RDLA_STRCO
ID RDLA_STRCO Reviewed; 131 AA.
AC Q7AY50; Q9L1J8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Rodlin protein RdlA {ECO:0000303|PubMed:12067338};
DE Flags: Precursor;
GN Name=rdlA {ECO:0000303|PubMed:12067338}; OrderedLocusNames=SCO2718;
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, NO AMYLOID FORMATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP DOMAIN, AND MUTAGENESIS OF 44-GLU--GLU-64.
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: Probably forms part of the rodlet layer on the spore surface;
CC despite their high similarity both RdlA and RdlB are required for
CC rodlet formation (PubMed:12067338, PubMed:15228525). Plays a role in
CC cell adhesion to polystyrene plates (PubMed:12067338). Does not form
CC amyloid fibrils in vitro, unlike RdlB (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 aerial hyphae and spores (at protein level).
CC {ECO:0000269|PubMed:12067338, ECO:0000269|PubMed:28211492}.
CC -!- INDUCTION: During aerial hyphae formation.
CC {ECO:0000269|PubMed:12067338}.
CC -!- DOMAIN: The N-terminus of RdlA is more highly charged than the same
CC region in RdlB; replacing 3 charged residues by polar residues confers
CC the ability to form amyloid rods to RdlA and allows the mutant protein
CC to form rodlets by itself, which neither RdlA or RdlB can do alone.
CC {ECO:0000269|PubMed:28211492}.
CC -!- DISRUPTION PHENOTYPE: A single rdlA mutant does not form the rodlet
CC layer on spore cell walls; disruption can be complemented by rdlA from
CC S.tendae or S.griseus but not by any rdlB. Decreased levels of rdlB
CC mRNA (PubMed:15228525). A double rdlA-rdlB deletion shows no effect on
CC spore germination, growth rates, differentiation of aerial hyphae into
CC spores or surface hydrophobicity on a number of media, but spore
CC surface rodlets are missing and cells adhere less strongly to a
CC polysytrene surface (PubMed:12067338). In the double rdlA-rdlB mutant
CC chaplin proteins are still correctly localized to the cell wall of
CC aerial hyphae (PubMed:12832396). In the double rdlA-rdlB mutant aerial
CC hyphae development is strongly delayed under high osmolarity (10.3%
CC sucrose or 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; AJ315950; CAC69979.1; -; Genomic_DNA.
DR EMBL; AL939113; CAB75307.1; -; Genomic_DNA.
DR RefSeq; NP_626951.1; NC_003888.3.
DR RefSeq; WP_003976082.1; NZ_VNID01000020.1.
DR AlphaFoldDB; Q7AY50; -.
DR STRING; 100226.SCO2718; -.
DR GeneID; 1098152; -.
DR KEGG; sco:SCO2718; -.
DR PATRIC; fig|100226.15.peg.2773; -.
DR eggNOG; ENOG5033VPI; Bacteria.
DR HOGENOM; CLU_1905512_0_0_11; -.
DR OMA; QNQQCAE; -.
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 Cell adhesion; Cell wall; Direct protein sequencing; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:12067338"
FT CHAIN 29..131
FT /note="Rodlin protein RdlA"
FT /id="PRO_5004287812"
FT MUTAGEN 44..64
FT /note="ESAFGNSATKGDMSPQLSLVE->QSAFGNSATKGNMSPQLSLVQ: Forms
FT amyloid-like structure in vitro, restores rodlets in double
FT rdlA-rdlB mutants."
FT /evidence="ECO:0000269|PubMed:28211492"
SQ SEQUENCE 131 AA; 13084 MW; 9108DBB47936DCDF CRC64;
MLKKAMVAAA AAASVIGMSA AAAPQALAIG DDNGPAVANG NGAESAFGNS ATKGDMSPQL
SLVEGTLNKP CLGVEDVNVA VINLVPIQDI NVLADDLNQQ CADNSTQAKR DGALSHVLED
LSVLSANGEG R
