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Anti-sigma factor RshA (Regulator of SigH) (Sigma-H anti-sigma factor RshA)

 RSHA_MYCTU              Reviewed;         101 AA.
P9WJ69; F2GK95; Q6MWZ6; Q8VJ46;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 21.
RecName: Full=Anti-sigma factor RshA;
AltName: Full=Regulator of SigH;
AltName: Full=Sigma-H anti-sigma factor RshA;
Name=rshA; OrderedLocusNames=Rv3221A;
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]
PROTEIN SEQUENCE OF 1-89, COFACTOR, AND INTERACTION WITH SIGH.
STRAIN=ATCC 25618 / H37Rv;
PubMed=22937074; DOI=10.1371/journal.pone.0043676;
Kumar S., Badireddy S., Pal K., Sharma S., Arora C., Garg S.K.,
Alam M.S., Agrawal P., Anand G.S., Swaminathan K.;
"Interaction of Mycobacterium tuberculosis RshA and SigH is mediated
by salt bridges.";
PLoS ONE 7:E43676-E43676(2012).
[3]
IDENTIFICATION.
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).
[4]
FUNCTION AS AN ANTI-SIGMA FACTOR, INTERACTION WITH SIGH, AND
INDUCTION.
PubMed=14617153; DOI=10.1046/j.1365-2958.2003.03739.x;
Song T., Dove S.L., Lee K.H., Husson R.N.;
"RshA, an anti-sigma factor that regulates the activity of the
mycobacterial stress response sigma factor SigH.";
Mol. Microbiol. 50:949-959(2003).
[5]
FUNCTION AS AN ANTI-SIGMA FACTOR, BINDING AFFINITY, AND SUBUNIT.
PubMed=16298337; DOI=10.1016/j.bbrc.2005.11.032;
Jeong E.H., Son Y.M., Hah Y.S., Choi Y.J., Lee K.H., Song T.,
Kim D.R.;
"RshA mimetic peptides inhibiting the transcription driven by a
Mycobacterium tuberculosis sigma factor SigH.";
Biochem. Biophys. Res. Commun. 339:392-398(2006).
[6]
PHOSPHORYLATION AT THR-94, INTERACTION WITH SIGH, REGULATION, AND
MUTAGENESIS OF THR-94.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18728196; DOI=10.1073/pnas.0801143105;
Park S.T., Kang C.M., Husson R.N.;
"Regulation of the SigH stress response regulon by an essential
protein kinase in Mycobacterium tuberculosis.";
Proc. Natl. Acad. Sci. U.S.A. 105:13105-13110(2008).
[7]
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: An redox-regulated anti-sigma factor for
extracytoplasmic function (ECF) sigma factor SigH. ECF sigma
factors are held in an inactive form by a cognate anti-sigma
factor. RshA and some peptides derived from it inhibit the sigma
factor activity of SigH. Probably releases SigH during oxidative
stress. {ECO:0000269|PubMed:14617153,
ECO:0000269|PubMed:16298337}.
-!- COFACTOR:
Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
Evidence={ECO:0000269|PubMed:22937074, ECO:0000305};
Note=Binds 1 iron-sulfur cluster per subunit. As the iron-sulfur
cluster is unstable, it is not clear from the contradictory
experimental evidence whether it is 2Fe-2S, 4Fe-4S or something
intermediate. Nor is it clear which other residues besides Cys-53
and Cys-56 are involved in metal binding (PubMed:22937074).
{ECO:0000269|PubMed:22937074, ECO:0000305};
-!- SUBUNIT: Interacts (affinity=15 nM) 1:1 with cognate sigma factor
SigH under reducing conditions; the complex is disrupted under
oxiding conditions or as temperatures rise. Binding inhibits the
interaction of SigH with the RNA polymerase catalytic core.
{ECO:0000269|PubMed:14617153, ECO:0000269|PubMed:16298337,
ECO:0000269|PubMed:18728196, ECO:0000269|PubMed:22937074}.
-!- INDUCTION: By SigH, part of the sigH-rshA operon.
{ECO:0000269|PubMed:14617153}.
-!- PTM: Phosphorylated, probably by PknB. Phosphorylation decreases
interaction with SigH, leading to increased SigH-mediated
transcription. {ECO:0000269|PubMed:18728196}.
-!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
superfamily. {ECO:0000305}.
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EMBL; AL123456; CCP46038.1; -; Genomic_DNA.
RefSeq; WP_003416891.1; NZ_KK339370.1.
RefSeq; YP_177945.1; NC_000962.3.
ProteinModelPortal; P9WJ69; -.
IntAct; P9WJ69; 2.
STRING; 83332.Rv3221A; -.
iPTMnet; P9WJ69; -.
PaxDb; P9WJ69; -.
EnsemblBacteria; CCP46038; CCP46038; Rv3221A.
GeneID; 3205091; -.
KEGG; mtu:Rv3221A; -.
TubercuList; Rv3221A; -.
OMA; PCLEKYG; -.
PhylomeDB; P9WJ69; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016989; F:sigma factor antagonist activity; IDA:MTBBASE.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0009408; P:response to heat; IDA:MTBBASE.
GO; GO:0006979; P:response to oxidative stress; IDA:MTBBASE.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR024020; Anit_sigma_mycothiol_RsrA.
InterPro; IPR014295; Anti-sigma.
InterPro; IPR027383; Znf_put.
Pfam; PF13490; zf-HC2; 1.
TIGRFAMs; TIGR02949; anti_SigH_actin; 1.
TIGRFAMs; TIGR03988; antisig_RsrA; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Iron; Iron-sulfur;
Metal-binding; Phosphoprotein; Reference proteome; Stress response;
Transcription; Transcription regulation.
CHAIN 1 101 Anti-sigma factor RshA.
/FTId=PRO_0000423650.
REGION 9 15 Inhibits SigH sigma factor activity.
REGION 28 34 Inhibits SigH sigma factor activity.
REGION 38 44 Inhibits SigH sigma factor activity.
METAL 23 23 Iron-sulfur. {ECO:0000255}.
METAL 49 49 Iron-sulfur. {ECO:0000255}.
METAL 53 53 Iron-sulfur. {ECO:0000305}.
METAL 56 56 Iron-sulfur. {ECO:0000305}.
MOD_RES 94 94 Phosphothreonine.
{ECO:0000269|PubMed:18728196}.
MUTAGEN 94 94 T->A: No in vitro phosphorylation by
PknB. {ECO:0000269|PubMed:18728196}.
SEQUENCE 101 AA; 11290 MW; 36636191A0D86341 CRC64;
MSENCGPTDA HADHDDSHGG MGCAEVIAEV WTLLDGECTP ETRERLRRHL EACPGCLRHY
GLEERIKALI GTKCRGDRAP EGLRERLRLE IRRTTIIRGG P


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