SIGH_MYCTO
ID SIGH_MYCTO Reviewed; 216 AA.
AC P9WGH8; L0TEP5; O05843; P66807;
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=ECF RNA polymerase sigma factor SigH;
DE Short=ECF sigma factor SigH;
DE AltName: Full=Alternative RNA polymerase sigma factor SigH;
DE AltName: Full=RNA polymerase sigma-H factor;
DE Short=Sigma-H factor;
GN Name=sigH; Synonyms=rpoE; OrderedLocusNames=MT3320;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP INDUCTION, DISRUPTION PHENOTYPE, AND REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12060776; DOI=10.1073/pnas.102055799;
RA Kaushal D., Schroeder B.G., Tyagi S., Yoshimatsu T., Scott C., Ko C.,
RA Carpenter L., Mehrotra J., Manabe Y.C., Fleischmann R.D., Bishai W.R.;
RT "Reduced immunopathology and mortality despite tissue persistence in a
RT Mycobacterium tuberculosis mutant lacking alternative sigma factor, SigH.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8330-8335(2002).
RN [3]
RP FUNCTION, INDUCTION BY DIAMIDE, AND REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=19376862; DOI=10.1128/jb.00064-09;
RA Mehra S., Kaushal D.;
RT "Functional genomics reveals extended roles of the Mycobacterium
RT tuberculosis stress response factor sigmaH.";
RL J. Bacteriol. 191:3965-3980(2009).
RN [4]
RP DISRUPTION PHENOTYPE IN RHESUS MACAQUE MACROPHAGES.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=22235255; DOI=10.1371/journal.pone.0028958;
RA Dutta N.K., Mehra S., Martinez A.N., Alvarez X., Renner N.A., Morici L.A.,
RA Pahar B., Maclean A.G., Lackner A.A., Kaushal D.;
RT "The stress-response factor SigH modulates the interaction between
RT Mycobacterium tuberculosis and host phagocytes.";
RL PLoS ONE 7:E28958-E28958(2012).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. Extracytoplasmic function (ECF) sigma factors are held in an
CC inactive form by a cognate anti-sigma factor (RshA) until released.
CC This sigma factor is involved in heat shock and oxidative stress
CC responses; it positively regulates the expression of itself, sigE, sigB
CC and a number of transcriptional regulators as well as other effectors
CC of heat and oxidative stress, leading to direct and indirect control of
CC up to 25% of the bacterial genome. Modulates expression of host genes
CC for intercrine beta (chemokine CC) and apoptosis, altering the host
CC immune response. {ECO:0000269|PubMed:19376862}.
CC -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core
CC formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1
CC omega subunit) to form the RNA polymerase holoenzyme that can initiate
CC transcription. {ECO:0000250}.
CC -!- INDUCTION: Poorly expressed in exponential phase; induced by heat shock
CC (20-fold, 45 degrees Celsius). Induced 10-fold by the thiol-oxidative
CC agent diamide within 30 minutes of exposure, by 2 hours expression is
CC again normal. Autoregulates its own expression, part of the sigH-rshA
CC operon. {ECO:0000269|PubMed:12060776, ECO:0000269|PubMed:19376862}.
CC -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific
CC interaction with the -10 element in promoter DNA, and plays an
CC important role in melting the double-stranded DNA and the formation of
CC the transcription bubble. The sigma-70 factor domain-2 mediates
CC interaction with the RNA polymerase subunits RpoB and RpoC (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-
CC H) motif that mediates interaction with the -35 element in promoter
CC DNA. The domain also mediates interaction with the RNA polymerase
CC subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-
CC sigma factors prevents interaction of sigma factors with the RNA
CC polymerase catalytic core.
CC -!- PTM: Phosphorylated, possibly on 2 residues, probably by PknB.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Yields a delayed lung infection in mouse C57BL/6
CC or C3H infections, although bacterial burden remains wild-type
CC (PubMed:12060776). Shows decreased bacterial burden 72 hours post-
CC infection in rhesus monkey-derived macrophages and altered induction of
CC host intercrine beta (chemokine CC) and apoptosis-related genes
CC (PubMed:22235255). {ECO:0000269|PubMed:12060776,
CC ECO:0000269|PubMed:22235255}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK47662.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK47662.1; ALT_INIT; Genomic_DNA.
DR PIR; H70596; H70596.
DR RefSeq; WP_003416897.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGH8; -.
DR SMR; P9WGH8; -.
DR EnsemblBacteria; AAK47662; AAK47662; MT3320.
DR KEGG; mtc:MT3320; -.
DR PATRIC; fig|83331.31.peg.3575; -.
DR HOGENOM; CLU_047691_1_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0009628; P:response to abiotic stimulus; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR039425; RNA_pol_sigma-70-like.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR014293; RNA_pol_sigma70_actinobac.
DR InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR013249; RNA_pol_sigma70_r4_t2.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR43133; PTHR43133; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF08281; Sigma70_r4_2; 1.
DR SUPFAM; SSF88659; SSF88659; 1.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02947; SigH_actino; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS01063; SIGMA70_ECF; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Phosphoprotein; Sigma factor; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..216
FT /note="ECF RNA polymerase sigma factor SigH"
FT /id="PRO_0000428359"
FT DNA_BIND 166..185
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..99
FT /note="Sigma-70 factor domain-2"
FT REGION 140..191
FT /note="Sigma-70 factor domain-4"
FT MOTIF 56..59
FT /note="Polymerase core binding"
FT /evidence="ECO:0000255"
SQ 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
