SIGE_MYCTU
ID SIGE_MYCTU Reviewed; 257 AA.
AC P9WGG7; F2GFW7; O06289; Q79FQ9; Q7D8K8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=ECF RNA polymerase sigma factor SigE;
DE Short=ECF sigma factor SigE;
DE AltName: Full=Alternative RNA polymerase sigma factor SigE;
DE AltName: Full=RNA polymerase sigma-E factor;
DE Short=Sigma-E factor;
GN Name=sigE; OrderedLocusNames=Rv1221;
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 [GENOMIC DNA], AND FUNCTION AS A SIGMA FACTOR.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9139909; DOI=10.1128/jb.179.9.2922-2929.1997;
RA Wu Q.L., Kong D., Lam K., Husson R.N.;
RT "A mycobacterial extracytoplasmic function sigma factor involved in
RT survival following stress.";
RL J. Bacteriol. 179:2922-2929(1997).
RN [2]
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 [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=10027986; DOI=10.1046/j.1365-2958.1999.01212.x;
RA Manganelli R., Dubnau E., Tyagi S., Kramer F.R., Smith I.;
RT "Differential expression of 10 sigma factor genes in Mycobacterium
RT tuberculosis.";
RL Mol. Microbiol. 31:715-724(1999).
RN [4]
RP INDUCTION BY SIGH.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11567012; DOI=10.1128/jb.183.20.6119-6125.2001;
RA Raman S., Song T., Puyang X., Bardarov S., Jacobs W.R. Jr., Husson R.N.;
RT "The alternative sigma factor SigH regulates major components of oxidative
RT and heat stress responses in Mycobacterium tuberculosis.";
RL J. Bacteriol. 183:6119-6125(2001).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE IN MACROPHAGES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11489128; DOI=10.1046/j.1365-2958.2001.02525.x;
RA Manganelli R., Voskuil M.I., Schoolnik G.K., Smith I.;
RT "The Mycobacterium tuberculosis ECF sigma factor sigmaE: role in global
RT gene expression and survival in macrophages.";
RL Mol. Microbiol. 41:423-437(2001).
RN [6]
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 [7]
RP DISRUPTION PHENOTYPE IN MICE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15102817; DOI=10.1128/iai.72.5.3038-3041.2004;
RA Manganelli R., Fattorini L., Tan D., Iona E., Orefici G., Altavilla G.,
RA Cusatelli P., Smith I.;
RT "The extra cytoplasmic function sigma factor sigma(E) is essential for
RT Mycobacterium tuberculosis virulence in mice.";
RL Infect. Immun. 72:3038-3041(2004).
RN [8]
RP REGULATION BY MPRAB.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16513743; DOI=10.1128/jb.188.6.2134-2143.2006;
RA He H., Hovey R., Kane J., Singh V., Zahrt T.C.;
RT "MprAB is a stress-responsive two-component system that directly regulates
RT expression of sigma factors SigB and SigE in Mycobacterium tuberculosis.";
RL J. Bacteriol. 188:2134-2143(2006).
RN [9]
RP REGULATION BY MPRAB.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17379732; DOI=10.1099/mic.0.29281-0;
RA Pang X., Vu P., Byrd T.F., Ghanny S., Soteropoulos P., Mukamolova G.V.,
RA Wu S., Samten B., Howard S.T.;
RT "Evidence for complex interactions of stress-associated regulons in an
RT mprAB deletion mutant of Mycobacterium tuberculosis.";
RL Microbiology 153:1229-1242(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE IN MACROPHAGES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18657035; DOI=10.1086/591098;
RA Fontan P.A., Aris V., Alvarez M.E., Ghanny S., Cheng J., Soteropoulos P.,
RA Trevani A., Pine R., Smith I.;
RT "Mycobacterium tuberculosis sigma factor E regulon modulates the host
RT inflammatory response.";
RL J. Infect. Dis. 198:877-885(2008).
RN [11]
RP REGULATION, INTERACTION WITH RSEA, AND ALTERNATIVE PROMOTER USAGE (ISOFORMS
RP 2 AND 3).
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18606740; DOI=10.1128/jb.00622-08;
RA Dona V., Rodrigue S., Dainese E., Palu G., Gaudreau L., Manganelli R.,
RA Provvedi R.;
RT "Evidence of complex transcriptional, translational, and posttranslational
RT regulation of the extracytoplasmic function sigma factor sigmaE in
RT Mycobacterium tuberculosis.";
RL J. Bacteriol. 190:5963-5971(2008).
RN [12]
RP FUNCTION AS A SIGMA FACTOR, REGULATION, AND INTERACTION WITH RSEA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20025669; DOI=10.1111/j.1365-2958.2009.07008.x;
RA Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.;
RT "RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis,
RT is inactivated by phosphorylation-dependent ClpC1P2 proteolysis.";
RL Mol. Microbiol. 75:592-606(2010).
RN [13]
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: 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 an anti-sigma factor until released. Responds to heat
CC shock and surface stress (detergent exposure). When combined with
CC isolated core RNA polymerase from M.smegmatis is able to guide
CC initiation from the sigB promoter. Required for full expression of
CC sigB, and for sigB induction after detergent exposure but not after
CC heat shock. Controls a regulon of about 38 genes in culture
CC (PubMed:11489128) and about 16 genes during macrophage infection
CC (PubMed:18657035), most of which have decreased expression in a
CC disruption mutant. Probably down regulates the host immune response to
CC mycobacterial infection. {ECO:0000269|PubMed:11489128,
CC ECO:0000269|PubMed:18657035, ECO:0000269|PubMed:20025669,
CC ECO:0000269|PubMed:9139909}.
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. Interacts (via sigma-70 factor domain 4) with cognate
CC anti-sigma-E factor RseA under reducing conditions, which stops the
CC sigma factor from functioning. Inhibition is specific; RsaH and RsaL
CC (anti-sigma-H and -L factors) do not inhibit SigE.
CC {ECO:0000269|PubMed:18606740, ECO:0000269|PubMed:20025669}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=3;
CC Name=1; Synonyms=Sigma-E 257;
CC IsoId=P9WGG7-1; Sequence=Displayed;
CC Name=2; Synonyms=Sigma-E 218;
CC IsoId=P9WGG7-2; Sequence=VSP_047441, VSP_047443;
CC Name=3; Synonyms=Sigma-E 215;
CC IsoId=P9WGG7-3; Sequence=VSP_047440, VSP_047442;
CC -!- INDUCTION: Unlike many sigma factors not directly autoregulated.
CC Expressed from 3 promoters. P1 is 55 nucleotides upstream of the major
CC start codon, used during normal growth, repressed by surface stress, P2
CC is at the start codon, under control of MprAB and is induced following
CC surface stress and alkaline pH leading to a leader-less RNA, while P3
CC is 63 nucleotides downstream of the major start codon, transcribed from
CC a SigH-responsive promoter under conditions of oxidative stress and
CC heat shock. Expressed in exponential phase; further induced by
CC detergent (6-fold) and heat shock (3-fold, 45 degrees Celsius) under
CC control of SigH. Positively regulated by MprAB, as is induction by
CC detergent. 6-fold induced by starvation, not known by which promoter.
CC {ECO:0000269|PubMed:10027986, ECO:0000269|PubMed:11489128,
CC ECO:0000269|PubMed:11567012, ECO:0000269|PubMed:11929527}.
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 (Probable). {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to detergent and heat
CC shock, slighty decreased resistance to oxidative stress. Poor growth in
CC both human and mouse macrophage-derived cell lines. Attenuated
CC infection in both SCID and BALB/c mice. 13-fold decreased transcription
CC of sigB, no change in its own transcript in culture. The sigE mutant
CC induced the up-regulation of human and mouse macrophage gene
CC expression, which correlated with an increased innate immune response.
CC {ECO:0000269|PubMed:11489128, ECO:0000269|PubMed:15102817,
CC ECO:0000269|PubMed:18657035}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced following surface stress.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced following oxidative stress and
CC heat shock. Shown by mutagenesis of the start codon and subsequent loss
CC of translationally fused LacZ. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced following oxidative stress and
CC heat shock. Able to interact with RseA. Shown by mutagenesis of the
CC start codon and subsequent loss of translationally fused LacZ.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {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; U87242; AAC45268.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43977.1; -; Genomic_DNA.
DR PIR; H70507; H70507.
DR RefSeq; NP_215737.1; NC_000962.3. [P9WGG7-1]
DR RefSeq; WP_003406257.1; NZ_NVQJ01000039.1.
DR PDB; 6JCY; X-ray; 3.11 A; F=150-190.
DR PDBsum; 6JCY; -.
DR AlphaFoldDB; P9WGG7; -.
DR SMR; P9WGG7; -.
DR STRING; 83332.Rv1221; -.
DR PaxDb; P9WGG7; -.
DR DNASU; 888751; -.
DR GeneID; 45425191; -.
DR GeneID; 888751; -.
DR KEGG; mtu:Rv1221; -.
DR TubercuList; Rv1221; -.
DR eggNOG; COG1595; Bacteria.
DR OMA; RIAINQC; -.
DR PhylomeDB; P9WGG7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0016987; F:sigma factor activity; IDA:MTBBASE.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEP:MTBBASE.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:MTBBASE.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:MTBBASE.
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; 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; TIGR02937; sigma70-ECF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; DNA-binding; Reference proteome;
KW Sigma factor; Transcription; Transcription regulation.
FT CHAIN 1..257
FT /note="ECF RNA polymerase sigma factor SigE"
FT /id="PRO_0000422945"
FT DNA_BIND 211..230
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 87..153
FT /note="Sigma-70 factor domain-2"
FT REGION 186..236
FT /note="Sigma-70 factor domain-4"
FT MOTIF 111..114
FT /note="Polymerase core binding"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047441"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047440"
FT VAR_SEQ 40
FT /note="I -> M (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047442"
FT VAR_SEQ 43
FT /note="L -> M (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047443"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6JCY"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6JCY"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:6JCY"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:6JCY"
SQ SEQUENCE 257 AA; 28877 MW; E7AB77CAECBF6CE7 CRC64;
MELLGGPRVG NTESQLCVAD GDDLPTYCSA NSEDLNITTI TTLSPTSMSH PQQVRDDQWV
EPSDQLQGTA VFDATGDKAT MPSWDELVRQ HADRVYRLAY RLSGNQHDAE DLTQETFIRV
FRSVQNYQPG TFEGWLHRIT TNLFLDMVRR RARIRMEALP EDYDRVPADE PNPEQIYHDA
RLGPDLQAAL ASLPPEFRAA VVLCDIEGLS YEEIGATLGV KLGTVRSRIH RGRQALRDYL
AAHPEHGECA VHVNPVR
