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 03-AUG-2022, entry version 159.
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).
RN [8]
RP FUNCTION, SUBUNIT, AND INDUCTION BY SPORULATION.
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 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). Associates with the RNAP core only in stationary
CC phase cells (PubMed:21710567). {ECO:0000269|PubMed:21710567,
CC 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 -!- SUBUNIT: Interacts transiently with the RNAP core.
CC {ECO:0000305|PubMed:21710567}.
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, ECO:0000305|PubMed:21710567}.
CC -!- INDUCTION: Association with RNAP core increases during sporulation but
CC not tested stresses (at protein level). {ECO:0000269|PubMed:21710567}.
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};
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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 AlphaFoldDB; P07860; -.
DR SMR; P07860; -.
DR STRING; 224308.BSU23450; -.
DR PaxDb; P07860; -.
DR EnsemblBacteria; CAB14277; CAB14277; BSU_23450.
DR GeneID; 938729; -.
DR KEGG; bsu:BSU23450; -.
DR PATRIC; fig|224308.179.peg.2555; -.
DR eggNOG; COG1191; Bacteria.
DR InParanoid; P07860; -.
DR OMA; RDDGMIK; -.
DR PhylomeDB; P07860; -.
DR BioCyc; BSUB:BSU23450-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:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR001387; Cro/C1-type_HTH.
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;
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
