RSBW_MYCTU
ID RSBW_MYCTU Reviewed; 168 AA.
AC P9WGX7; Q798J8; Q7D5S1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Anti-sigma-F factor RsbW;
DE AltName: Full=Anti-sigma-F factor UsfX;
DE AltName: Full=Regulator of SigF;
DE AltName: Full=Sigma-F anti-sigma factor RsbW;
GN Name=rsbW; Synonyms=usfX; OrderedLocusNames=Rv3287c;
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 SEQUENCE REVISION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12368430; DOI=10.1099/00221287-148-10-2967;
RA Camus J.-C., Pryor M.J., Medigue C., Cole S.T.;
RT "Re-annotation of the genome sequence of Mycobacterium tuberculosis
RT H37Rv.";
RL Microbiology 148:2967-2973(2002).
RN [3]
RP INDUCTION FOLLOWING STARVATION.
RC STRAIN=ATCC 25618 / H37Rv / NCTC 7416;
RX PubMed=11929527; DOI=10.1046/j.1365-2958.2002.02779.x;
RA Betts J.C., Lukey P.T., Robb L.C., McAdam R.A., Duncan K.;
RT "Evaluation of a nutrient starvation model of Mycobacterium tuberculosis
RT persistence by gene and protein expression profiling.";
RL Mol. Microbiol. 43:717-731(2002).
RN [4]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, AND INTERACTION WITH SIGF; RSFA AND RSFB.
RX PubMed=12354223; DOI=10.1046/j.1365-2958.2002.03135.x;
RA Beaucher J., Rodrigue S., Jacques P.E., Smith I., Brzezinski R.,
RA Gaudreau L.;
RT "Novel Mycobacterium tuberculosis anti-sigma factor antagonists control
RT sigmaF activity by distinct mechanisms.";
RL Mol. Microbiol. 45:1527-1540(2002).
RN [5]
RP POSSIBLE NUCLEOTIDE HYDROLYSIS, SUBUNIT, AND NUCLEOTIDE-BINDING.
RX PubMed=18722345; DOI=10.1016/j.bbrc.2008.08.043;
RA Malik S.S., Luthra A., Srivastava S.K., Ramachandran R.;
RT "Mycobacterium tuberculosis UsfX (Rv3287c) exhibits novel nucleotide
RT binding and hydrolysis properties.";
RL Biochem. Biophys. Res. Commun. 375:465-470(2008).
RN [6]
RP SUBUNIT, AND INTERACTION WITH SIGF AND RSFA.
RX PubMed=19130906; DOI=10.1016/j.bbapap.2008.11.007;
RA Malik S.S., Luthra A., Ramachandran R.;
RT "Interactions of the M. tuberculosis UsfX with the cognate sigma factor
RT SigF and the anti-anti sigma factor RsfA.";
RL Biochim. Biophys. Acta 1794:541-553(2009).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20729364; DOI=10.1128/jb.00687-10;
RA Hartkoorn R.C., Sala C., Magnet S.J., Chen J.M., Pojer F., Cole S.T.;
RT "Sigma factor F does not prevent rifampin inhibition of RNA polymerase or
RT cause rifampin tolerance in Mycobacterium tuberculosis.";
RL J. Bacteriol. 192:5472-5479(2010).
RN [8]
RP INTERACTION WITH SIGF.
RX PubMed=20600947; DOI=10.1016/j.pep.2010.06.018;
RA Thakur K.G., Jaiswal R.K., Shukla J.K., Praveena T., Gopal B.;
RT "Over-expression and purification strategies for recombinant multi-protein
RT oligomers: a case study of Mycobacterium tuberculosis sigma/anti-sigma
RT factor protein complexes.";
RL Protein Expr. Purif. 74:223-230(2010).
RN [9]
RP INTERACTION WITH OBG.
RC STRAIN=H37Rv;
RX PubMed=21352546; DOI=10.1186/1471-2180-11-43;
RA Sasindran S.J., Saikolappan S., Scofield V.L., Dhandayuthapani S.;
RT "Biochemical and physiological characterization of the GTP-binding protein
RT Obg of Mycobacterium tuberculosis.";
RL BMC Microbiol. 11:43-43(2011).
RN [10]
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).
CC -!- FUNCTION: A cognate anti-sigma factor for alternative sigma factor
CC SigF. Alternative sigma factors are held in an inactive form by an
CC anti-sigma factor. Binds ATP and GTP, may hydrolyze both.
CC {ECO:0000269|PubMed:12354223}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with cognate RNA polymerase
CC sigma factor SigF with a possible 2:1 RbsW:SigF stoichiometry; this
CC inhibits the interaction of SigF with the RNA polymerase catalytic
CC core. Interacts with anti-sigma-F factor antagonist RsfA with a
CC possible 2:1 RbsW:RsfA stoichiometry; this blocks binding to SigF, thus
CC indirectly activating transcription. Interacts with GTPase Obg
CC (PubMed:21352546). {ECO:0000269|PubMed:12354223,
CC ECO:0000269|PubMed:18722345, ECO:0000269|PubMed:19130906,
CC ECO:0000269|PubMed:20600947, ECO:0000269|PubMed:21352546, ECO:0000305}.
CC -!- INDUCTION: 9-fold induced by starvation. {ECO:0000269|PubMed:11929527}.
CC -!- DOMAIN: The cytosolic domain interacts with sigma factor SigF.
CC -!- DISRUPTION PHENOTYPE: A double rsbW-sigF disruption shows no effect in
CC the presence or absence of rifampicin. {ECO:0000269|PubMed:20729364}.
CC -!- SIMILARITY: Belongs to the anti-sigma-factor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP46106.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
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DR EMBL; AL123456; CCP46106.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_217804.4; NC_000962.3.
DR AlphaFoldDB; P9WGX7; -.
DR SMR; P9WGX7; -.
DR IntAct; P9WGX7; 6.
DR STRING; 83332.Rv3287c; -.
DR PaxDb; P9WGX7; -.
DR DNASU; 887977; -.
DR GeneID; 887977; -.
DR KEGG; mtu:Rv3287c; -.
DR TubercuList; Rv3287c; -.
DR eggNOG; COG2172; Bacteria.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IDA:MTBBASE.
DR GO; GO:0016989; F:sigma factor antagonist activity; IDA:MTBBASE.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MTBBASE.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..168
FT /note="Anti-sigma-F factor RsbW"
FT /id="PRO_0000422955"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 168 AA; 17928 MW; D1E729A26DFD765E CRC64;
MTDQLEDQTQ GGSTVDRSLP GGCMADSDLP TKGRQRGVRA VELNVAARLE NLALLRTLVG
AIGTFEDLDF DAVADLRLAV DEVCTRLIRS ALPDATLRLV VDPRKDEVVV EASAACDTHD
VVAPGSFSWH VLTALADDVQ TFHDGRQPDV AGSVFGITLT ARRAASSR
