SIGL_MYCTU
ID SIGL_MYCTU Reviewed; 177 AA.
AC P9WGH5; F2GMW0; Q7ARS1; Q7D9D4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=ECF RNA polymerase sigma factor SigL;
DE Short=ECF sigma factor SigL;
DE AltName: Full=Alternative RNA polymerase sigma factor SigL;
DE AltName: Full=RNA polymerase sigma-L factor;
DE Short=Sigma-L factor;
GN Name=sigL; OrderedLocusNames=Rv0735;
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 FUNCTION, INTERACTION WITH RSLA, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16199577; DOI=10.1128/jb.187.20.7062-7071.2005;
RA Hahn M.Y., Raman S., Anaya M., Husson R.N.;
RT "The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL
RT regulates polyketide synthases and secreted or membrane proteins and is
RT required for virulence.";
RL J. Bacteriol. 187:7062-7071(2005).
RN [3]
RP FUNCTION, INTERACTION WITH RSLA, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16552079; DOI=10.1128/iai.74.4.2457-2461.2006;
RA Dainese E., Rodrigue S., Delogu G., Provvedi R., Laflamme L.,
RA Brzezinski R., Fadda G., Smith I., Gaudreau L., Palu G., Manganelli R.;
RT "Posttranslational regulation of Mycobacterium tuberculosis
RT extracytoplasmic-function sigma factor sigma L and roles in virulence and
RT in global regulation of gene expression.";
RL Infect. Immun. 74:2457-2461(2006).
RN [4]
RP INTERACTION WITH RSLA.
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 99-177 IN COMPLEX WITH RSLA, AND
RP SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20184899; DOI=10.1016/j.jmb.2010.02.026;
RA Thakur K.G., Praveena T., Gopal B.;
RT "Structural and biochemical bases for the redox sensitivity of
RT Mycobacterium tuberculosis RslA.";
RL J. Mol. Biol. 397:1199-1208(2010).
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 by regulated
CC intramembrane proteolysis. Over-expression of SigL induces 19-28 genes
CC including polyketide synthases, secreted and membrane proteins. Might
CC play a minor role in regulating SigB. {ECO:0000269|PubMed:16199577,
CC ECO:0000269|PubMed:16552079}.
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-L factor RslA. {ECO:0000269|PubMed:16199577,
CC ECO:0000269|PubMed:16552079, ECO:0000269|PubMed:20184899,
CC ECO:0000269|PubMed:20600947}.
CC -!- INDUCTION: Expressed during growth in culture; expression increases
CC from lag to exponential phase. Has a weak SigL-independent promoter, is
CC also weakly autoregulated, no other sigma factor allows its
CC transcription. Forms an operon with rslA. {ECO:0000269|PubMed:16199577,
CC ECO:0000269|PubMed:16552079}.
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: In a single sigL (PubMed:16199577) or double
CC sigL-rslA (PubMed:16552079) disruption mutant, no visible phenotype;
CC not more susceptible than the parental strain to several oxidative and
CC nitrosative stresses. Infected BALB/c or DBA/2 mice showed a
CC significantly prolonged survival time relative to mice infected with
CC wild-type bacteria, although bacteria proliferate normally.
CC {ECO:0000269|PubMed:16199577, ECO:0000269|PubMed:16552079}.
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 SigL
CC (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43480.1; -; Genomic_DNA.
DR RefSeq; NP_215249.1; NC_000962.3.
DR RefSeq; WP_003403731.1; NZ_NVQJ01000007.1.
DR PDB; 3HUG; X-ray; 2.35 A; A/C/E/G/I/K/M/O/Q/S=99-177.
DR PDB; 6DV9; X-ray; 3.80 A; F=1-177.
DR PDB; 6DVB; X-ray; 3.80 A; F=1-177.
DR PDB; 6DVC; X-ray; 3.30 A; F=1-177.
DR PDB; 6DVD; X-ray; 3.90 A; F=1-177.
DR PDB; 6DVE; X-ray; 3.81 A; F=1-177.
DR PDB; 6TYE; X-ray; 3.79 A; F=1-177.
DR PDB; 6TYF; X-ray; 3.80 A; F=1-177.
DR PDB; 6TYG; X-ray; 3.50 A; F=1-177.
DR PDBsum; 3HUG; -.
DR PDBsum; 6DV9; -.
DR PDBsum; 6DVB; -.
DR PDBsum; 6DVC; -.
DR PDBsum; 6DVD; -.
DR PDBsum; 6DVE; -.
DR PDBsum; 6TYE; -.
DR PDBsum; 6TYF; -.
DR PDBsum; 6TYG; -.
DR AlphaFoldDB; P9WGH5; -.
DR SMR; P9WGH5; -.
DR STRING; 83332.Rv0735; -.
DR PaxDb; P9WGH5; -.
DR DNASU; 888609; -.
DR GeneID; 45424700; -.
DR GeneID; 888609; -.
DR KEGG; mtu:Rv0735; -.
DR TubercuList; Rv0735; -.
DR eggNOG; COG1595; Bacteria.
DR OMA; AWRHPEV; -.
DR PhylomeDB; P9WGH5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IDA:MTBBASE.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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; IPR000838; RNA_pol_sigma70_ECF_CS.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
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 PANTHER; PTHR43133; PTHR43133; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF04545; Sigma70_r4; 1.
DR SUPFAM; SSF88659; SSF88659; 1.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS01063; SIGMA70_ECF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..177
FT /note="ECF RNA polymerase sigma factor SigL"
FT /id="PRO_0000423646"
FT DNA_BIND 141..160
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 18..85
FT /note="Sigma-70 factor domain-2"
FT REGION 119..167
FT /note="Sigma-70 factor domain-4"
FT MOTIF 42..45
FT /note="Interaction with polymerase core subunit RpoC"
FT /evidence="ECO:0000250"
FT HELIX 5..34
FT /evidence="ECO:0007829|PDB:6DVC"
FT HELIX 37..52
FT /evidence="ECO:0007829|PDB:6DVC"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:6DVC"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6DVC"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:6DVC"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:6DVC"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6DVC"
FT HELIX 103..121
FT /evidence="ECO:0007829|PDB:3HUG"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3HUG"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:3HUG"
FT HELIX 152..173
FT /evidence="ECO:0007829|PDB:3HUG"
SQ SEQUENCE 177 AA; 19538 MW; 8E13D528AEDD9E16 CRC64;
MARVSGAAAA EAALMRALYD EHAAVLWRYA LRLTGDAAQA EDVVQETLLR AWQHPEVIGD
TARPARAWLF TVARNMIIDE RRSARFRNVV GSTDQSGTPE QSTPDEVNAA LDRLLIADAL
AQLSAEHRAV IQRSYYRGWS TAQIATDLGI AEGTVKSRLH YAVRALRLTL QELGVTR
