ID   RPSB_BACSU              Reviewed;         262 AA.
AC   P06574;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=RNA polymerase sigma-B factor;
DE   AltName: Full=General stress protein 84;
DE            Short=GSP84;
DE   AltName: Full=Sigma-37;
GN   Name=sigB; Synonyms=rpoF; OrderedLocusNames=BSU04730;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3016731; DOI=10.1073/pnas.83.16.5943;
RA   Binnie C., Lampe M., Losick R.;
RT   "Gene encoding the sigma 37 species of RNA polymerase sigma factor from
RT   Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:5943-5947(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=3027048; DOI=10.1128/jb.169.2.771-778.1987;
RA   Duncan M.L., Kalman S.S., Thomas S.M., Price C.W.;
RT   "Gene encoding the 37,000-dalton minor sigma factor of Bacillus subtilis
RT   RNA polymerase: isolation, nucleotide sequence, chromosomal locus, and
RT   cryptic function.";
RL   J. Bacteriol. 169:771-778(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=2170324; DOI=10.1128/jb.172.10.5575-5585.1990;
RA   Kalman S., Duncan M.L., Thomas S.M., Price C.W.;
RT   "Similar organization of the sigB and spoIIA operons encoding alternate
RT   sigma factors of Bacillus subtilis RNA polymerase.";
RL   J. Bacteriol. 172:5575-5585(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-22.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [7]
RP   FUNCTION, SUBUNIT, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=21710567; DOI=10.1002/pmic.201000790;
RA   Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA   Hecker M., Becher D., Polard P., Noirot P.;
RT   "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL   Proteomics 11:2992-3001(2011).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase (RNAP) to specific initiation sites and
CC       are then released. Sigma B is not essential for sporulation; rather it
CC       is required for maximal expression of ctc and csbA which are
CC       transcribed in the early stationary phase under conditions inimical to
CC       sporulation. May play a role in the ability of the bacterium to adapt
CC       to various stresses but is not essential for its survival under these
CC       conditions. Positively regulates expression of its own operon. The
CC       second most abundant sigma factor, it associates with RNAP core under
CC       all growth phases (PubMed:21710567). {ECO:0000269|PubMed:21710567}.
CC   -!- SUBUNIT: Interacts transiently with the RNAP core.
CC       {ECO:0000305|PubMed:21710567}.
CC   -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC       limitation, oxygen limitation and entry into stationary phase.
CC       Association with RNAP core increases during alcohol, NaOH, NaCl stress
CC       and during sporulation (at protein level) (PubMed:21710567).
CC       {ECO:0000269|PubMed:21710567}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. SigB subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAA22715.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA19310.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M13927; AAA22754.1; -; Genomic_DNA.
DR   EMBL; M14508; AAA22715.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M34995; AAA22713.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AB001488; BAA19310.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB12280.2; -; Genomic_DNA.
DR   PIR; A27762; A25944.
DR   RefSeq; NP_388354.2; NC_000964.3.
DR   RefSeq; WP_003246715.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; P06574; -.
DR   SMR; P06574; -.
DR   IntAct; P06574; 6.
DR   STRING; 224308.BSU04730; -.
DR   PaxDb; P06574; -.
DR   PRIDE; P06574; -.
DR   EnsemblBacteria; CAB12280; CAB12280; BSU_04730.
DR   GeneID; 939937; -.
DR   KEGG; bsu:BSU04730; -.
DR   PATRIC; fig|224308.179.peg.501; -.
DR   eggNOG; COG1191; Bacteria.
DR   InParanoid; P06574; -.
DR   OMA; FIRDKTW; -.
DR   PhylomeDB; P06574; -.
DR   BioCyc; BSUB:BSU04730-MON; -.
DR   Proteomes; UP000001570; 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:0043620; P:regulation of DNA-templated transcription in response to stress; IMP:CACAO.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR014288; RNA_pol_sigma-B.
DR   InterPro; IPR014322; RNA_pol_sigma-B/F/G.
DR   InterPro; IPR000943; RNA_pol_sigma70.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR007624; RNA_pol_sigma70_r3.
DR   InterPro; IPR007630; RNA_pol_sigma70_r4.
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   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF04539; Sigma70_r3; 1.
DR   Pfam; PF04545; Sigma70_r4; 1.
DR   PRINTS; PR00046; SIGMA70FCT.
DR   SUPFAM; SSF88659; SSF88659; 2.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02980; SigBFG; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   TIGRFAMs; TIGR02941; Sigma_B; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Reference proteome; Sigma factor;
KW   Stress response; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298659"
FT   CHAIN           2..262
FT                   /note="RNA polymerase sigma-B factor"
FT                   /id="PRO_0000093939"
FT   DNA_BIND        224..243
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           58..71
FT                   /note="Polymerase core binding"
SQ   SEQUENCE   262 AA;  29901 MW;  CAFC038982167CD1 CRC64;
     MTQPSKTTKL TKDEVDRLIS DYQTKQDEQA QETLVRVYTN LVDMLAKKYS KGKSFHEDLR
     QVGMIGLLGA IKRYDPVVGK SFEAFAIPTI IGEIKRFLRD KTWSVHVPRR IKELGPRIKM
     AVDQLTTETQ RSPKVEEIAE FLDVSEEEVL ETMEMGKSYQ ALSVDHSIEA DSDGSTVTIL
     DIVGSQEDGY ERVNQQLMLQ SVLHVLSDRE KQIIDLTYIQ NKSQKETGDI LGISQMHVSR
     LQRKAVKKLR EALIEDPSME LM