ID   SIGF_AZOOP              Reviewed;         190 AA.
AC   G8QM61;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=ECF RNA polymerase sigma factor SigF {ECO:0000303|PubMed:25968643};
DE            Short=ECF sigma factor SigF;
GN   Name=sigF {ECO:0000303|PubMed:25968643}; OrderedLocusNames=Dsui_0155;
OS   Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS   suillum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azospira.
OX   NCBI_TaxID=640081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-33 / DSM 13638 / PS;
RX   PubMed=22535943; DOI=10.1128/jb.00124-12;
RA   Byrne-Bailey K.G., Coates J.D.;
RT   "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT   Azospira suillum strain PS.";
RL   J. Bacteriol. 194:2767-2768(2012).
RN   [2]
RP   FUNCTION, REGULON, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-33 / DSM 13638 / PS;
RX   PubMed=25968643; DOI=10.1128/mbio.00233-15;
RA   Melnyk R.A., Youngblut M.D., Clark I.C., Carlson H.K., Wetmore K.M.,
RA   Price M.N., Iavarone A.T., Deutschbauer A.M., Arkin A.P., Coates J.D.;
RT   "Novel mechanism for scavenging of hypochlorite involving a periplasmic
RT   methionine-rich peptide and methionine sulfoxide reductase.";
RL   MBio 6:E00233-E00233(2015).
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 (NrsF in this case) until
CC       they are released (Probable). Regulates expression of only a few genes
CC       (Dsui_0154 to Dsui_0159) in response to (hypo)chlorite, conferring
CC       resistance to reactive chlorine species (RCS) during oxic growth
CC       (PubMed:25968643). {ECO:0000269|PubMed:25968643,
CC       ECO:0000305|PubMed:25968643}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Tightly associated
CC       with the inner cell membrane via NrsF which holds it in an inactive
CC       form until it is released (By similarity).
CC       {ECO:0000250|UniProtKB:A0A0H3CCX2}.
CC   -!- INDUCTION: Part of the SigF regulon, induced by chlorite under auto-
CC       control. Part of the probable sigF-nrsF operon.
CC       {ECO:0000269|PubMed:25968643}.
CC   -!- DISRUPTION PHENOTYPE: Growth inhibited by 100 uM chlorite during
CC       aerobic log-phase growth, no expression of the SigF regulon (Dsui_0156
CC       to Dsui_0159). Growth of a double sigF-yedY2 mutant is completely
CC       inhibited by 20 mM chlorite. {ECO:0000269|PubMed:25968643}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP003153; AEV24577.1; -; Genomic_DNA.
DR   RefSeq; WP_014235279.1; NC_016616.1.
DR   AlphaFoldDB; G8QM61; -.
DR   SMR; G8QM61; -.
DR   STRING; 640081.Dsui_0155; -.
DR   EnsemblBacteria; AEV24577; AEV24577; Dsui_0155.
DR   KEGG; dsu:Dsui_0155; -.
DR   eggNOG; COG1595; Bacteria.
DR   HOGENOM; CLU_047691_10_2_4; -.
DR   OMA; AVKVGIH; -.
DR   OrthoDB; 1914729at2; -.
DR   Proteomes; UP000005633; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0050896; P:response to stimulus; 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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Reference proteome; Sigma factor; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..190
FT                   /note="ECF RNA polymerase sigma factor SigF"
FT                   /id="PRO_0000440885"
FT   DNA_BIND        157..176
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGB6"
FT   REGION          34..102
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000305"
FT   REGION          130..182
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000305"
FT   MOTIF           60..73
FT                   /note="Polymerase core binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGB6"
SQ   SEQUENCE   190 AA;  21617 MW;  A0A06DE6F80E5C30 CRC64;
     MQRINREESF RAKEERLKDL FVRGLSGNNA AYQTFLGELS SYLRAFLRKR LIRLPDEVED
     LVQEALLAVH NQRHTYDPSQ PLSAWVQAIA RYKLVDLFRR RAIYEQRNDT LDDGMDLFSS
     ADAEAAEARR DLNKLLADLP DHFRLPIMHT KLEGLSVREA ADVSGMSESA IKVGVHRGLK
     ALAAKIRGAL