RBPA_STRCO
ID RBPA_STRCO Reviewed; 124 AA.
AC Q9RKY0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=RNA polymerase-binding protein RbpA {ECO:0000255|HAMAP-Rule:MF_01483};
GN Name=rbpA {ECO:0000255|HAMAP-Rule:MF_01483}; OrderedLocusNames=SCO1421;
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 PROTEIN SEQUENCE OF 2-25, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=11737643; DOI=10.1046/j.1365-2958.2001.02675.x;
RA Paget M.S.B., Molle V., Cohen G., Aharonowitz Y., Buttner M.J.;
RT "Defining the disulphide stress response in Streptomyces coelicolor A3(2):
RT identification of the sigmaR regulon.";
RL Mol. Microbiol. 42:1007-1020(2001).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH RNA POLYMERASE, ANTIBIOTIC RESISTANCE,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=16629670; DOI=10.1111/j.1365-2958.2006.05116.x;
RA Newell K.V., Thomas D.P., Brekasis D., Paget M.S.;
RT "The RNA polymerase-binding protein RbpA confers basal levels of rifampicin
RT resistance on Streptomyces coelicolor.";
RL Mol. Microbiol. 60:687-696(2006).
RN [4]
RP STRUCTURE BY NMR OF 28-75, FUNCTION, SUBUNIT, INTERACTION WITH HRDB (SIGA),
RP COFACTOR, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-34; HIS-38; CYS-56;
RP CYS-59; HIS-82; GLU-88; 89-ARG-ARG-90; ARG-89; ARG-90 AND HIS-116.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=23605043; DOI=10.1093/nar/gkt277;
RA Tabib-Salazar A., Liu B., Doughty P., Lewis R.A., Ghosh S., Parsy M.L.,
RA Simpson P.J., O'Dwyer K., Matthews S.J., Paget M.S.;
RT "The actinobacterial transcription factor RbpA binds to the principal sigma
RT subunit of RNA polymerase.";
RL Nucleic Acids Res. 41:5679-5691(2013).
CC -!- FUNCTION: Binds to RNA polymerase (RNAP), stimulating transcription
CC from principal, but not alternative sigma factor promoters. Stimulates
CC transcription from several principal sigma factor HrdB (SigA)-dependent
CC promoters but not from a SigR-dependent promoter. Stimulation occurs in
CC the presence of the transcription initiation inhibitor rifampicin
CC (Rif). {ECO:0000255|HAMAP-Rule:MF_01483, ECO:0000269|PubMed:16629670,
CC ECO:0000269|PubMed:23605043}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01483,
CC ECO:0000269|PubMed:23605043};
CC Note=Bind 1 Zn(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01483,
CC ECO:0000269|PubMed:23605043};
CC -!- SUBUNIT: Homodimer (Probable). Forms a complex with the RNAP, and a
CC complex with RNAP plus principal sigma factor HrdB associated with
CC promoter. Binds to free principal sigma factors HrdB and HrdA, probably
CC via the sigma-2 domain, but not to 6 other sigma factors tested.
CC {ECO:0000269|PubMed:11737643, ECO:0000269|PubMed:16629670,
CC ECO:0000269|PubMed:23605043, ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed partially under control of SigR;
CC both SigR-dependent and independent induction are further induced by
CC the thiol-oxidant diamide (disulfide stress). Induced by Rif.
CC {ECO:0000269|PubMed:11737643}.
CC -!- DISRUPTION PHENOTYPE: Grows slowly, colonies are smaller. Not more
CC diamide sensitive than wild-type, sporulation normal, 15-fold more
CC sensitive to Rif. {ECO:0000269|PubMed:16629670,
CC ECO:0000269|PubMed:23605043}.
CC -!- SIMILARITY: Belongs to the RNA polymerase-binding protein RbpA family.
CC {ECO:0000255|HAMAP-Rule:MF_01483}.
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DR EMBL; AL939108; CAB61670.1; -; Genomic_DNA.
DR RefSeq; NP_625703.1; NC_003888.3.
DR RefSeq; WP_003977404.1; NZ_VNID01000029.1.
DR PDB; 2M6O; NMR; -; A=28-75.
DR PDBsum; 2M6O; -.
DR AlphaFoldDB; Q9RKY0; -.
DR BMRB; Q9RKY0; -.
DR SMR; Q9RKY0; -.
DR STRING; 100226.SCO1421; -.
DR GeneID; 1096847; -.
DR GeneID; 24307678; -.
DR KEGG; sco:SCO1421; -.
DR PATRIC; fig|100226.15.peg.1431; -.
DR eggNOG; ENOG5032SI2; Bacteria.
DR HOGENOM; CLU_134276_0_0_11; -.
DR InParanoid; Q9RKY0; -.
DR OMA; VWECRCG; -.
DR PhylomeDB; Q9RKY0; -.
DR PRO; PR:Q9RKY0; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0001000; F:bacterial-type RNA polymerase core enzyme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001108; F:bacterial-type RNA polymerase holo enzyme binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 2.20.28.270; -; 1.
DR HAMAP; MF_01483; RbpA; 1.
DR InterPro; IPR038638; RbpA_sf.
DR InterPro; IPR025182; RNApol-bd_RbpA.
DR Pfam; PF13397; RbpA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing;
KW Metal-binding; Reference proteome; Transcription; Transcription regulation;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11737643"
FT CHAIN 2..124
FT /note="RNA polymerase-binding protein RbpA"
FT /id="PRO_0000423657"
FT REGION 73..124
FT /note="Sufficient for interaction with HrdB (SigA)"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01483"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT MUTAGEN 34
FT /note="C->A: Colonies remain small."
FT /evidence="ECO:0000269|PubMed:23605043"
FT MUTAGEN 38
FT /note="H->A: Restores wild-type size colonies."
FT /evidence="ECO:0000269|PubMed:23605043"
FT MUTAGEN 56
FT /note="C->A: Colonies remain small."
FT /evidence="ECO:0000269|PubMed:23605043"
FT MUTAGEN 59
FT /note="C->A: Colonies remain small."
FT /evidence="ECO:0000269|PubMed:23605043"
FT MUTAGEN 82
FT /note="H->A: Restores wild-type size colonies."
FT /evidence="ECO:0000269|PubMed:23605043"
FT MUTAGEN 88..89
FT /note="ER->AA: Loss of binding to HrdB (SigA), colonies
FT remain small, does not stimulate transcription."
FT MUTAGEN 88
FT /note="E->A: Increased binding to HrdB (SigA), restores
FT wild-type size colonies."
FT /evidence="ECO:0000269|PubMed:23605043"
FT MUTAGEN 89
FT /note="R->A: 25% binding to HrdB (SigA), nearly wild-type
FT size colonies."
FT /evidence="ECO:0000269|PubMed:23605043"
FT MUTAGEN 90
FT /note="R->A: 50% binding to HrdB (SigA), nearly wild-type
FT size colonies."
FT /evidence="ECO:0000269|PubMed:23605043"
FT MUTAGEN 116
FT /note="H->A: Restores wild-type size colonies."
FT /evidence="ECO:0000269|PubMed:23605043"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2M6O"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2M6O"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2M6O"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:2M6O"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2M6O"
SQ SEQUENCE 124 AA; 14123 MW; FCE40C099384DD12 CRC64;
MSERALRGTR LVVTSYETDR GIDLAPRQAV EYACEKGHRF EMPFSVEAEI PPEWECKVCG
AQALLVDGDG PEEKKAKPAR THWDMLMERR TREELEEVLE ERLAVLRSGA MNIAVHPRDS
RKSA
