SIGH_MYCBO
ID SIGH_MYCBO Reviewed; 216 AA.
AC P66808; A0A1R3Y3H2; O05843; X2BMK2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ECF RNA polymerase sigma factor SigH;
DE Short=ECF sigma factor SigH;
DE AltName: Full=Alternative RNA polymerase sigma factor SigH;
DE AltName: Full=RNA polymerase sigma-H factor;
DE Short=Sigma-H factor;
GN Name=sigH; Synonyms=rpoE; OrderedLocusNames=BQ2027_MB3250C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP INDUCTION.
RC STRAIN=BCG;
RX PubMed=10400584; DOI=10.1128/jb.181.14.4266-4274.1999;
RA Fernandes N.D., Wu Q.-L., Kong D., Puyang X., Garg S., Husson R.N.;
RT "A mycobacterial extracytoplasmic sigma factor involved in survival
RT following heat shock and oxidative stress.";
RL J. Bacteriol. 181:4266-4274(1999).
RN [4]
RP PHOSPHORYLATION AT THR-106 AND THR-110.
RC STRAIN=BCG;
RX PubMed=18728196; DOI=10.1073/pnas.0801143105;
RA Park S.T., Kang C.M., Husson R.N.;
RT "Regulation of the SigH stress response regulon by an essential protein
RT kinase in Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13105-13110(2008).
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 (RshA) until released.
CC This sigma factor is involved in heat shock and oxidative stress
CC response; it is believed to control protein processing in the
CC extracytoplasmic compartment (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. Interacts (via sigma-70 factor domain 4) with anti-
CC sigma-H factor RshA which prevents its interaction with RNA polymerase
CC (By similarity). {ECO:0000250}.
CC -!- INDUCTION: By heat shock at 50 degrees Celsius.
CC {ECO:0000269|PubMed:10400584}.
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 -!- PTM: Phosphorylated in vivo, probably on Thr-106 and/or Thr-110, when
CC PknB is overexpressed. {ECO:0000269|PubMed:18728196}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIU01879.1; -; Genomic_DNA.
DR RefSeq; NP_856895.1; NC_002945.3.
DR RefSeq; WP_003416897.1; NC_002945.4.
DR AlphaFoldDB; P66808; -.
DR SMR; P66808; -.
DR iPTMnet; P66808; -.
DR EnsemblBacteria; SIU01879; SIU01879; BQ2027_MB3250C.
DR PATRIC; fig|233413.5.peg.3578; -.
DR OMA; NAKAWLF; -.
DR Proteomes; UP000001419; 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; IPR014293; RNA_pol_sigma70_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; 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; TIGR02947; SigH_actino; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS01063; SIGMA70_ECF; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Phosphoprotein; Sigma factor; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..216
FT /note="ECF RNA polymerase sigma factor SigH"
FT /id="PRO_0000094005"
FT DNA_BIND 166..185
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..99
FT /note="Sigma-70 factor domain-2"
FT REGION 140..191
FT /note="Sigma-70 factor domain-4"
FT MOTIF 56..69
FT /note="Polymerase core binding"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:18728196"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:18728196"
SQ SEQUENCE 216 AA; 24225 MW; AC0C33B47DB40CFD CRC64;
MADIDGVTGS AGLQPGPSEE TDEELTARFE RDAIPLLDQL YGGALRMTRN PADAEDLLQE
TMVKAYAGFR SFRHGTNLKA WLYRILTNTY INSYRKKQRQ PAEYPTEQIT DWQLASNAEH
SSTGLRSAEV EALEALPDTE IKEALQALPE EFRMAVYYAD VEGFPYKEIA EIMDTPIGTV
MSRLHRGRRQ LRGLLADVAR DRGFARGEQA HEGVSS
