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ECF RNA polymerase sigma factor SigH (ECF sigma factor SigH) (Alternative RNA polymerase sigma factor SigH) (RNA polymerase sigma-H factor) (Sigma-H factor)

 SIGH_MYCTU              Reviewed;         216 AA.
P9WGH9; L0TEP5; O05843; P66807;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-NOV-2018, entry version 27.
RecName: Full=ECF RNA polymerase sigma factor SigH;
Short=ECF sigma factor SigH;
AltName: Full=Alternative RNA polymerase sigma factor SigH;
AltName: Full=RNA polymerase sigma-H factor;
Short=Sigma-H factor;
Name=sigH; Synonyms=rpoE; OrderedLocusNames=Rv3223c;
ORFNames=MTCY07D11.03;
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 1-25; 3-44; 46-69 AND 90-196, AND INTERACTION WITH
RSHA.
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]
INDUCTION BY HEAT SHOCK.
STRAIN=ATCC 25618 / H37Rv;
PubMed=10027986; DOI=10.1046/j.1365-2958.1999.01212.x;
Manganelli R., Dubnau E., Tyagi S., Kramer F.R., Smith I.;
"Differential expression of 10 sigma factor genes in Mycobacterium
tuberculosis.";
Mol. Microbiol. 31:715-724(1999).
[4]
FUNCTION AS A SIGMA FACTOR, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11567012; DOI=10.1128/JB.183.20.6119-6125.2001;
Raman S., Song T., Puyang X., Bardarov S., Jacobs W.R. Jr.,
Husson R.N.;
"The alternative sigma factor SigH regulates major components of
oxidative and heat stress responses in Mycobacterium tuberculosis.";
J. Bacteriol. 183:6119-6125(2001).
[5]
FUNCTION, REGULON, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12123450; DOI=10.1046/j.1365-2958.2002.03005.x;
Manganelli R., Voskuil M.I., Schoolnik G.K., Dubnau E., Gomez M.,
Smith I.;
"Role of the extracytoplasmic-function sigma factor sigma(H) in
Mycobacterium tuberculosis global gene expression.";
Mol. Microbiol. 45:365-374(2002).
[6]
FUNCTION AS A SIGMA FACTOR, AND INTERACTION WITH RSHA.
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).
[7]
FUNCTION AS A 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).
[8]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[9]
REGULATION, INTERACTION WITH RSHA, PHOSPHORYLATION, AND MUTAGENESIS OF
THR-26 AND THR-106.
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).
[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: Sigma factors are initiation factors that promote the
attachment of RNA polymerase to specific initiation sites and are
then released. Extracytoplasmic function (ECF) sigma factors are
held in an inactive form by a cognate anti-sigma factor (RshA)
until released. This sigma factor is involved in heat shock and
oxidative stress responses; it positively regulates the expression
of itself, sigE, sigB and a number of transcriptional regulators
as well as other effectors of heat and oxidative stress, leading
to direct and indirect control of up to 25% of the bacterial
genome. Modulates expression of host genes for intercrine beta
(chemokine CC) and apoptosis, altering the host immune response.
{ECO:0000269|PubMed:11567012, ECO:0000269|PubMed:12123450,
ECO:0000269|PubMed:14617153, ECO:0000269|PubMed:16298337}.
-!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic
core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta'
and 1 omega subunit) to form the RNA polymerase holoenzyme that
can initiate transcription. Interacts (affinity=15 nM) 1:1 (via
sigma-70 factor domain-4) with RshA under reducing conditions; the
complex is disrupted as temperatures rise. Phosphorylation of RshA
decreases its interaction with SigH, leading to increased SigH-
mediated transcription. {ECO:0000269|PubMed:14617153,
ECO:0000269|PubMed:16298337, ECO:0000269|PubMed:18728196,
ECO:0000269|PubMed:22937074}.
-!- INDUCTION: Poorly expressed in exponential phase; induced by heat
shock (20-fold, 45 degrees Celsius). Induced 10-fold by the thiol-
oxidative agent diamide within 30 minutes of exposure, by 2 hours
expression is again normal. Autoregulates its own expression, part
of the sigH-rshA operon. {ECO:0000269|PubMed:10027986,
ECO:0000269|PubMed:12123450}.
-!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific
interaction with the -10 element in promoter DNA, and plays an
important role in melting the double-stranded DNA and the
formation of the transcription bubble. The sigma-70 factor domain-
2 mediates interaction with the RNA polymerase subunits RpoB and
RpoC (By similarity). {ECO:0000250}.
-!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix
(H-T-H) motif that mediates interaction with the -35 element in
promoter DNA. The domain also mediates interaction with the RNA
polymerase subunit RpoA. Interactions between sigma-70 factor
domain-4 and anti-sigma factors prevents interaction of sigma
factors with the RNA polymerase catalytic core.
-!- PTM: Phosphorylated, possibly on 2 residues, probably by PknB.
Phosphorylation of SigH has no effect on interaction with RshA.
{ECO:0000269|PubMed:18728196}.
-!- DISRUPTION PHENOTYPE: Increased susceptibility to oxidative stress
(H(2)O(2), cumene hydroperoxide and diamide, PubMed:12123450) and
heat shock (45 and 52 degrees Celsius). Loss of stress-induced
expression of a number of genes including clpB, dnaK, sigE and
trxB (PubMed:11567012), sigB and itself (PubMed:12123450). No
effect on infection of human derived macrophages, and murine
J774.1 activated and unactivated macrophages (PubMed:12123450).
{ECO:0000269|PubMed:11567012, ECO:0000269|PubMed:12123450}.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
-!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
{ECO:0000305}.
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EMBL; AL123456; CCP46040.1; -; Genomic_DNA.
PIR; H70596; H70596.
RefSeq; NP_217739.1; NC_000962.3.
RefSeq; WP_003416897.1; NZ_NVQJ01000003.1.
ProteinModelPortal; P9WGH9; -.
SMR; P9WGH9; -.
IntAct; P9WGH9; 2.
STRING; 83332.Rv3223c; -.
PaxDb; P9WGH9; -.
EnsemblBacteria; CCP46040; CCP46040; Rv3223c.
GeneID; 888094; -.
KEGG; mtu:Rv3223c; -.
KEGG; mtv:RVBD_3223c; -.
PATRIC; fig|83332.111.peg.3600; -.
TubercuList; Rv3223c; -.
eggNOG; ENOG4105EMN; Bacteria.
eggNOG; COG1595; LUCA.
KO; K03088; -.
OMA; TYINLYR; -.
PhylomeDB; P9WGH9; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
GO; GO:0034605; P:cellular response to heat; IMP:MTBBASE.
GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
GO; GO:0009408; P:response to heat; IMP:MTBBASE.
GO; GO:0051409; P:response to nitrosative stress; IMP:MTBBASE.
GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR039425; RNA_pol_sigma-70.
InterPro; IPR014284; RNA_pol_sigma-70_dom.
InterPro; IPR014293; RNA_pol_sigma70_actinobac.
InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
InterPro; IPR007627; RNA_pol_sigma70_r2.
InterPro; IPR013249; RNA_pol_sigma70_r4_t2.
InterPro; IPR013325; RNA_pol_sigma_r2.
InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
InterPro; IPR036388; WH-like_DNA-bd_sf.
PANTHER; PTHR43133; PTHR43133; 1.
Pfam; PF04542; Sigma70_r2; 1.
Pfam; PF08281; Sigma70_r4_2; 1.
SUPFAM; SSF88659; SSF88659; 1.
SUPFAM; SSF88946; SSF88946; 1.
TIGRFAMs; TIGR02947; SigH_actino; 1.
TIGRFAMs; TIGR02937; sigma70-ECF; 1.
PROSITE; PS01063; SIGMA70_ECF; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; DNA-binding;
Phosphoprotein; Reference proteome; Sigma factor; Stress response;
Transcription; Transcription regulation.
CHAIN 1 216 ECF RNA polymerase sigma factor SigH.
/FTId=PRO_0000094004.
DNA_BIND 166 185 H-T-H motif. {ECO:0000250}.
REGION 37 99 Sigma-70 factor domain-2.
REGION 140 191 Sigma-70 factor domain-4.
MOTIF 56 59 Polymerase core binding. {ECO:0000255}.
MUTAGEN 26 26 T->A: No in vitro phosphorylation by
PknB; when associated with A-106.
{ECO:0000269|PubMed:18728196}.
MUTAGEN 106 106 T->A: No in vitro phosphorylation by
PknB; when associated with A-26.
{ECO:0000269|PubMed:18728196}.
SEQUENCE 216 AA; 24225 MW; AC0C33B47DB40CFD CRC64;
MADIDGVTGS AGLQPGPSEE TDEELTARFE RDAIPLLDQL YGGALRMTRN PADAEDLLQE
TMVKAYAGFR SFRHGTNLKA WLYRILTNTY INSYRKKQRQ PAEYPTEQIT DWQLASNAEH
SSTGLRSAEV EALEALPDTE IKEALQALPE EFRMAVYYAD VEGFPYKEIA EIMDTPIGTV
MSRLHRGRRQ LRGLLADVAR DRGFARGEQA HEGVSS


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