SIGM_MYCTU
ID SIGM_MYCTU Reviewed; 196 AA.
AC O53590; L0TH42;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=ECF RNA polymerase sigma factor SigM;
DE Short=ECF sigma factor SigM;
DE AltName: Full=Alternative RNA polymerase sigma factor SigM;
DE AltName: Full=RNA polymerase sigma-M factor;
DE Short=Sigma-M factor;
GN Name=sigM; OrderedLocusNames=Rv3911;
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 [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 [2]
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 [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17028284; DOI=10.1128/jb.01212-06;
RA Raman S., Puyang X., Cheng T.Y., Young D.C., Moody D.B., Husson R.N.;
RT "Mycobacterium tuberculosis SigM positively regulates Esx secreted protein
RT and nonribosomal peptide synthetase genes and down regulates virulence-
RT associated surface lipid synthesis.";
RL J. Bacteriol. 188:8460-8468(2006).
RN [4]
RP DISRUPTION PHENOTYPE.
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 [5]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [6]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22733573; DOI=10.1128/iai.06328-11;
RA Casonato S., Cervantes Sanchez A., Haruki H., Rengifo Gonzalez M.,
RA Provvedi R., Dainese E., Jaouen T., Gola S., Bini E., Vicente M.,
RA Johnsson K., Ghisotti D., Palu G., Hernandez-Pando R., Manganelli R.;
RT "WhiB5, a transcriptional regulator that contributes to Mycobacterium
RT tuberculosis virulence and reactivation.";
RL Infect. Immun. 80:3132-3144(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 an anti-sigma factor (RsaM, AC L7N5D7) until released
CC by regulated intramembrane proteolysis (Probable). This sigma factor is
CC required for the synthesis of surface or secreted molecules.
CC {ECO:0000269|PubMed:17028284, ECO:0000305}.
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 anti-
CC sigma-M factor RsmA (AC L7N5D7) (By similarity). {ECO:0000250}.
CC -!- INDUCTION: Constitutively low in all growth stages; repressed by
CC detergent (3.5-fold). Induced by WhiB5. {ECO:0000269|PubMed:10027986,
CC ECO:0000269|PubMed:17028284, ECO:0000269|PubMed:22733573}.
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: No effect on growth in culture, or in isolated
CC macrophages; infected guinea pigs have a partially attenuated lung
CC infection. {ECO:0000269|PubMed:16735723, ECO:0000269|PubMed:17028284}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- MISCELLANEOUS: Extracytoplasmic function (ECF) sigma factors are held
CC in an inactive form by an anti-sigma factor until released by regulated
CC intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic
CC signal triggers a concerted proteolytic cascade to transmit information
CC and elicit cellular responses. The membrane-spanning anti-sigma factor
CC is first cut extracytoplasmically (site-1 protease, S1P), then within
CC the membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic
CC proteases finish degrading the regulatory protein, liberating SigM
CC (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP46740.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP46740.1; ALT_FRAME; Genomic_DNA.
DR PIR; G70850; G70850.
DR RefSeq; NP_218428.1; NC_000962.3.
DR RefSeq; WP_003400144.1; NZ_KK339374.1.
DR AlphaFoldDB; O53590; -.
DR SMR; O53590; -.
DR STRING; 83332.Rv3911; -.
DR PaxDb; O53590; -.
DR GeneID; 886246; -.
DR KEGG; mtu:Rv3911; -.
DR PATRIC; fig|83332.111.peg.4356; -.
DR TubercuList; Rv3911; -.
DR eggNOG; COG1595; Bacteria.
DR InParanoid; O53590; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:0009415; P:response to water; 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 2: Evidence at transcript level;
KW DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..196
FT /note="ECF RNA polymerase sigma factor SigM"
FT /id="PRO_0000420400"
FT DNA_BIND 156..175
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 39..105
FT /note="Sigma-70 factor domain-2"
FT REGION 130..181
FT /note="Sigma-70 factor domain-4"
FT MOTIF 63..66
FT /note="Polymerase core binding"
FT /evidence="ECO:0000255"
SQ SEQUENCE 196 AA; 21649 MW; 5C1175E850ABA298 CRC64;
MPPPIGYCPA VGFGGRHERS DAELLAAHVA GDRYAFDQLF RRHHRQLHRL ARLTSRTSED
ADDALQDAML SAHRGAGSFR YDAAVSSWLH RIVVNACLDR LRRAKAHPTA PLEDVYPVAD
RTAQVETAIA VQRALMRLPV EQRAAVVAVD MQGYSIADTA RMLGVAEGTV KSRCARARAR
LARLLGYLNT GVNIRR
