SIGA_BACSU
ID SIGA_BACSU Reviewed; 371 AA.
AC P06224;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=RNA polymerase sigma factor SigA {ECO:0000255|HAMAP-Rule:MF_00963};
DE AltName: Full=Sigma-43;
DE AltName: Full=Sigma-A;
GN Name=sigA {ECO:0000255|HAMAP-Rule:MF_00963}; Synonyms=rpoD;
GN OrderedLocusNames=BSU25200;
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=2987246; DOI=10.1016/s0021-9258(17)39591-1;
RA Gitt M.A., Wang L.-F., Doi R.H.;
RT "A strong sequence homology exists between the major RNA polymerase sigma
RT factors of Bacillus subtilis and Escherichia coli.";
RL J. Biol. Chem. 260:7178-7185(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3086839; DOI=10.1093/nar/14.10.4293;
RA Wang L.F., Doi R.H.;
RT "Nucleotide sequence and organization of Bacillus subtilis RNA polymerase
RT major sigma (sigma 43) operon.";
RL Nucleic Acids Res. 14:4293-4307(1986).
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 SEQUENCE REVISION TO 165.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-371.
RC STRAIN=168;
RX PubMed=2166045; DOI=10.1016/s0021-9258(18)77439-5;
RA von Wachenfeldt C., Hederstedt L.;
RT "Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by cccA consists
RT of a membrane-anchor and a heme domain.";
RL J. Biol. Chem. 265:13939-13948(1990).
RN [7]
RP PROTEIN SEQUENCE OF 81-90, AND CONFORMATIONAL CHANGE.
RX PubMed=8363585; DOI=10.1042/bj2940043;
RA Chang B.-Y., Doi R.H.;
RT "Conformational properties of Bacillus subtilis RNA polymerase sigma A
RT factor during transcription initiation.";
RL Biochem. J. 294:43-47(1993).
RN [8]
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 sigma factor is the primary sigma factor during
CC all growth phases, stress and during sporulation. It associates with
CC the RNAP core at all growth stages with a slight increase in stationary
CC phase. {ECO:0000269|PubMed:21710567}.
CC -!- SUBUNIT: Interacts transiently with the RNAP core. {ECO:0000255|HAMAP-
CC Rule:MF_00963, ECO:0000305|PubMed:21710567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}.
CC -!- INDUCTION: Association with RNAP core remains approximately constant
CC during all stresses tested and during sporulation (at protein level).
CC {ECO:0000269|PubMed:21710567}.
CC -!- MISCELLANEOUS: A conformational change of sigma-A occurs during its
CC association with the core enzyme. {ECO:0000269|PubMed:8363585}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00963}.
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DR EMBL; M10089; AAA22709.1; -; Genomic_DNA.
DR EMBL; X03897; CAA27538.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12489.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14450.2; -; Genomic_DNA.
DR EMBL; J05569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A22626; RNBS43.
DR RefSeq; NP_390399.2; NC_000964.3.
DR RefSeq; WP_003226225.1; NZ_JNCM01000036.1.
DR PDB; 5MWW; NMR; -; A=2-72.
DR PDB; 7CKQ; EM; 4.40 A; F=1-371.
DR PDB; 7F75; EM; 4.20 A; F=1-371.
DR PDBsum; 5MWW; -.
DR PDBsum; 7CKQ; -.
DR PDBsum; 7F75; -.
DR AlphaFoldDB; P06224; -.
DR BMRB; P06224; -.
DR SMR; P06224; -.
DR IntAct; P06224; 2.
DR STRING; 224308.BSU25200; -.
DR jPOST; P06224; -.
DR PaxDb; P06224; -.
DR PRIDE; P06224; -.
DR EnsemblBacteria; CAB14450; CAB14450; BSU_25200.
DR GeneID; 50136979; -.
DR GeneID; 64304311; -.
DR GeneID; 937897; -.
DR KEGG; bsu:BSU25200; -.
DR PATRIC; fig|224308.179.peg.2740; -.
DR eggNOG; COG0568; Bacteria.
DR InParanoid; P06224; -.
DR OMA; YQRWLAE; -.
DR PhylomeDB; P06224; -.
DR BioCyc; BSUB:BSU25200-MON; -.
DR PRO; PR:P06224; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 1.10.220.120; -; 1.
DR HAMAP; MF_00963; Sigma70_RpoD_SigA; 1.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR000943; RNA_pol_sigma70.
DR InterPro; IPR009042; RNA_pol_sigma70_r1_2.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR007624; RNA_pol_sigma70_r3.
DR InterPro; IPR007630; RNA_pol_sigma70_r4.
DR InterPro; IPR007127; RNA_pol_sigma_70_r1_1.
DR InterPro; IPR042189; RNA_pol_sigma_70_r1_1_sf.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR012760; RNA_pol_sigma_RpoD_C.
DR InterPro; IPR028630; Sigma70_RpoD.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF03979; Sigma70_r1_1; 1.
DR Pfam; PF00140; Sigma70_r1_2; 1.
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; TIGR02393; RpoD_Cterm; 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 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome; Sigma factor; Transcription; Transcription regulation.
FT CHAIN 1..371
FT /note="RNA polymerase sigma factor SigA"
FT /id="PRO_0000093874"
FT DNA_BIND 332..351
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 138..208
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 217..293
FT /note="Sigma-70 factor domain-3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 306..359
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT MOTIF 162..165
FT /note="Interaction with polymerase core subunit RpoC"
FT CONFLICT 165
FT /note="Q -> H (in Ref. 1; AAA22709, 2; CAA27538 and 3;
FT BAA12489)"
FT /evidence="ECO:0000305"
FT HELIX 13..27
FT /evidence="ECO:0007829|PDB:5MWW"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:5MWW"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:5MWW"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:5MWW"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:5MWW"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5MWW"
SQ SEQUENCE 371 AA; 42948 MW; 71EF04508FBF6471 CRC64;
MADKQTHETE LTFDQVKEQL TESGKKRGVL TYEEIAERMS SFEIESDQMD EYYEFLGEQG
VELISENEET EDPNIQQLAK AEEEFDLNDL SVPPGVKIND PVRMYLKEIG RVNLLSAKEE
IAYAQKIEEG DEESKRRLAE ANLRLVVSIA KRYVGRGMLF LDLIQEGNMG LMKAVEKFDY
RKGYKFSTYA TWWIRQAITR AIADQARTIR IPVHMVETIN KLIRVQRQLL QDLGREPTPE
EIAEDMDLTP EKVREILKIA QEPVSLETPI GEEDDSHLGD FIEDQEATSP SDHAAYELLK
EQLEDVLDTL TDREENVLRL RFGLDDGRTR TLEEVGKVFG VTRERIRQIE AKALRKLRHP
SRSKRLKDFL E
