RSBW_BACSU
ID RSBW_BACSU Reviewed; 160 AA.
AC P17904;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine-protein kinase RsbW;
DE EC=2.7.11.1;
DE AltName: Full=Anti-sigma-B factor;
DE AltName: Full=Sigma-B negative effector RsbW;
GN Name=rsbW; OrderedLocusNames=BSU04720;
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;
RX PubMed=2170324; DOI=10.1128/jb.172.10.5575-5585.1990;
RA Kalman S., Duncan M.L., Thomas S.M., Price C.W.;
RT "Similar organization of the sigB and spoIIA operons encoding alternate
RT sigma factors of Bacillus subtilis RNA polymerase.";
RL J. Bacteriol. 172:5575-5585(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=3027048; DOI=10.1128/jb.169.2.771-778.1987;
RA Duncan M.L., Kalman S.S., Thomas S.M., Price C.W.;
RT "Gene encoding the 37,000-dalton minor sigma factor of Bacillus subtilis
RT RNA polymerase: isolation, nucleotide sequence, chromosomal locus, and
RT cryptic function.";
RL J. Bacteriol. 169:771-778(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT subtilis genome.";
RL Submitted (MAR-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 PROTEIN SEQUENCE OF 1-15.
RC STRAIN=168 / IS58;
RX PubMed=8012595; DOI=10.1099/00221287-140-4-741;
RA Voelker U., Engelmann S., Maul B., Riethdorf S., Voelker A., Schmid R.,
RA Mach H., Hecker M.;
RT "Analysis of the induction of general stress proteins of Bacillus
RT subtilis.";
RL Microbiology 140:741-752(1994).
RN [6]
RP FUNCTION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=1592822; DOI=10.1128/jb.174.11.3695-3706.1992;
RA Boylan S.A., Rutherford A., Thomas S.M., Price C.W.;
RT "Activation of Bacillus subtilis transcription factor sigma B by a
RT regulatory pathway responsive to stationary-phase signals.";
RL J. Bacteriol. 174:3695-3706(1992).
RN [7]
RP FUNCTION.
RC STRAIN=PY22;
RX PubMed=8468294; DOI=10.1128/jb.175.8.2347-2356.1993;
RA Benson A.K., Haldenwang W.G.;
RT "Regulation of sigma B levels and activity in Bacillus subtilis.";
RL J. Bacteriol. 175:2347-2356(1993).
RN [8]
RP FUNCTION.
RC STRAIN=PY22;
RX PubMed=8144446; DOI=10.1128/jb.176.7.1813-1820.1994;
RA Dufour A., Haldenwang W.G.;
RT "Interactions between a Bacillus subtilis anti-sigma factor (RsbW) and its
RT antagonist (RsbV).";
RL J. Bacteriol. 176:1813-1820(1994).
RN [9]
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=SG38;
RX PubMed=12270815; DOI=10.1128/jb.184.20.5583-5589.2002;
RA Delumeau O., Lewis R.J., Yudkin M.D.;
RT "Protein-protein interactions that regulate the energy stress activation of
RT sigma(B) in Bacillus subtilis.";
RL J. Bacteriol. 184:5583-5589(2002).
CC -!- FUNCTION: Negative regulator of sigma-B activity. Phosphorylates and
CC inactivates its specific antagonist protein, RsbV. Upon phosphorylation
CC of RsbV, RsbW is released and binds to sigma-B, thereby blocking its
CC ability to form an RNA polymerase holoenzyme (E-sigma-B).
CC {ECO:0000269|PubMed:1592822, ECO:0000269|PubMed:8144446,
CC ECO:0000269|PubMed:8468294}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: The higher affinity of RsbW for RsbV than for
CC sigma-B, rather than a difference in the concentrations of RsbV and
CC sigma-B, is the driving force that is responsible for the switch of
CC RsbW to non-phosphorylated RsbV. The kinase activity of RsbW is
CC directly regulated by changes in the ATP/ADP ratio.
CC -!- SUBUNIT: Homodimer. In stressed cells, forms a complex with RsbV. The
CC predominant form of this complex has a stoichiometry of 2:2 (one dimer
CC of RsbW is bound by two monomers of RsbV). In unstressed cells, forms a
CC 2:1 complex with sigma-B.
CC -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC limitation and oxygen limitation.
CC -!- MASS SPECTROMETRY: Mass=36220; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12270815};
CC -!- SIMILARITY: Belongs to the anti-sigma-factor family. {ECO:0000305}.
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DR EMBL; M34995; AAA22712.1; -; Genomic_DNA.
DR EMBL; AB001488; BAA19309.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12279.1; -; Genomic_DNA.
DR PIR; B36131; B36131.
DR RefSeq; NP_388353.1; NC_000964.3.
DR RefSeq; WP_003234299.1; NZ_JNCM01000031.1.
DR PDB; 6M36; X-ray; 3.40 A; A/C/E/G/I/K/M/O=5-145.
DR PDB; 6M37; X-ray; 3.10 A; A/C=5-145.
DR PDBsum; 6M36; -.
DR PDBsum; 6M37; -.
DR AlphaFoldDB; P17904; -.
DR SMR; P17904; -.
DR BioGRID; 855787; 1.
DR DIP; DIP-319N; -.
DR IntAct; P17904; 7.
DR STRING; 224308.BSU04720; -.
DR PaxDb; P17904; -.
DR PRIDE; P17904; -.
DR DNASU; 938167; -.
DR EnsemblBacteria; CAB12279; CAB12279; BSU_04720.
DR GeneID; 938167; -.
DR KEGG; bsu:BSU04720; -.
DR PATRIC; fig|224308.179.peg.500; -.
DR eggNOG; COG2172; Bacteria.
DR InParanoid; P17904; -.
DR OMA; KPEYVGV; -.
DR PhylomeDB; P17904; -.
DR BioCyc; BSUB:BSU04720-MON; -.
DR PRO; PR:P17904; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016989; F:sigma factor antagonist activity; IMP:CACAO.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00638; Anti_sigma_B; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010193; RsbW.
DR Pfam; PF13581; HATPase_c_2; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR01924; rsbW_low_gc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transferase.
FT CHAIN 1..160
FT /note="Serine-protein kinase RsbW"
FT /id="PRO_0000203532"
FT VARIANT 14
FT /note="A -> S (in strain: IS58)"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:6M37"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6M37"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:6M37"
FT HELIX 37..60
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:6M37"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:6M37"
SQ SEQUENCE 160 AA; 17993 MW; A698AA3114646DA0 CRC64;
MKNNADYIEM KVPAQPEYVG IIRLTLSGVA SRMGYTYDEI EDLKIAVSEA CTNAVQHAYK
EDKNGEVSIR FGVFEDRLEV IVADEGDSFD FDQKQQDLGP YTPSHTVDQL SEGGLGLYLM
ETLMDEVRVQ NHSGVTVAMT KYLNGERVDH DTTIKNYETN
