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Anti-sigma-F factor RsbW (Anti-sigma-F factor UsfX) (Regulator of SigF) (Sigma-F anti-sigma factor RsbW)

 RSBW_MYCTU              Reviewed;         168 AA.
P9WGX7; Q798J8; Q7D5S1;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
02-NOV-2016, sequence version 2.
08-MAY-2019, entry version 28.
RecName: Full=Anti-sigma-F factor RsbW;
AltName: Full=Anti-sigma-F factor UsfX;
AltName: Full=Regulator of SigF;
AltName: Full=Sigma-F anti-sigma factor RsbW;
Name=rsbW; Synonyms=usfX; OrderedLocusNames=Rv3287c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
SEQUENCE REVISION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12368430;
Camus J.-C., Pryor M.J., Medigue C., Cole S.T.;
"Re-annotation of the genome sequence of Mycobacterium tuberculosis
H37Rv.";
Microbiology 148:2967-2973(2002).
[3]
INDUCTION FOLLOWING STARVATION.
STRAIN=ATCC 25618 / H37Rv / NCTC 7416;
PubMed=11929527; DOI=10.1046/j.1365-2958.2002.02779.x;
Betts J.C., Lukey P.T., Robb L.C., McAdam R.A., Duncan K.;
"Evaluation of a nutrient starvation model of Mycobacterium
tuberculosis persistence by gene and protein expression profiling.";
Mol. Microbiol. 43:717-731(2002).
[4]
FUNCTION AS AN ANTI-SIGMA FACTOR, AND INTERACTION WITH SIGF; RSFA AND
RSFB.
PubMed=12354223; DOI=10.1046/j.1365-2958.2002.03135.x;
Beaucher J., Rodrigue S., Jacques P.E., Smith I., Brzezinski R.,
Gaudreau L.;
"Novel Mycobacterium tuberculosis anti-sigma factor antagonists
control sigmaF activity by distinct mechanisms.";
Mol. Microbiol. 45:1527-1540(2002).
[5]
POSSIBLE NUCLEOTIDE HYDROLYSIS, SUBUNIT, AND NUCLEOTIDE-BINDING.
PubMed=18722345; DOI=10.1016/j.bbrc.2008.08.043;
Malik S.S., Luthra A., Srivastava S.K., Ramachandran R.;
"Mycobacterium tuberculosis UsfX (Rv3287c) exhibits novel nucleotide
binding and hydrolysis properties.";
Biochem. Biophys. Res. Commun. 375:465-470(2008).
[6]
SUBUNIT, AND INTERACTION WITH SIGF AND RSFA.
PubMed=19130906; DOI=10.1016/j.bbapap.2008.11.007;
Malik S.S., Luthra A., Ramachandran R.;
"Interactions of the M. tuberculosis UsfX with the cognate sigma
factor SigF and the anti-anti sigma factor RsfA.";
Biochim. Biophys. Acta 1794:541-553(2009).
[7]
DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20729364; DOI=10.1128/JB.00687-10;
Hartkoorn R.C., Sala C., Magnet S.J., Chen J.M., Pojer F., Cole S.T.;
"Sigma factor F does not prevent rifampin inhibition of RNA polymerase
or cause rifampin tolerance in Mycobacterium tuberculosis.";
J. Bacteriol. 192:5472-5479(2010).
[8]
INTERACTION WITH SIGF.
PubMed=20600947; DOI=10.1016/j.pep.2010.06.018;
Thakur K.G., Jaiswal R.K., Shukla J.K., Praveena T., Gopal B.;
"Over-expression and purification strategies for recombinant multi-
protein oligomers: a case study of Mycobacterium tuberculosis
sigma/anti-sigma factor protein complexes.";
Protein Expr. Purif. 74:223-230(2010).
[9]
INTERACTION WITH OBG.
STRAIN=H37Rv;
PubMed=21352546; DOI=10.1186/1471-2180-11-43;
Sasindran S.J., Saikolappan S., Scofield V.L., Dhandayuthapani S.;
"Biochemical and physiological characterization of the GTP-binding
protein Obg of Mycobacterium tuberculosis.";
BMC Microbiol. 11:43-43(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- FUNCTION: A cognate anti-sigma factor for alternative sigma factor
SigF. Alternative sigma factors are held in an inactive form by an
anti-sigma factor. Binds ATP and GTP, may hydrolyze both.
{ECO:0000269|PubMed:12354223}.
-!- SUBUNIT: Homodimer (Probable). Interacts with cognate RNA
polymerase sigma factor SigF with a possible 2:1 RbsW:SigF
stoichiometry; this inhibits the interaction of SigF with the RNA
polymerase catalytic core. Interacts with anti-sigma-F factor
antagonist RsfA with a possible 2:1 RbsW:RsfA stoichiometry; this
blocks binding to SigF, thus indirectly activating transcription.
Interacts with GTPase Obg (PubMed:21352546).
{ECO:0000269|PubMed:12354223, ECO:0000269|PubMed:18722345,
ECO:0000269|PubMed:19130906, ECO:0000269|PubMed:20600947,
ECO:0000269|PubMed:21352546, ECO:0000305}.
-!- INDUCTION: 9-fold induced by starvation.
{ECO:0000269|PubMed:11929527}.
-!- DOMAIN: The cytosolic domain interacts with sigma factor SigF.
-!- DISRUPTION PHENOTYPE: A double rsbW-sigF disruption shows no
effect in the presence or absence of rifampicin.
{ECO:0000269|PubMed:20729364}.
-!- SIMILARITY: Belongs to the anti-sigma-factor family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CCP46106.1; Type=Erroneous initiation; Note=Translation N-terminally extended.;
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EMBL; AL123456; CCP46106.1; ALT_INIT; Genomic_DNA.
RefSeq; NP_217804.4; NC_000962.3.
SMR; P9WGX7; -.
IntAct; P9WGX7; 6.
STRING; 83332.Rv3287c; -.
PaxDb; P9WGX7; -.
EnsemblBacteria; CCP46106; CCP46106; Rv3287c.
GeneID; 887977; -.
KEGG; mtu:Rv3287c; -.
TubercuList; Rv3287c; -.
eggNOG; ENOG4105XVZ; Bacteria.
eggNOG; COG2172; LUCA.
PhylomeDB; P9WGX7; -.
BioCyc; MTBH37RV:G185E-7561-MONOMER; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IDA:MTBBASE.
GO; GO:0016989; F:sigma factor antagonist activity; IDA:MTBBASE.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MTBBASE.
1: Evidence at protein level;
ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 168 Anti-sigma-F factor RsbW.
/FTId=PRO_0000422955.
NP_BIND 124 128 ATP. {ECO:0000255}.
SEQUENCE 168 AA; 17928 MW; D1E729A26DFD765E CRC64;
MTDQLEDQTQ GGSTVDRSLP GGCMADSDLP TKGRQRGVRA VELNVAARLE NLALLRTLVG
AIGTFEDLDF DAVADLRLAV DEVCTRLIRS ALPDATLRLV VDPRKDEVVV EASAACDTHD
VVAPGSFSWH VLTALADDVQ TFHDGRQPDV AGSVFGITLT ARRAASSR


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[MPR1] N-acetyltransferase MPR1 (EC 2.3.1.271) ((S)-1-pyrroline-5-carboxylate acetyltransferase) (L-azetidine-2-carboxylate acetyltransferase) (AZC acetyltransferase) (Sigma1278b gene for proline-analog resistance 1)
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[csfB gin yaaM BSU00240] Anti-sigma-G factor Gin (Protein CsfB)
[GCN4 AAS3 ARG9 YEL009C] General control protein GCN4 (Amino acid biosynthesis regulatory protein)
[rseA STM14_3233] Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA) (Sigma-E factor negative regulatory protein)
[FLO11 MAL5 MUC1 S1 S2 YIR019C] Flocculation protein FLO11 (Flo11p) (Flocculin-11) (Mucin-like protein 1)
[rpoE sigE b2573 JW2557] ECF RNA polymerase sigma-E factor (RNA polymerase sigma-E factor) (Sigma-24)
[NPR1 YNL183C N1631] Nitrogen permease reactivator protein (EC 2.7.11.1) (Serine/threonine-protein kinase NPR1)
[GPB2 KRH1 YAL056W] Guanine nucleotide-binding protein subunit beta 2 (Gbeta mimic kelch protein 2)
[CWP1 YKL096W YJU1 YKL443] Cell wall protein CWP1 (Glycoprotein GP40)
[ARO9 YHR137W] Aromatic amino acid aminotransferase 2 (EC 2.6.1.57) (Aromatic amino acid aminotransferase II) (Aromatic amino acid-requiring protein 9) (Kynurenine aminotransferase I) (KAT I) (EC 2.6.1.7)
[rpoH fam hin htpR b3461 JW3426] RNA polymerase sigma factor RpoH (Heat shock regulatory protein F33.4) (RNA polymerase sigma-32 factor)
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