR or the ramC-ramS-ramA-ramB operon) leads to the complete loss
CC of robust aerial hyphae (PubMed:17462011). Deletion of all 8 chaplin
CC genes significantly reduces cellular attachment to a hydrophobic
CC substrate; thin fibrils instead of fimbrae are detected. The long
CC chaplins (ChpA, ChpB and ChpC, as seen by near wild-type attachment of
CC the hextuple chpA-chpB-chpC-chpD-chpE-chpH knockout) are not essential
CC but may contribute to attachment (PubMed:19682261).
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; AL939113; CAB92271.1; -; Genomic_DNA.
DR RefSeq; NP_626939.1; NC_003888.3.
DR RefSeq; WP_003976095.1; NC_003888.3.
DR AlphaFoldDB; Q9KYG7; -.
DR STRING; 100226.SCO2705; -.
DR DNASU; 1098139; -.
DR GeneID; 1098139; -.
DR KEGG; sco:SCO2705; -.
DR PATRIC; fig|100226.15.peg.2760; -.
DR eggNOG; ENOG50348JU; Bacteria.
DR HOGENOM; CLU_145456_3_1_11; -.
DR OMA; NTCINAD; -.
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..36
FT /evidence="ECO:0000269|PubMed:12832396,
FT ECO:0000269|PubMed:12832397"
FT CHAIN 37..88
FT /note="Chaplin-F"
FT /id="PRO_5004329169"
FT DOMAIN 47..87
FT /note="Chaplin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT DISULFID 67..85
FT /evidence="ECO:0000305|PubMed:12832397"
SQ SEQUENCE 88 AA; 8698 MW; D0AEB6579BD330D9 CRC64;
MYNPKEHFSM SRIAKGLALT SVAAAAVAGT AGVAAADSGA QAAAAHSPGV LSGNVVQVPV
HIPVNVCGNT IDVIGLLNPA FGNECEND
