RBPA_MYCTU
ID RBPA_MYCTU Reviewed; 111 AA.
AC P9WHJ5; L7N5Z6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=RNA polymerase-binding protein RbpA {ECO:0000255|HAMAP-Rule:MF_01483};
GN Name=rbpA {ECO:0000255|HAMAP-Rule:MF_01483}; OrderedLocusNames=Rv2050;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21840262; DOI=10.1016/j.tube.2011.07.004;
RA Forti F., Mauri V., Deho G., Ghisotti D.;
RT "Isolation of conditional expression mutants in Mycobacterium tuberculosis
RT by transposon mutagenesis.";
RL Tuberculosis 91:569-578(2011).
RN [4]
RP FUNCTION, INTERACTION WITH RPOB, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22570422; DOI=10.1093/nar/gks346;
RA Hu Y., Morichaud Z., Chen S., Leonetti J.P., Brodolin K.;
RT "Mycobacterium tuberculosis RbpA protein is a new type of transcriptional
RT activator that stabilizes the sigma A-containing RNA polymerase
RT holoenzyme.";
RL Nucleic Acids Res. 40:6547-6557(2012).
RN [5]
RP STRUCTURE BY NMR OF 1-79, INTERACTION WITH SIGB, SUBUNIT, BIOTECHNOLOGY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=23548911; DOI=10.1074/jbc.m113.459883;
RA Bortoluzzi A., Muskett F.W., Waters L.C., Addis P.W., Rieck B., Munder T.,
RA Schleier S., Forti F., Ghisotti D., Carr M.D., O'Hare H.M.;
RT "Mycobacterium tuberculosis RNA polymerase-binding protein A (RbpA) and its
RT interactions with sigma factors.";
RL J. Biol. Chem. 288:14438-14450(2013).
RN [6]
RP STRUCTURE BY NMR OF 26-71, AND SUBUNIT.
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 and stabilizing
CC the formation of stable RNAP promoter complexes up to 2-fold from
CC principal sigma factor SigA-dependent but not alternative sigma factor
CC SigF-dependent promoters. Increases the affinity of core RNAP for SigA,
CC increasing the transcriptional activity of RNAP. Unlike the case in
CC M.smegmatis or S.coelicolor, has no effect on rifampicin inhibition of
CC transcription. Has no effect on E.coli RNAP.
CC {ECO:0000269|PubMed:22570422}.
CC -!- SUBUNIT: Oligomerizes at more than 3 uM; this requires the C-terminal
CC 32 residues. Forms a complex with the RNAP catalytic core, specifically
CC with the beta subunit (rpoB). Interacts with free SigB, probably as a
CC 1:1 complex, and also with free SigA, probably via its sigma-2 domain.
CC {ECO:0000269|PubMed:22570422, ECO:0000269|PubMed:23548911,
CC ECO:0000269|PubMed:23605043}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted.
CC {ECO:0000269|PubMed:21840262, ECO:0000269|PubMed:23548911}.
CC -!- BIOTECHNOLOGY: This protein is only found in actinomycetes; as it is
CC essential in M.tuberculosis, it might make a potential drug target.
CC {ECO:0000269|PubMed:23548911}.
CC -!- SIMILARITY: Belongs to the RNA polymerase-binding protein RbpA family.
CC {ECO:0000255|HAMAP-Rule:MF_01483}.
CC -!- CAUTION: Unlike its ortholog in S.coelicolor, it is not seen to bind
CC zinc. {ECO:0000305|PubMed:23605043}.
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DR EMBL; AL123456; CCP44823.1; -; Genomic_DNA.
DR PIR; A70945; A70945.
DR RefSeq; NP_216566.1; NC_000962.3.
DR RefSeq; WP_003410601.1; NZ_NVQJ01000047.1.
DR PDB; 2M4V; NMR; -; A=1-79.
DR PDB; 2M6P; NMR; -; A=26-71.
DR PDB; 4X8K; X-ray; 2.20 A; B=23-111.
DR PDB; 6BZO; EM; 3.38 A; J=1-111.
DR PDB; 6C04; EM; 3.27 A; J=1-111.
DR PDB; 6C05; EM; 5.15 A; J=1-111.
DR PDB; 6C06; EM; 5.15 A; J=1-111.
DR PDB; 6EDT; EM; -; J=1-111.
DR PDB; 6EE8; EM; 3.92 A; J=1-111.
DR PDB; 6EEC; EM; 3.55 A; J=1-111.
DR PDB; 6M7J; EM; 4.40 A; J=1-111.
DR PDB; 6VVX; EM; 3.39 A; J=1-111.
DR PDB; 6VVY; EM; 3.42 A; J=1-111.
DR PDB; 6VVZ; EM; 3.72 A; J=1-111.
DR PDB; 6VW0; EM; 3.59 A; J=1-111.
DR PDB; 7KIF; EM; 2.94 A; J=1-111.
DR PDB; 7KIM; EM; 3.38 A; J=1-111.
DR PDB; 7KIN; EM; 2.74 A; J=1-111.
DR PDBsum; 2M4V; -.
DR PDBsum; 2M6P; -.
DR PDBsum; 4X8K; -.
DR PDBsum; 6BZO; -.
DR PDBsum; 6C04; -.
DR PDBsum; 6C05; -.
DR PDBsum; 6C06; -.
DR PDBsum; 6EDT; -.
DR PDBsum; 6EE8; -.
DR PDBsum; 6EEC; -.
DR PDBsum; 6M7J; -.
DR PDBsum; 6VVX; -.
DR PDBsum; 6VVY; -.
DR PDBsum; 6VVZ; -.
DR PDBsum; 6VW0; -.
DR PDBsum; 7KIF; -.
DR PDBsum; 7KIM; -.
DR PDBsum; 7KIN; -.
DR AlphaFoldDB; P9WHJ5; -.
DR BMRB; P9WHJ5; -.
DR SMR; P9WHJ5; -.
DR IntAct; P9WHJ5; 6.
DR STRING; 83332.Rv2050; -.
DR PaxDb; P9WHJ5; -.
DR DNASU; 888598; -.
DR GeneID; 45426029; -.
DR GeneID; 888598; -.
DR KEGG; mtu:Rv2050; -.
DR TubercuList; Rv2050; -.
DR eggNOG; ENOG5031DSU; Bacteria.
DR OMA; VWECRCG; -.
DR PhylomeDB; P9WHJ5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR DisProt; DP00791; -.
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; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..111
FT /note="RNA polymerase-binding protein RbpA"
FT /id="PRO_0000423656"
FT REGION 1..24
FT /note="Not required for interaction with SigB"
FT REGION 80..111
FT /note="Required for oligomerization and to complement a
FT conditional disruption mutant"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6BZO"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:4X8K"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:4X8K"
SQ SEQUENCE 111 AA; 12972 MW; EF75746152BB5CEB CRC64;
MADRVLRGSR LGAVSYETDR NHDLAPRQIA RYRTDNGEEF EVPFADDAEI PGTWLCRNGM
EGTLIEGDLP EPKKVKPPRT HWDMLLERRS IEELEELLKE RLELIRSRRR G
