SIGB_MYCTU
ID SIGB_MYCTU Reviewed; 323 AA.
AC P9WGI5; O08496; O08514; Q59563; Q79FB5; Q7D6Q4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=RNA polymerase sigma factor SigB;
GN Name=sigB; Synonyms=mysB; OrderedLocusNames=Rv2710;
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].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=7489918; DOI=10.1016/0378-1119(95)00427-8;
RA Doukhan L., Predich M., Nair G., Dussurget O., Mandic-Mulec I., Cole S.T.,
RA Smith D.R., Smith I.;
RT "Genomic organization of the mycobacterial sigma gene cluster.";
RL Gene 165:67-70(1995).
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 IN STATIONARY PHASE AND BY H(2)O(2), AND HALF-LIFE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9882660; DOI=10.1128/jb.181.2.469-476.1999;
RA Hu Y., Coates A.R.;
RT "Transcription of two sigma 70 homologue genes, sigA and sigB, in
RT stationary-phase Mycobacterium tuberculosis.";
RL J. Bacteriol. 181:469-476(1999).
RN [4]
RP INDUCTION BY STRESSES.
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 [5]
RP INDUCTION BY SIGE AND 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 [6]
RP INDUCTION BY SIGE.
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 [7]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12123450; DOI=10.1046/j.1365-2958.2002.03005.x;
RA Manganelli R., Voskuil M.I., Schoolnik G.K., Dubnau E., Gomez M., Smith I.;
RT "Role of the extracytoplasmic-function sigma factor sigma(H) in
RT Mycobacterium tuberculosis global gene expression.";
RL Mol. Microbiol. 45:365-374(2002).
RN [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION, REGULON, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19592585; DOI=10.1128/jb.00510-09;
RA Fontan P.A., Voskuil M.I., Gomez M., Tan D., Pardini M., Manganelli R.,
RA Fattorini L., Schoolnik G.K., Smith I.;
RT "The Mycobacterium tuberculosis sigma factor sigmaB is required for full
RT response to cell envelope stress and hypoxia in vitro, but it is
RT dispensable for in vivo growth.";
RL J. Bacteriol. 191:5628-5633(2009).
RN [12]
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).
RN [13]
RP SUBUNIT.
RX PubMed=23605043; DOI=10.1093/nar/gkt277;
RA Tabib-Salazar A., Liu B., Doughty P., Lewis R.A., Ghosh S., Parsy M.L.,
RA Simpson P.J., O'Dwyer K., Matthews S.J., Paget M.S.;
RT "The actinobacterial transcription factor RbpA binds to the principal sigma
RT subunit of RNA polymerase.";
RL Nucleic Acids Res. 41:5679-5691(2013).
RN [14]
RP SUBUNIT, AND INTERACTION WITH RBPA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=23548911; DOI=10.1074/jbc.m113.459883;
RA Bortoluzzi A., Muskett F.W., Waters L.C., Addis P.W., Rieck B., Munder T.,
RA Schleier S., Forti F., Ghisotti D., Carr M.D., O'Hare H.M.;
RT "Mycobacterium tuberculosis RNA polymerase-binding protein A (RbpA) and its
RT interactions with sigma factors.";
RL J. Biol. Chem. 288:14438-14450(2013).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. A non-essential principal sigma factor that responds to cell
CC envelope stress and hypoxia. Controls a regulon of about 40 genes, with
CC another 100 genes expression being altered during SDS stress and about
CC 50 gene being altered during diamide (oxidative) stress.
CC {ECO:0000269|PubMed:19592585}.
CC -!- SUBUNIT: Monomer (Probable). Interacts transiently with the RNA
CC polymerase catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha,
CC 1 beta, 1 beta' and 1 omega subunit) to form the RNA polymerase
CC holoenzyme that can initiate transcription (By similarity). Interacts
CC with RbpA, probably 1:1. {ECO:0000250, ECO:0000269|PubMed:23548911,
CC ECO:0000269|PubMed:23605043, ECO:0000305}.
CC -!- INDUCTION: Expressed in exponential phase, peaks at 10 days and
CC decreases after up to 50 days in culture; induced by detergent (11-
CC fold), heat shock (23-fold, 45 degrees Celsius), low aeration (2.5-
CC fold) and oxidative stress (2.7-fold, SigE and SigH responsive). Seen
CC to be induced (PubMed:9882660) and slightly repressed (PubMed:10027986)
CC by 10 mM H(2)O(2). 2- to 6-fold induced by starvation. Its basal
CC expression is largely under control of SigE, probably via MrpAB,
CC although other factors including SigH also play a role. Half-life of
CC about 2 minutes. {ECO:0000269|PubMed:10027986,
CC ECO:0000269|PubMed:11489128, ECO:0000269|PubMed:11567012,
CC ECO:0000269|PubMed:11929527, ECO:0000269|PubMed:12123450,
CC ECO:0000269|PubMed:9882660}.
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 (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: More sensitive to SDS (cell envelope stress) and
CC hypoxic treatment in vitro. No effect in human THP-1 macrophage-like
CC cells, intravenously inoculated BALB/c mice or aerosol-infected Hartley
CC strain guinea pigs. {ECO:0000269|PubMed:19592585}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. {ECO:0000305}.
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DR EMBL; U10059; AAA86044.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45508.1; -; Genomic_DNA.
DR PIR; JC5011; JC5011.
DR RefSeq; NP_217226.1; NC_000962.3.
DR RefSeq; WP_003413958.1; NZ_NVQJ01000017.1.
DR AlphaFoldDB; P9WGI5; -.
DR SMR; P9WGI5; -.
DR STRING; 83332.Rv2710; -.
DR BindingDB; P9WGI5; -.
DR PaxDb; P9WGI5; -.
DR DNASU; 888580; -.
DR GeneID; 45426697; -.
DR GeneID; 888580; -.
DR KEGG; mtu:Rv2710; -.
DR TubercuList; Rv2710; -.
DR eggNOG; COG0568; Bacteria.
DR OMA; YQRWLAE; -.
DR PhylomeDB; P9WGI5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; IDA:MTBBASE.
DR GO; GO:0016987; F:sigma factor activity; IGI:MTBBASE.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:0009408; P:response to heat; IEP:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IEP:MTBBASE.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:MTBBASE.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR000943; RNA_pol_sigma70.
DR InterPro; IPR009042; RNA_pol_sigma70_r1_2.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR007624; RNA_pol_sigma70_r3.
DR InterPro; IPR007630; RNA_pol_sigma70_r4.
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 Pfam; PF00140; Sigma70_r1_2; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF04539; Sigma70_r3; 1.
DR Pfam; PF04545; Sigma70_r4; 1.
DR PRINTS; PR00046; SIGMA70FCT.
DR SUPFAM; SSF88659; SSF88659; 2.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS00715; SIGMA70_1; 1.
DR PROSITE; PS00716; SIGMA70_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Sigma factor; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..323
FT /note="RNA polymerase sigma factor SigB"
FT /id="PRO_0000423644"
FT DNA_BIND 284..303
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 1..228
FT /note="Sufficient to interact with RbpA"
FT REGION 25..59
FT /note="Sigma-70 factor domain-1"
FT REGION 90..160
FT /note="Sigma-70 factor domain-2"
FT REGION 169..245
FT /note="Sigma-70 factor domain-3"
FT REGION 258..311
FT /note="Sigma-70 factor domain-4"
FT MOTIF 114..117
FT /note="Polymerase core binding"
FT /evidence="ECO:0000255"
SQ SEQUENCE 323 AA; 36343 MW; 761DA93B9A18242F CRC64;
MADAPTRATT SRVDSDLDAQ SPAADLVRVY LNGIGKTALL NAAGEVELAK RIEAGLYAEH
LLETRKRLGE NRKRDLAAVV RDGEAARRHL LEANLRLVVS LAKRYTGRGM PLLDLIQEGN
LGLIRAMEKF DYTKGFKFST YATWWIRQAI TRGMADQSRT IRLPVHLVEQ VNKLARIKRE
MHQHLGREAT DEELAAESGI PIDKINDLLE HSRDPVSLDM PVGSEEEAPL GDFIEDAEAM
SAENAVIAEL LHTDIRSVLA TLDEREHQVI RLRFGLDDGQ PRTLDQIGKL FGLSRERVRQ
IERDVMSKLR HGERADRLRS YAS
