RP54_BACSU
ID RP54_BACSU Reviewed; 436 AA.
AC P24219;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=RNA polymerase sigma-54 factor;
GN Name=sigL; OrderedLocusNames=BSU34200;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=1924373; DOI=10.1073/pnas.88.20.9092;
RA Debarbouille M., Martin-Verstraete I., Kunst F., Rapoport G.;
RT "The Bacillus subtilis sigL gene encodes an equivalent of sigma 54 from
RT Gram-negative bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9092-9096(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969506; DOI=10.1099/13500872-142-11-3089;
RA Fabret C., Quentin Y., Chapal N., Guiseppi A., Haiech J., Denizot F.;
RT "Integrated mapping and sequencing of a 115 kb DNA fragment from Bacillus
RT subtilis: sequence analysis of a 21 kb segment containing the sigL locus.";
RL Microbiology 142:3089-3096(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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 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 responsible for the expression
CC of the levanase operon. The open complex (sigma-54 and core RNA
CC polymerase) serves as the receptor for receipt of the melting signal
CC from the remotely bound activator protein LevR for the expression of
CC the levanase operon. Associates with the RNAP core only in stationary
CC phase cells (PubMed:21710567). {ECO:0000269|PubMed:21710567}.
CC -!- SUBUNIT: Interacts transiently with the RNAP core.
CC {ECO:0000305|PubMed:21710567}.
CC -!- INDUCTION: Association with RNAP core increases slightly during late
CC sporulation but not tested stresses (at protein level).
CC {ECO:0000269|PubMed:21710567}.
CC -!- SIMILARITY: Belongs to the sigma-54 factor family. {ECO:0000305}.
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DR EMBL; M73443; AAA22753.1; -; Genomic_DNA.
DR EMBL; Z71928; CAA96485.1; -; Genomic_DNA.
DR EMBL; Z94043; CAB08001.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15425.1; -; Genomic_DNA.
DR PIR; A41229; A41229.
DR RefSeq; NP_391300.1; NC_000964.3.
DR RefSeq; WP_003242595.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P24219; -.
DR SMR; P24219; -.
DR STRING; 224308.BSU34200; -.
DR PaxDb; P24219; -.
DR PRIDE; P24219; -.
DR DNASU; 936362; -.
DR EnsemblBacteria; CAB15425; CAB15425; BSU_34200.
DR GeneID; 936362; -.
DR KEGG; bsu:BSU34200; -.
DR PATRIC; fig|224308.179.peg.3707; -.
DR eggNOG; COG1508; Bacteria.
DR InParanoid; P24219; -.
DR OMA; VTTQKFM; -.
DR PhylomeDB; P24219; -.
DR BioCyc; BSUB:BSU34200-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; 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 Gene3D; 1.10.10.1330; -; 1.
DR InterPro; IPR000394; RNA_pol_sigma_54.
DR InterPro; IPR007046; RNA_pol_sigma_54_core-bd.
DR InterPro; IPR007634; RNA_pol_sigma_54_DNA-bd.
DR InterPro; IPR038709; RpoN_core-bd_sf.
DR PANTHER; PTHR32248; PTHR32248; 1.
DR Pfam; PF00309; Sigma54_AID; 1.
DR Pfam; PF04963; Sigma54_CBD; 1.
DR Pfam; PF04552; Sigma54_DBD; 1.
DR PIRSF; PIRSF000774; RpoN; 1.
DR PRINTS; PR00045; SIGMA54FCT.
DR TIGRFAMs; TIGR02395; rpoN_sigma; 1.
DR PROSITE; PS00717; SIGMA54_1; 1.
DR PROSITE; PS00718; SIGMA54_2; 1.
DR PROSITE; PS50044; SIGMA54_3; 1.
PE 1: Evidence at protein level;
KW DNA-binding; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Sigma factor; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..436
FT /note="RNA polymerase sigma-54 factor"
FT /id="PRO_0000205526"
FT DNA_BIND 324..343
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT MOTIF 413..421
FT /note="RPON box"
SQ SEQUENCE 436 AA; 49701 MW; 48C60D4BD306BF24 CRC64;
MDMKLQQVQV LKPQLTQELR QAITLLGYHS AELAEYIDEL SLENPLIERK ETDTPPLSYH
KTNKNRMNAQ EAGLQLSNPQ KTLQDALKQQ SLDMNLTNTE KKIFNYLIHS LDSNGYLEED
IEEAARRLSV SAKEAEAVLA KLQSLEPAGI GARSLQECIL LQLQRLPNRN EQAEMLVSAH
FDAFAQKKWK TLSVETGIPL HTIQDISDDI AALHPRPGLL FARPEQDVYI EPDIFITVKN
GHIAAELNTR SFPEIDLHPQ YRTLLSSGSC QDTVSYLSAK YQEWRWLSRA LRQRKQTITR
IINELITRQK DFFLKGRSAM KPLTLREVAD CLSLHESTVS RAIKGKTIQT PYGLFEMKLF
FSAKAEASGD GDASNYAVKT HLENLINQED KTKPLSDQKL VDLLYEQHGI QISRRTVAKY
RDQMNIPSSA ARKRYK