CHPA_STRCO
ID CHPA_STRCO Reviewed; 252 AA.
AC Q8CJY7; Q8KVT6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Chaplin-A {ECO:0000303|PubMed:12832396};
DE Flags: Precursor;
GN Name=chpA {ECO:0000303|PubMed:12832396};
GN Synonyms=ecrD {ECO:0000303|PubMed:11731481}; OrderedLocusNames=SCO2716;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-247, AND INDUCTION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=11731481; DOI=10.1101/gad.943401;
RA Huang J., Lih C.J., Pan K.H., Cohen S.N.;
RT "Global analysis of growth phase responsive gene expression and regulation
RT of antibiotic biosynthetic pathways in Streptomyces coelicolor using DNA
RT microarrays.";
RL Genes Dev. 15:3183-3192(2001).
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, 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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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. A second minimal chaplin strain with ChpA, ChpD and
CC ChpE makes slightly less robust hyphae (PubMed:18586935). The long
CC chaplins (ChpA, ChpB, ChpC) are not absolutely necessary for short
CC chaplin localization or rodlet formation, but probably play a role in
CC initiating aerial hyphae development (PubMed:22296345). Chaplins are
CC also involved in cell attachment to a hydrophobic surface
CC (PubMed:19682261). {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:22296345}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000305|PubMed:12832397,
CC ECO:0000305|PubMed:22296345}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:12832397,
CC ECO:0000305|PubMed:22296345}. Note=Anchored to the cell wall by at
CC least one of sortases SrtE1 and SrtE2. {ECO:0000305|PubMed:22296345}.
CC -!- INDUCTION: Transcription is coordinated with that of the antibiotic
CC undecylprodigiosin (Red) locus (PubMed:11731481). Transcribed during
CC aerial hyphae formation on minimal medium, about 10- to 25-fold lower
CC expression than the short chaplins. Weak expression in aerial hyphae
CC (at protein level) (PubMed:12832396). Expressed during aerial hyphae
CC formation and early sporulation on rich medium, under control of ECF
CC sigma factor BldN (PubMed:12832397). {ECO:0000269|PubMed:11731481,
CC ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397}.
CC -!- DISRUPTION PHENOTYPE: A single chpA disruption and double chpA-chpD
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; AL939113; CAD55200.1; -; Genomic_DNA.
DR EMBL; AF425993; AAM78434.1; -; Genomic_DNA.
DR RefSeq; NP_733581.1; NC_003888.3.
DR RefSeq; WP_003976084.1; NZ_VNID01000020.1.
DR AlphaFoldDB; Q8CJY7; -.
DR STRING; 100226.SCO2716; -.
DR GeneID; 1098150; -.
DR KEGG; sco:SCO2716; -.
DR PATRIC; fig|100226.15.peg.2771; -.
DR eggNOG; ENOG5033KAN; Bacteria.
DR HOGENOM; CLU_070271_0_0_11; -.
DR OMA; EEPPGYG; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR005528; ChpA-H.
DR InterPro; IPR019931; LPXTG_anchor.
DR Pfam; PF03777; ChpA-C; 2.
DR PROSITE; PS51884; CHAPLIN; 2.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Amyloid; Cell adhesion; Cell wall; Peptidoglycan-anchor;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..252
FT /note="Chaplin-A"
FT /evidence="ECO:0000255"
FT /id="PRO_5004304513"
FT PROPEP 219..252
FT /note="Removed by sortase"
FT /evidence="ECO:0000305|PubMed:22296345"
FT /id="PRO_0000445187"
FT PROPEP 221..252
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:22296345"
FT /id="PRO_0000445188"
FT DOMAIN 31..71
FT /note="Chaplin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT DOMAIN 112..152
FT /note="Chaplin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT REGION 71..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 217..221
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:22296345"
FT COMPBIAS 86..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:22296345"
SQ SEQUENCE 252 AA; 24640 MW; 6910768D70B366FF CRC64;
MVAAAAATGI LSLCGSPALA DSHADGAATN SPGAVSGNAL QVPVDVPVNA CGNTVDVIAA
LNPAFGNECE NASDEKTDGH GGGYGEDASS SSSSSTSASS SGSHADGATE GSPGVGSGNN
AQVPVDVPVN LCGNTVDVIA ALNPVFGNKC ENDAEEPPGY GEEEPPPPTT PPGYGEEEPP
PPTHEEPPPP SGEEEPPPPS EEEHTPPAPQ TEQPPALAET GSEGTLGAAA AGAVLIAGGA
ILYRRGRALS GR
