RPSD_MYCTO
ID RPSD_MYCTO Reviewed; 212 AA.
AC P9WGG8; L0TFB3; P66811; Q50712;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=ECF RNA polymerase sigma factor SigD;
DE Short=ECF sigma factor SigD;
DE AltName: Full=Alternative RNA polymerase sigma factor SigD;
DE AltName: Full=RNA polymerase sigma-D factor;
DE AltName: Full=Sigma-D factor;
GN Name=sigD; OrderedLocusNames=MT3523;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 (By similarity). {ECO:0000250}.
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:0000250}.
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 -!- MISCELLANEOUS: Extracytoplasmic function sigma factors (ECF) 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), while cytoplasmic proteases
CC finish degrading the regulatory protein, liberating SigD (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK47861.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK47861.1; ALT_INIT; Genomic_DNA.
DR PIR; C70737; C70737.
DR RefSeq; WP_003418013.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGG8; -.
DR SMR; P9WGG8; -.
DR EnsemblBacteria; AAK47861; AAK47861; MT3523.
DR GeneID; 45427410; -.
DR KEGG; mtc:MT3523; -.
DR PATRIC; fig|83331.31.peg.3780; -.
DR HOGENOM; CLU_047691_10_1_11; -.
DR Proteomes; UP000001020; Chromosome.
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:0009628; P:response to abiotic stimulus; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
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; 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.
DR PROSITE; PS01063; SIGMA70_ECF; 1.
PE 3: Inferred from homology;
KW DNA-binding; Sigma factor; Transcription; Transcription regulation;
KW Virulence.
FT CHAIN 1..212
FT /note="ECF RNA polymerase sigma factor SigD"
FT /id="PRO_0000428364"
FT DNA_BIND 176..195
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 49..119
FT /note="Sigma-70 factor domain-2"
FT REGION 152..201
FT /note="Sigma-70 factor domain-4"
FT MOTIF 75..78
FT /note="Polymerase core binding"
FT /evidence="ECO:0000255"
SQ SEQUENCE 212 AA; 22919 MW; 12A157F6F66BB0C3 CRC64;
MVDPGVSPGC VRFVTLEISP SMTMQGERLD AVVAEAVAGD RNALREVLET IRPIVVRYCR
ARVGTVERSG LSADDVAQEV CLATITALPR YRDRGRPFLA FLYGIAAHKV ADAHRAAGRD
RAYPAETLPE RWSADAGPEQ MAIEADSVTR MNELLEILPA KQREILILRV VVGLSAEETA
AAVGSTTGAV RVAQHRALQR LKDEIVAAGD YA
