SIGF_MYCTU
ID SIGF_MYCTU Reviewed; 261 AA.
AC P9WGI3; F2GKV9; Q50547; Q798K1; Q7D5S2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=RNA polymerase sigma factor SigF;
DE Short=Sigma factor SigF;
DE AltName: Full=Alternative RNA polymerase sigma factor SigF;
DE AltName: Full=RNA polymerase sigma-F factor;
DE Short=Sigma-F factor;
DE AltName: Full=Stress response/stationary phase sigma factor SigF;
GN Name=sigF; OrderedLocusNames=Rv3286c;
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=8610119; DOI=10.1073/pnas.93.7.2790;
RA DeMaio J., Zhang Y., Ko C., Young D.B., Bishai W.R.;
RT "A stationary-phase stress-response sigma factor from Mycobacterium
RT tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2790-2794(1996).
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 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 [5]
RP FUNCTION AS A SIGMA FACTOR, REGULATION, AND INTERACTION WITH RSBW.
RX PubMed=12354223; DOI=10.1046/j.1365-2958.2002.03135.x;
RA Beaucher J., Rodrigue S., Jacques P.E., Smith I., Brzezinski R.,
RA Gaudreau L.;
RT "Novel Mycobacterium tuberculosis anti-sigma factor antagonists control
RT sigmaF activity by distinct mechanisms.";
RL Mol. Microbiol. 45:1527-1540(2002).
RN [6]
RP DISRUPTION PHENOTYPE IN GUINEA PIGS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16735723; DOI=10.1099/mic.0.28591-0;
RA Karls R.K., Guarner J., McMurray D.N., Birkness K.A., Quinn F.D.;
RT "Examination of Mycobacterium tuberculosis sigma factor mutants using low-
RT dose aerosol infection of guinea pigs suggests a role for SigC in
RT pathogenesis.";
RL Microbiology 152:1591-1600(2006).
RN [7]
RP SUBUNIT, AND INTERACTION WITH RSBW.
RX PubMed=19130906; DOI=10.1016/j.bbapap.2008.11.007;
RA Malik S.S., Luthra A., Ramachandran R.;
RT "Interactions of the M. tuberculosis UsfX with the cognate sigma factor
RT SigF and the anti-anti sigma factor RsfA.";
RL Biochim. Biophys. Acta 1794:541-553(2009).
RN [8]
RP FUNCTION AS A SIGMA FACTOR, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20729364; DOI=10.1128/jb.00687-10;
RA Hartkoorn R.C., Sala C., Magnet S.J., Chen J.M., Pojer F., Cole S.T.;
RT "Sigma factor F does not prevent rifampin inhibition of RNA polymerase or
RT cause rifampin tolerance in Mycobacterium tuberculosis.";
RL J. Bacteriol. 192:5472-5479(2010).
RN [9]
RP INTERACTION WITH RSBW.
RX PubMed=20600947; DOI=10.1016/j.pep.2010.06.018;
RA Thakur K.G., Jaiswal R.K., Shukla J.K., Praveena T., Gopal B.;
RT "Over-expression and purification strategies for recombinant multi-protein
RT oligomers: a case study of Mycobacterium tuberculosis sigma/anti-sigma
RT factor protein complexes.";
RL Protein Expr. Purif. 74:223-230(2010).
RN [10]
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 [11]
RP FUNCTION, AND REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22307756; DOI=10.1128/jb.06692-11;
RA Hartkoorn R.C., Sala C., Uplekar S., Busso P., Rougemont J., Cole S.T.;
RT "Genome-wide definition of the SigF regulon in Mycobacterium
RT tuberculosis.";
RL J. Bacteriol. 194:2001-2009(2012).
RN [12]
RP FUNCTION AS A SIGMA FACTOR.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22570422; DOI=10.1093/nar/gks346;
RA Hu Y., Morichaud Z., Chen S., Leonetti J.P., Brodolin K.;
RT "Mycobacterium tuberculosis RbpA protein is a new type of transcriptional
RT activator that stabilizes the sigma A-containing RNA polymerase
RT holoenzyme.";
RL Nucleic Acids Res. 40:6547-6557(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. Held in an inactive form by a cognate anti-sigma factor RsbW
CC (UsfX) until released. Increased expression decreases growth rate, and
CC after 3 days increases the expression of 51 loci encoding 33 protein-
CC coding genes as well as some non-coding RNA (PubMed:22307756).
CC {ECO:0000269|PubMed:12354223, ECO:0000269|PubMed:20729364,
CC ECO:0000269|PubMed:22307756, ECO:0000269|PubMed:22570422}.
CC -!- SUBUNIT: Monomer. Interacts transiently with the RNA polymerase
CC catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1
CC beta' and 1 omega subunit) to form the RNA polymerase holoenzyme that
CC can initiate transcription. Interacts (via sigma-70 factor domain 4)
CC with anti-sigma-F factor RsbW (UsfX) with a possible 2:1 RbsW:SigF
CC stoichiometry, which inhibits SigF activity.
CC {ECO:0000269|PubMed:12354223, ECO:0000269|PubMed:19130906,
CC ECO:0000269|PubMed:20600947}.
CC -!- INDUCTION: Constitutively expressed at a low level under all conditions
CC tested, including stationary phase and several stresses. 3-fold induced
CC during starvation (PubMed:11929527). Positively controls expression of
CC its own operon (rsbW-sigF). {ECO:0000269|PubMed:10027986,
CC 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 (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Infected guinea pigs mutant and wild-type
CC bacteria grow comparably (PubMed:16735723). A double rsbW-sigF
CC disruption shows no effect in the presence or absence of rifampicin
CC (PubMed:20729364). {ECO:0000269|PubMed:16735723,
CC ECO:0000269|PubMed:20729364}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. {ECO:0000305}.
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DR EMBL; U41061; AAC44103.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46105.1; -; Genomic_DNA.
DR RefSeq; NP_217803.1; NC_000962.3.
DR RefSeq; WP_003417158.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; P9WGI3; -.
DR SMR; P9WGI3; -.
DR IntAct; P9WGI3; 5.
DR STRING; 83332.Rv3286c; -.
DR PaxDb; P9WGI3; -.
DR DNASU; 888727; -.
DR GeneID; 45427282; -.
DR GeneID; 888727; -.
DR KEGG; mtu:Rv3286c; -.
DR TubercuList; Rv3286c; -.
DR eggNOG; COG1191; Bacteria.
DR OMA; CGVNTAK; -.
DR PhylomeDB; P9WGI3; -.
DR Proteomes; UP000001584; Chromosome.
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:0070417; P:cellular response to cold; IEP:MTBBASE.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:MTBBASE.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MTBBASE.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0034059; P:response to anoxia; IMP:MTBBASE.
DR GO; GO:0046677; P:response to antibiotic; IMP:MTBBASE.
DR GO; GO:0009409; P:response to cold; IMP:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR014322; RNA_pol_sigma-B/F/G.
DR InterPro; IPR000943; RNA_pol_sigma70.
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; 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; TIGR02980; SigBFG; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..261
FT /note="RNA polymerase sigma factor SigF"
FT /id="PRO_0000422954"
FT DNA_BIND 231..250
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 43..112
FT /note="Sigma-70 factor domain-2"
FT REGION 123..189
FT /note="Sigma-70 factor domain-3"
FT REGION 209..258
FT /note="Sigma-70 factor domain-4"
FT MOTIF 67..70
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000250"
FT CONFLICT 248
FT /note="L -> V (in Ref. 1; AAC44103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 28794 MW; 7FD4AA6AB64061AB CRC64;
MTARAAGGSA SRANEYADVP EMFRELVGLP AGSPEFQRHR DKIVQRCLPL ADHIARRFEG
RGEPRDDLIQ VARVGLVNAA VRFDVKTGSD FVSFAVPTIM GEVRRHFRDN SWSVKVPRRL
KELHLRLGTA TADLSQRLGR APSASELAAE LGMDRAEVIE GLLAGSSYHT LSIDSGGGSD
DDARAITDTL GDVDAGLDQI ENREVLRPLL EALPERERTV LVLRFFDSMT QTQIAERVGI
SQMHVSRLLA KSLARLRDQL E
