CHPC_STRCO
ID CHPC_STRCO Reviewed; 259 AA.
AC Q9AD93;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Chaplin-C {ECO:0000303|PubMed:12832396};
DE Flags: Precursor;
GN Name=chpC {ECO:0000303|PubMed:12832396}; OrderedLocusNames=SCO1674;
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, INDUCTION, 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, INDUCTION, 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, AND 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, AND 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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=A3(2) / M600;
RX PubMed=22296345; DOI=10.1111/j.1365-2958.2012.07983.x;
RA Duong A., Capstick D.S., Di Berardo C., Findlay K.C., Hesketh A.,
RA Hong H.J., Elliot M.A.;
RT "Aerial development in Streptomyces coelicolor requires sortase activity.";
RL Mol. Microbiol. 83:992-1005(2012).
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). A minimal chaplin strain
CC capable of forming aerial mycelium/hyphae on minimal medium contains
CC ChpC, ChpE and ChpH. The strain also has restored rodlet formation on
CC the hyphae surface (PubMed:18586935). The long chaplins (ChpA, ChpB,
CC ChpC) are not absolutely necessary for short chaplin localization or
CC rodlet formation, but probably play a role in initiating aerial hyphae
CC development (PubMed:22296345). Chaplins are also involved in cell
CC attachment to a hydrophobic surface (PubMed:19682261).
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:22296345}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22296345}. Secreted,
CC cell wall {ECO:0000255|PROSITE-ProRule:PRU00477,
CC ECO:0000269|PubMed:22296345}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477}. Note=Anchored to the cell wall
CC by sortase SrtE2 and to a lesser extent by sortase SrtE1.
CC {ECO:0000269|PubMed:22296345}.
CC -!- INDUCTION: Transcribed during aerial hyphae formation on minimal
CC medium, about 10- to 25-fold lower expression than the short chaplins
CC (Probable). Strongly induced during aerial hyphae formation and early
CC sporulation on rich medium, under control of ECF sigma factor BldN
CC (PubMed:12832397). {ECO:0000269|PubMed:12832397,
CC ECO:0000305|PubMed:12832396}.
CC -!- DISRUPTION PHENOTYPE: A single chpC disruption and double chpC-chpH
CC knockout have no phenotype; a quadruple chpA-chpC-chpD-chpH knockout
CC has delayed aerial hyphae formation and sporulation. A quintuple chpA-
CC chpB-chpC-chpD-chpH knockout has a longer delay in aerial hyphae
CC formation and an almost complete lack of sporulation. The quintuple
CC knockout still expresses ChpE, ChpF and ChpG (PubMed:12832397).
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 the 3 long chaplins (ChpA-ChpB-ChpC) results in a 24 hour
CC delay in aerial hyphae formation, while rodlets are about 1.5-fold
CC longer than wild-type (PubMed:22296345). 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 cellular 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, ECO:0000269|PubMed:22296345}.
CC -!- SIMILARITY: Belongs to the chaplin family. Long chaplin subfamily.
CC {ECO:0000305|PubMed:12832397}.
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DR EMBL; AL939109; CAC36377.1; -; Genomic_DNA.
DR RefSeq; NP_625949.1; NC_003888.3.
DR RefSeq; WP_011027911.1; NZ_VNID01000018.1.
DR AlphaFoldDB; Q9AD93; -.
DR STRING; 100226.SCO1674; -.
DR GeneID; 1097105; -.
DR KEGG; sco:SCO1674; -.
DR PATRIC; fig|100226.15.peg.1691; -.
DR eggNOG; ENOG5033GQX; Bacteria.
DR HOGENOM; CLU_070271_0_0_11; -.
DR OMA; RKGLMTM; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR005528; ChpA-H.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF03777; ChpA-C; 2.
DR PROSITE; PS51884; CHAPLIN; 2.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Amyloid; Cell adhesion; Cell wall; Peptidoglycan-anchor;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..259
FT /note="Chaplin-C"
FT /evidence="ECO:0000255"
FT /id="PRO_5004325719"
FT PROPEP 229..259
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000445190"
FT DOMAIN 39..79
FT /note="Chaplin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT DOMAIN 119..159
FT /note="Chaplin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT REGION 84..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 225..229
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 172..192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 228
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:22296345"
SQ SEQUENCE 259 AA; 24519 MW; 916D561EDBC3E25A CRC64;
MRQATRKGLM TMAAATGVIA AAGGAAHADS GAHGTSSGSP GVLSGNTVQA PVHVPVNVCG
NTVDVVGVLN PAMGNACANQ GGGASGGHGG HGGHGGYGDS GGEGGSHGGS HAGGHATDSP
GVGSGNHVEV PIDVPVNVCG NSIDVVGALN PTTGNDCGNG GGGDHSTPPG DHETPPGEPH
NPGNPGNPDT PDKPSGPDDE TPGDSTDGNR PGAQTVDQPR GDAALAETGS DLPLGLALPV
GAGALLAGTV LYRKARASV
