SIGG_MYCTU
ID SIGG_MYCTU Reviewed; 370 AA.
AC P9WGG5; L7N5U5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=ECF RNA polymerase sigma factor SigG;
DE Short=ECF sigma factor SigG;
DE AltName: Full=Alternative RNA polymerase sigma factor SigG;
DE AltName: Full=RNA polymerase sigma-G factor;
DE Short=Sigma-g factor;
GN Name=sigG; OrderedLocusNames=Rv0182c;
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, AND INDUCTION IN HUMAN MACROPHAGES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16483748; DOI=10.1016/j.resmic.2005.10.007;
RA Cappelli G., Volpe E., Grassi M., Liseo B., Colizzi V., Mariani F.;
RT "Profiling of Mycobacterium tuberculosis gene expression during human
RT macrophage infection: upregulation of the alternative sigma factor G, a
RT group of transcriptional regulators, and proteins with unknown function.";
RL Res. Microbiol. 157:445-455(2006).
RN [4]
RP FUNCTION, INDUCTION BY DNA DAMAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21169493; DOI=10.1128/jb.01241-10;
RA Smollett K.L., Dawson L.F., Davis E.O.;
RT "SigG does not control gene expression in response to DNA damage in
RT Mycobacterium tuberculosis H37Rv.";
RL J. Bacteriol. 193:1007-1011(2011).
RN [5]
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 a cognate anti-sigma factor until released, although
CC no anti-sigma factor is known for this protein. May be involved in host
CC intracellular survival after infection (strains H37Rv and CDC 1551). A
CC role in the SOS response is controversial; it has been seen in strain
CC CDC 1551 (PubMed:18039768) but not in H37Rv (PubMed:21169493).
CC {ECO:0000269|PubMed:16483748, ECO:0000269|PubMed:21169493}.
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. {ECO:0000305}.
CC -!- INDUCTION: Very poorly expressed in exponential phase; further
CC repressed at room temperature. Up-regulated 10-fold 7 days after
CC infection of human macrophages. Induced by DNA-damaging agents but not
CC by surface stress (detergent). {ECO:0000269|PubMed:10027986,
CC ECO:0000269|PubMed:16483748, ECO:0000269|PubMed:21169493}.
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: Not essential, no effect on the SOS response
CC genes, no change in resistance to DNA-damaging agents including
CC mitomycin C. {ECO:0000269|PubMed:21169493}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42908.1; -; Genomic_DNA.
DR PIR; A70906; A70906.
DR RefSeq; NP_214696.1; NC_000962.3.
DR RefSeq; WP_003401110.1; NZ_NVQJ01000001.1.
DR AlphaFoldDB; P9WGG5; -.
DR SMR; P9WGG5; -.
DR STRING; 83332.Rv0182c; -.
DR PaxDb; P9WGG5; -.
DR DNASU; 886786; -.
DR GeneID; 886786; -.
DR KEGG; mtu:Rv0182c; -.
DR PATRIC; fig|83332.111.peg.209; -.
DR TubercuList; Rv0182c; -.
DR eggNOG; COG1595; Bacteria.
DR eggNOG; COG3631; Bacteria.
DR OMA; VPWLEPL; -.
DR PhylomeDB; P9WGG5; -.
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:0001666; P:response to hypoxia; IEP:MTBBASE.
DR GO; GO:0009415; P:response to water; IEP:MTBBASE.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR039425; RNA_pol_sigma-70-like.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR014305; RNA_pol_sigma-G_actinobac.
DR InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
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; IPR037401; SnoaL-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 Pfam; PF12680; SnoaL_2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF88659; SSF88659; 1.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR TIGRFAMs; TIGR02960; SigX5; 1.
DR PROSITE; PS01063; SIGMA70_ECF; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..370
FT /note="ECF RNA polymerase sigma factor SigG"
FT /id="PRO_0000423098"
FT DNA_BIND 207..226
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 63..129
FT /note="Sigma-70 factor domain-2"
FT REGION 180..232
FT /note="Sigma-70 factor domain-4"
FT MOTIF 85..88
FT /note="Polymerase core binding"
FT /evidence="ECO:0000255"
SQ SEQUENCE 370 AA; 40983 MW; DF6CA9852FF3A793 CRC64;
MRTSPMPAKF RSVRVVVITG SVTAAPVRVS ETLRRLIDVS VLAENSGREP ADERRGDFSA
HTEPYRRELL AHCYRMTGSL HDAEDLVQET LLRAWKAYEG FAGKSSLRTW LHRIATNTCL
TALEGRRRRP LPTGLGRPSA DPSGELVERR EVSWLEPLPD VTDDPADPST IVGNRESVRL
AFVAALQHLS PRQRAVLLLR DVLQWKSAEV ADAIGTSTVA VNSLLQRARS QLQTVRPSAA
DRLSAPDSPE AQDLLARYIA AFEAYDIDRL VELFTAEAIW EMPPYTGWYQ GAQAIVTLIH
QQCPAYSPGD MRLISLIANG QPAAAMYMRA GDVHLPFQLH VLDMAADRVS HVVAFLDTTL
FPKFGLPDSL
