CHPB_STRCO
ID CHPB_STRCO Reviewed; 237 AA.
AC Q9X7U2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Chaplin-B {ECO:0000303|PubMed:12832396};
DE Flags: Precursor;
GN Name=chpB {ECO:0000303|PubMed:12832396}; OrderedLocusNames=SCO7257;
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 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 [7]
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). The long chaplins (ChpA,
CC ChpB, ChpC) are not absolutely necessary for short chaplin localization
CC or rodlet formation, but probably play a role in initiating aerial
CC hyphae development (PubMed:22296345). Chaplins are also involved in
CC cell 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: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: Transcribed during aerial hyphae formation on minimal
CC medium, about 10- to 25-fold lower expression than the short chaplins.
CC Weak expression in aerial hyphae (at protein level) (Probable). Very
CC low expression on rich medium, unaffected by ECF sigma factor BldN
CC (PubMed:12832397). {ECO:0000269|PubMed:12832397,
CC ECO:0000305|PubMed:12832396}.
CC -!- DISRUPTION PHENOTYPE: A single chpB disruption has no phenotype; a
CC quadruple chpA-chpC-chpD-chpH knockout has delayed aerial hyphae
CC formation and sporulation. A quintuple chpA-chpB-chpC-chpD-chpH
CC knockout has a longer delay in aerial hyphae formation and an almost
CC complete lack of sporulation. The quintuple knockout still expresses
CC ChpE, ChpF and ChpG (PubMed:12832397). Quintuple knockout chpA-chpB-
CC chpC-chpD-chpH has strongly delayed aerial hyphae formation, makes many
CC fewer aerial hyphae but no effect on viability of the spores produced.
CC Further deletion of chpE leads to more severe effects, and on rich
CC media few aerial hyphae are produced after prolonged growth. Those few
CC hyphae do differentiate into spores and have a rodlet layer
CC (PubMed:12832396). 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 the 3 long
CC chaplins (ChpA, ChpB, ChpC) results in a 24 hour delay in aerial hyphae
CC formation, while rodlets are about 1.5-fold longer than wild-type
CC (PubMed:22296345). Deletion of all 8 chaplin genes significantly
CC reduces cellular attachment to a hydrophobic substrate; thin fibrils
CC instead of fimbrae are detected. The long chaplins (ChpA, ChpB and
CC ChpC, as seen by near wild-type attachment of the hextuple chpA-chpB-
CC chpC-chpD-chpE-chpH knockout) are not essential but may contribute to
CC cellular attachment (PubMed:19682261). {ECO:0000269|PubMed:12832396,
CC ECO:0000269|PubMed:12832397, ECO:0000269|PubMed:15228525,
CC ECO:0000269|PubMed:17462011, ECO:0000269|PubMed:19682261,
CC 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; AL939131; CAB42960.1; -; Genomic_DNA.
DR PIR; T35351; T35351.
DR RefSeq; NP_631313.1; NC_003888.3.
DR RefSeq; WP_011031547.1; NC_003888.3.
DR AlphaFoldDB; Q9X7U2; -.
DR STRING; 100226.SCO7257; -.
DR GeneID; 1102695; -.
DR KEGG; sco:SCO7257; -.
DR PATRIC; fig|100226.15.peg.7359; -.
DR eggNOG; ENOG5034C0V; Bacteria.
DR HOGENOM; CLU_070271_0_0_11; -.
DR OMA; RRTEDRI; -.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..237
FT /note="Chaplin-B"
FT /evidence="ECO:0000255"
FT /id="PRO_5004336275"
FT PROPEP 206..237
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000445189"
FT DOMAIN 42..82
FT /note="Chaplin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT DOMAIN 120..160
FT /note="Chaplin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01232"
FT REGION 81..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 202..206
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 93..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 237 AA; 22741 MW; 73E3C5F2A0C745AF CRC64;
MRRVTRNGVL AVAASGALAV TMPAYAAFAS DGAGAEGSAA GSPGLISGNT VQLPVDVPVD
VCGNTVNVVG LLNPAAGNGC ADSGEPGASY QAAGASGGTS GSATEATSGG AAAEGSGKDS
PGVLSGNGVQ LPVHLPVNVS GNSVNVVGIG NPAVGNESTN DSGDHPEPVR PPAEPEPSAP
EEERAGPGPS AHAAPPREEV SLAHTGTDRT LPTLAGGAAL VLGGTVLYRR FRPGSGD
