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