SIGJ_MYCTU
ID SIGJ_MYCTU Reviewed; 312 AA.
AC L0TCG5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=ECF RNA polymerase sigma factor SigJ;
DE Short=ECF sigma factor SigJ;
DE AltName: Full=Alternative RNA polymerase sigma factor SigJ;
DE AltName: Full=RNA polymerase sigma-J factor;
DE Short=Sigma-J factor;
GN Name=sigJ; OrderedLocusNames=Rv3328c;
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 IN LATE STATIONARY PHASE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11506908; DOI=10.1111/j.1574-6968.2001.tb10780.x;
RA Hu Y., Coates A.R.;
RT "Increased levels of sigJ mRNA in late stationary phase cultures of
RT Mycobacterium tuberculosis detected by DNA array hybridisation.";
RL FEMS Microbiol. Lett. 202:59-65(2001).
RN [3]
RP INDUCTION, AND DISRUPTION PHENOTYPE IN MOUSE INFECTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15321691; DOI=10.1111/j.1574-6968.2004.tb09725.x;
RA Hu Y., Kendall S., Stoker N.G., Coates A.R.;
RT "The Mycobacterium tuberculosis sigJ gene controls sensitivity of the
RT bacterium to hydrogen peroxide.";
RL FEMS Microbiol. Lett. 237:415-423(2004).
RN [4]
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 [5]
RP FUNCTION AS A SIGMA FACTOR.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18248429; DOI=10.1111/j.1574-6968.2007.01054.x;
RA Homerova D., Halgasova L., Kormanec J.;
RT "Cascade of extracytoplasmic function sigma factors in Mycobacterium
RT tuberculosis: identification of a sigmaJ-dependent promoter upstream of
RT sigI.";
RL FEMS Microbiol. Lett. 280:120-126(2008).
RN [6]
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 an anti-sigma factor until released, although no anti-
CC sigma factor is known for this protein (By similarity). Regulates the
CC promoter of SigI, may not be autoregulated. {ECO:0000250,
CC ECO:0000269|PubMed:16483748, ECO:0000269|PubMed:18248429}.
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: Undetectable expression in log phase, 18-fold induced by 30
CC days, decreasing slightly after (at protein level). Up-regulated 2.4-
CC fold 7 days after infection of human macrophages.
CC {ECO:0000269|PubMed:11506908, ECO:0000269|PubMed:15321691,
CC ECO:0000269|PubMed:16483748}.
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 difference in growth in culture up to 120
CC days. Increased sensitivity to 10 and 20 mM H(2)O(2), no difference in
CC response to growth at 53 degrees Celsius, pH 4.0, 10% ethanol or 0.05%
CC sodium dodecyl sulfate (surface stress). No detectable difference in
CC spleen or lungs of infected BALB/c mice during 15 weeks growth.
CC {ECO:0000269|PubMed:15321691}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46149.1; -; Genomic_DNA.
DR RefSeq; NP_217845.1; NC_000962.3.
DR RefSeq; WP_009935306.1; NZ_NVQJ01000051.1.
DR PDB; 5XE7; X-ray; 2.16 A; A/B=1-306.
DR PDBsum; 5XE7; -.
DR AlphaFoldDB; L0TCG5; -.
DR SMR; L0TCG5; -.
DR STRING; 83332.Rv3328c; -.
DR PaxDb; L0TCG5; -.
DR DNASU; 887964; -.
DR GeneID; 887964; -.
DR KEGG; mtu:Rv3328c; -.
DR TubercuList; Rv3328c; -.
DR eggNOG; COG1595; Bacteria.
DR InParanoid; L0TCG5; -.
DR OMA; IRWMGAD; -.
DR PhylomeDB; L0TCG5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:MTBBASE.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
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; IPR037401; SnoaL-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
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.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Sigma factor;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..312
FT /note="ECF RNA polymerase sigma factor SigJ"
FT /id="PRO_0000423648"
FT DNA_BIND 131..150
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 6..65
FT /note="Sigma-70 factor domain-2"
FT REGION 107..155
FT /note="Sigma-70 factor domain-4"
FT REGION 293..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 29..32
FT /note="Polymerase core binding"
FT /evidence="ECO:0000255"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:5XE7"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:5XE7"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:5XE7"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:5XE7"
SQ SEQUENCE 312 AA; 33530 MW; F7ABF82998560A5C CRC64;
MEVSEFEALR QHLMSVAYRL TGTVADAEDI VQEAWLRWDS PDTVIADPRA WLTTVVSRLG
LDKLRSAAHR RETYTGTWLP EPVVTGLDAT DPLAAVVAAE DARFAAMVVL ERLRPDQRVA
FVLHDGFAVP FAEVAEVLGT SEAAARQLAS RARKAVTAQP ALISGDPDPA HNEVVGRLMA
AMAAGDLDTV VSLLHPDVTF TGDSNGKAPT AVRAVRGSDK VVRFILGLVQ RYGPGLFGAN
QLALVNGELG AYTAGLPGVD GYRAMAPRIT AITVRDGKVC ALWDIANPDK FTGSPLKERR
AQPTGRGRHH RN
