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RPSD_BACSU
ID   RPSD_BACSU              Reviewed;         254 AA.
AC   P10726;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=RNA polymerase sigma-D factor;
DE   AltName: Full=Sigma-28;
GN   Name=sigD; Synonyms=flaB; OrderedLocusNames=BSU16470;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2832368; DOI=10.1128/jb.170.4.1568-1574.1988;
RA   Helmann J.D., Marquez L.M., Chamberlin M.J.;
RT   "Cloning, sequencing, and disruption of the Bacillus subtilis sigma 28
RT   gene.";
RL   J. Bacteriol. 170:1568-1574(1988).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 1-20 AND 156-178, SUBUNIT, AND MASS SPECTROMETRY.
RX   PubMed=7602586; DOI=10.1006/jmbi.1995.0333;
RA   Chen Y.-F., Helmann J.D.;
RT   "The Bacillus subtilis flagellar regulatory protein sigma D:
RT   overproduction, domain analysis and DNA-binding properties.";
RL   J. Mol. Biol. 249:743-753(1995).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=8157612; DOI=10.1128/jb.176.8.2427-2434.1994;
RA   Marquez-Magana L.M., Chamberlin M.J.;
RT   "Characterization of the sigD transcription unit of Bacillus subtilis.";
RL   J. Bacteriol. 176:2427-2434(1994).
RN   [5]
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. This alternative sigma factor is required for the
CC       transcription of the flagellin and motility genes as well as for wild-
CC       type chemotaxis. Associates with the RNAP core during all growth phases
CC       with a peak at the transition to stationary phase (PubMed:21710567).
CC       {ECO:0000269|PubMed:21710567}.
CC   -!- SUBUNIT: Monomer (PubMed:7602586). Interacts transiently with the RNAP
CC       core (Probable). {ECO:0000269|PubMed:7602586,
CC       ECO:0000305|PubMed:21710567}.
CC   -!- INDUCTION: Association with RNAP core increases during H(2)O(2), NaOH,
CC       rifampicin stress and during sporulation (at protein level).
CC       {ECO:0000269|PubMed:21710567}.
CC   -!- MASS SPECTROMETRY: Mass=29533; Mass_error=295; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:7602586};
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. {ECO:0000305}.
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DR   EMBL; M20144; AAA61470.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13520.1; -; Genomic_DNA.
DR   PIR; C55216; C55216.
DR   RefSeq; NP_389529.1; NC_000964.3.
DR   RefSeq; WP_003220911.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P10726; -.
DR   SMR; P10726; -.
DR   STRING; 224308.BSU16470; -.
DR   PaxDb; P10726; -.
DR   PRIDE; P10726; -.
DR   EnsemblBacteria; CAB13520; CAB13520; BSU_16470.
DR   GeneID; 64303540; -.
DR   GeneID; 938482; -.
DR   KEGG; bsu:BSU16470; -.
DR   PATRIC; fig|224308.179.peg.1788; -.
DR   eggNOG; COG1191; Bacteria.
DR   InParanoid; P10726; -.
DR   OMA; IKFETYA; -.
DR   PhylomeDB; P10726; -.
DR   BioCyc; BSUB:BSU16470-MON; -.
DR   PRO; PR:P10726; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:CACAO.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
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; IPR012845; RNA_pol_sigma_FliA_WhiG.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF04539; Sigma70_r3; 1.
DR   Pfam; PF04545; Sigma70_r4; 1.
DR   PIRSF; PIRSF000770; RNA_pol_sigma-SigE/K; 1.
DR   PRINTS; PR00046; SIGMA70FCT.
DR   SUPFAM; SSF88659; SSF88659; 2.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02479; FliA_WhiG; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Reference proteome; Sigma factor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..254
FT                   /note="RNA polymerase sigma-D factor"
FT                   /id="PRO_0000093978"
FT   DNA_BIND        220..239
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           54..67
FT                   /note="Polymerase core binding"
SQ   SEQUENCE   254 AA;  29468 MW;  F70D15559F575D59 CRC64;
     MQSLNYEDQV LWTRWKEWKD PKAGDDLMRR YMPLVTYHVG RISVGLPKSV HKDDLMSLGM
     LGLYDALEKF DPSRDLKFDT YASFRIRGAI IDGLRKEDWL PRTSREKTKK VEAAIEKLEQ
     RYLRNVSPAE IAEELGMTVQ DVVSTMNEGF FANLLSIDEK LHDQDDGENI QVMIRDDKNV
     PPEEKIMKDE LIAQLAEKIH ELSEKEQLVV SLFYKEELTL TEIGQVLNLS TSRISQIHSK
     ALFKLKNLLE KVIQ
 
 
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