RDLB_STRCO
ID RDLB_STRCO Reviewed; 133 AA.
AC Q934F8; Q9L1J7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Rodlin protein RdlB {ECO:0000303|PubMed:12067338};
DE Flags: Precursor;
GN Name=rdlB {ECO:0000303|PubMed:12067338}; OrderedLocusNames=SCO2719;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12067338; DOI=10.1046/j.1365-2958.2002.02980.x;
RA Claessen D., Wosten H.A., van Keulen G., Faber O.G., Alves A.M.,
RA Meijer W.G., Dijkhuizen L.;
RT "Two novel homologous proteins of Streptomyces coelicolor and Streptomyces
RT lividans are involved in the formation of the rodlet layer and mediate
RT attachment to a hydrophobic surface.";
RL Mol. Microbiol. 44:1483-1492(2002).
RN [2]
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 [3]
RP 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, AND DISRUPTION PHENOTYPE.
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 DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=22309453; DOI=10.1111/j.1574-6968.2012.02517.x;
RA de Jong W., Vijgenboom E., Dijkhuizen L., Woesten H.A., Claessen D.;
RT "SapB and the rodlins are required for development of Streptomyces
RT coelicolor in high osmolarity media.";
RL FEMS Microbiol. Lett. 329:154-159(2012).
RN [6]
RP FUNCTION, AMYLOID FORMATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP DOMAIN, AND MUTAGENESIS OF 45-GLU--PRO-70 AND 45-GLU--ASN-68.
RX PubMed=28211492; DOI=10.1038/srep42867;
RA Yang W., Willemse J., Sawyer E.B., Lou F., Gong W., Zhang H., Gras S.L.,
RA Claessen D., Perrett S.;
RT "The propensity of the bacterial rodlin protein RdlB to form amyloid
RT fibrils determines its function in Streptomyces coelicolor.";
RL Sci. Rep. 7:42867-42867(2017).
CC -!- FUNCTION: Forms part of the rodlet layer on the spore surface; despite
CC their high similarity both RdlA and RdlB are required for rodlet
CC formation (PubMed:12067338, PubMed:15228525). Plays a role in cell
CC adhesion to polystyrene plates (PubMed:12067338). Forms amyloid-like
CC fibrils in vitro composed of stacked beta-sheets (PubMed:28211492).
CC {ECO:0000269|PubMed:12067338, ECO:0000269|PubMed:15228525,
CC ECO:0000269|PubMed:28211492}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:12067338}. Spore wall {ECO:0000269|PubMed:28211492,
CC ECO:0000305|PubMed:12067338, ECO:0000305|PubMed:15228525}. Note=Found
CC on the surface of aerial hyphae and probably on the surface of the
CC spore wall (PubMed:12067338). Rodlins probably contribute to the semi-
CC transparent sheath-like structure which encapsulates spores, probably
CC outside the chaplin layer (Probable). {ECO:0000269|PubMed:12067338,
CC ECO:0000305|PubMed:28211492}.
CC -!- DEVELOPMENTAL STAGE: Present in aerial but not submerged hyphae,
CC persists as hyphae differentitate and form spores; present at the outer
CC surface of these structures (at protein level).
CC {ECO:0000269|PubMed:12067338, ECO:0000269|PubMed:28211492}.
CC -!- INDUCTION: During aerial hyphae formation.
CC {ECO:0000305|PubMed:12067338}.
CC -!- DOMAIN: The mature protein has 2 regions in the N-terminus capable of
CC forming amyloid rods of slightly differing conformation; intact protein
CC makes longer fibrils. Amyloid formation depends on polar residues
CC between amino acids 45 and 70. {ECO:0000269|PubMed:28211492}.
CC -!- DISRUPTION PHENOTYPE: A single rdlB mutant does not form the rodlet
CC layer on spores; disruption can be complemented by rdlB from S.tendae
CC or S.griseus but not by any rdlA. Decreased levels of rdlA mRNA
CC (PubMed:15228525). A double rdlA-rdlB deletion shows no effect on spore
CC germination, growth rates, differentiation of aerial hyphae into spores
CC or surface hydrophobicity on a number of media, but spore surface
CC rodlets are missing and cells adhere less strongly to a polysytrene
CC surface (PubMed:12067338). In the double rdlA-rdlB mutant chaplin
CC proteins are still correctly localized to the cell wall of aerial
CC hyphae (PubMed:12832396). In the double rdlA-rdlB mutant aerial hyphae
CC development is strongly delayed under high osmolarity (10.3% sucrose or
CC 0.5 M KCl) (PubMed:22309453). {ECO:0000269|PubMed:12067338,
CC ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:15228525,
CC ECO:0000269|PubMed:22309453}.
CC -!- SIMILARITY: Belongs to the rodlin family. {ECO:0000305}.
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DR EMBL; AJ315951; CAC69980.1; -; Genomic_DNA.
DR EMBL; AL939113; CAB75308.1; -; Genomic_DNA.
DR RefSeq; NP_626952.1; NC_003888.3.
DR RefSeq; WP_003976081.1; NZ_CP042324.1.
DR AlphaFoldDB; Q934F8; -.
DR STRING; 100226.SCO2719; -.
DR GeneID; 1098153; -.
DR KEGG; sco:SCO2719; -.
DR PATRIC; fig|100226.15.peg.2774; -.
DR eggNOG; ENOG5033VPI; Bacteria.
DR HOGENOM; CLU_1905512_0_0_11; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0031160; C:spore wall; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amyloid; Cell adhesion; Cell wall; Direct protein sequencing;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:12067338"
FT CHAIN 29..133
FT /note="Rodlin protein RdlB"
FT /id="PRO_5004319781"
FT REGION 45..70
FT /note="Required for amyloid formation"
FT /evidence="ECO:0000269|PubMed:28211492"
FT REGION 45..57
FT /note="Amyloid-forming"
FT /evidence="ECO:0000269|PubMed:28211492"
FT REGION 59..70
FT /note="Amyloid-forming"
FT /evidence="ECO:0000269|PubMed:28211492"
FT MUTAGEN 45..70
FT /note="Missing: No longer makes amyloid-like structures in
FT vitro, does not complement an rdlB disruption."
FT /evidence="ECO:0000269|PubMed:28211492"
FT MUTAGEN 45..68
FT /note="QYFGNSMTTGNMSPQMALIQGSFN->EYFGDSMTTGDMSPEMALIEGSFD:
FT No longer makes amyloid-like structures in vitro, does not
FT complement an rdlB disruption."
FT /evidence="ECO:0000269|PubMed:28211492"
FT CONFLICT 1
FT /note="M -> MSSGGRGFLRKDWPV (in Ref. 2; CAB75308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 133 AA; 13355 MW; B3B71F9CA29E7FB7 CRC64;
MIKKVVAYAA IAASVMGASA AAAPQAMAIG DDSGPVSANG NGASQYFGNS MTTGNMSPQM
ALIQGSFNKP CIAVSDIPVS VIGLVPIQDL NVLGDDMNQQ CAENSTQAKR DGALAHLLED
VSILSSNGEG GKG
