(data stored in SCRATCH zone)

SWISSPROT: RPSF_BACSU

ID   RPSF_BACSU              Reviewed;         255 AA.
AC   P07860;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   11-DEC-2019, entry version 148.
DE   RecName: Full=RNA polymerase sigma-F factor;
DE   AltName: Full=Sporulation sigma factor;
DE   AltName: Full=Stage II sporulation protein AC;
GN   Name=sigF; Synonyms=spoIIAC; OrderedLocusNames=BSU23450;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   SER-73; 99-ARG--GLY-255; ARG-111; VAL-233; ARG-237 AND 245-GLN--GLY-255.
RC   STRAIN=168 / PY79;
RX   PubMed=3116160; DOI=10.1099/00221287-133-3-475;
RA   Yudkin M.D.;
RT   "Structure and function in a Bacillus subtilis sporulation-specific sigma
RT   factor: molecular nature of mutations in spoIIAC.";
RL   J. Gen. Microbiol. 133:475-481(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PY79;
RX   PubMed=6088674; DOI=10.1099/00221287-130-8-2147;
RA   Fort P., Piggot P.J.;
RT   "Nucleotide sequence of sporulation locus spoIIA in Bacillus subtilis.";
RL   J. Gen. Microbiol. 130:2147-2153(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, ACTIVITY REGULATION, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=CU267;
RX   PubMed=8358793; DOI=10.1016/0092-8674(93)90520-z;
RA   Min K.-T., Hilditch C.M., Diederich B., Errington J., Yudkin M.D.;
RT   "Sigma F, the first compartment-specific transcription factor of B.
RT   subtilis, is regulated by an anti-sigma factor that is also a protein
RT   kinase.";
RL   Cell 74:735-742(1993).
RN   [6]
RP   FUNCTION, AND REGULON.
RC   STRAIN=168 / PY79;
RX   PubMed=8759874; DOI=10.1128/jb.178.16.5039-5041.1996;
RA   Decatur A., Losick R.;
RT   "Identification of additional genes under the control of the transcription
RT   factor sigma F of Bacillus subtilis.";
RL   J. Bacteriol. 178:5039-5041(1996).
RN   [7]
RP   FUNCTION, AND ACTIVITY REGULATION.
RC   STRAIN=168 / PY79;
RX   PubMed=21037003; DOI=10.1128/jb.00949-10;
RA   Camp A.H., Wang A.F., Losick R.;
RT   "A small protein required for the switch from {sigma}F to {sigma}G during
RT   sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 193:116-124(2011).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. This sigma factor is responsible for the expression of
CC       sporulation specific genes (PubMed:8759874). Interaction with SpoIIAB
CC       inhibits sigma-F activity throughout the cell before the formation of
CC       the asymmetric septum; after septation the interaction is confined to
CC       the mother cell, and sigma F activity is released in the prespore.
CC       Responsible for expression of csfB (the anti-sigma-G factor Gin)
CC       (PubMed:8759874). {ECO:0000269|PubMed:8759874}.
CC   -!- ACTIVITY REGULATION: Interaction with SpoIIAB inhibits sigma-F activity
CC       throughout the cell before the formation of the asymmetric septum;
CC       after septation the interaction is confined to the mother cell, and
CC       sigma-F activity is released in the prespore (PubMed:8358793). Fin, a
CC       second, forespore-specific anti-sigma factor is induced in 2 successive
CC       waves by sigma-F and sigma-G, by antagonizing sigma-F it allows the
CC       switch to sigma-G factor and progression to the late sporulation
CC       development stages (PubMed:21037003). {ECO:0000269|PubMed:21037003,
CC       ECO:0000269|PubMed:8358793}.
CC   -!- DEVELOPMENTAL STAGE: Produced in the predivisional sporangium, but does
CC       not become active in directing gene expression until after septum
CC       formation when its activity is restricted to the forespore (at protein
CC       level). {ECO:0000269|PubMed:8358793}.
CC   -!- DISRUPTION PHENOTYPE: In spo-63 (loss of residues 27-255); no spores
CC       develop, no induction of sporulation-associated enzymes.
CC       {ECO:0000269|PubMed:3116160}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22791.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; M15744; AAA22788.1; -; Genomic_DNA.
DR   EMBL; M17643; AAA22791.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; D84432; BAA12655.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14277.1; -; Genomic_DNA.
DR   PIR; A28567; A28567.
DR   RefSeq; NP_390226.1; NC_000964.3.
DR   RefSeq; WP_003230458.1; NZ_JNCM01000036.1.
DR   SMR; P07860; -.
DR   STRING; 224308.BSU23450; -.
DR   PaxDb; P07860; -.
DR   PRIDE; P07860; -.
DR   EnsemblBacteria; CAB14277; CAB14277; BSU23450.
DR   GeneID; 938729; -.
DR   KEGG; bsu:BSU23450; -.
DR   PATRIC; fig|224308.179.peg.2555; -.
DR   eggNOG; ENOG4105CT2; Bacteria.
DR   eggNOG; COG1191; LUCA.
DR   HOGENOM; HOG000270270; -.
DR   InParanoid; P07860; -.
DR   KO; K03091; -.
DR   OMA; NEPMEDI; -.
DR   PhylomeDB; P07860; -.
DR   BioCyc; BSUB:BSU23450-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR014322; RNA_pol_sigma-B/F/G.
DR   InterPro; IPR014236; RNA_pol_sigma-F.
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   PIRSF; PIRSF000770; RNA_pol_sigma-SigE/K; 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; TIGR02885; spore_sigF; 1.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P07860.
DR   SWISS-2DPAGE; P07860.
KW   Direct protein sequencing; DNA-binding; Reference proteome; Sigma factor;
KW   Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..255
FT                   /note="RNA polymerase sigma-F factor"
FT                   /id="PRO_0000093943"
FT   DNA_BIND        221..240
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           61..74
FT                   /note="Polymerase core binding"
FT   MUTAGEN         73
FT                   /note="S->F: In spo-563; 10(6)-fold decrease in spore
FT                   production, 50% induction of sporulation-associated
FT                   enzymes."
FT                   /evidence="ECO:0000269|PubMed:3116160"
FT   MUTAGEN         99..255
FT                   /note="Missing: In spo-578; no spores develop, no induction
FT                   of sporulation-associated enzymes."
FT                   /evidence="ECO:0000269|PubMed:3116160"
FT   MUTAGEN         111
FT                   /note="R->Q: In spo-564; 1000-fold decrease in spore
FT                   production, 50% induction of sporulation-associated
FT                   enzymes."
FT                   /evidence="ECO:0000269|PubMed:3116160"
FT   MUTAGEN         233
FT                   /note="V->M: In spo-561; 10(6)-fold decrease in spore
FT                   production, 50% induction of sporulation-associated
FT                   enzymes."
FT                   /evidence="ECO:0000269|PubMed:3116160"
FT   MUTAGEN         237
FT                   /note="R->K: In spo-560; 1000-fold decrease in spore
FT                   production, 50% induction of sporulation-associated
FT                   enzymes."
FT                   /evidence="ECO:0000269|PubMed:3116160"
FT   MUTAGEN         245..255
FT                   /note="Missing: In spo-1; no spores develop, no induction
FT                   of sporulation-associated enzymes."
FT                   /evidence="ECO:0000269|PubMed:3116160"
SQ   SEQUENCE   255 AA;  29372 MW;  68970E159A1FE7D0 CRC64;
     MDVEVKKNGK NAQLKDHEVK ELIKQSQNGD QQARDLLIEK NMRLVWSVVQ RFLNRGYEPD
     DLFQIGCIGL LKSVDKFDLT YDVRFSTYAV PMIIGEIQRF IRDDGTVKVS RSLKELGNKI
     RRAKDELSKT LGRVPTVQEI ADHLEIEAED VVLAQEAVRA PSSIHETVYE NDGDPITLLD
     QIADNSEEKW FDKIALKEAI SDLEEREKLI VYLRYYKDQT QSEVAERLGI SQVQVSRLEK
     KILKQIKVQM DHTDG
//

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