(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 138.
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 / 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}.
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   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; BSU04720.
DR   GeneID; 938167; -.
DR   KEGG; bsu:BSU04720; -.
DR   PATRIC; fig|224308.179.peg.500; -.
DR   eggNOG; ENOG4108ZBE; Bacteria.
DR   eggNOG; COG2172; LUCA.
DR   HOGENOM; HOG000269932; -.
DR   InParanoid; P17904; -.
DR   KO; K04757; -.
DR   OMA; KPEYVGV; -.
DR   PhylomeDB; P17904; -.
DR   BioCyc; BSUB:BSU04720-MONOMER; -.
DR   PRO; PR:P17904; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0045892; P:negative regulation of transcription, DNA-templated; 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;
DR   PRODOM; P17904.
DR   SWISS-2DPAGE; P17904.
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Stress response;
KW   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)"
SQ   SEQUENCE   160 AA;  17993 MW;  A698AA3114646DA0 CRC64;
     MKNNADYIEM KVPAQPEYVG IIRLTLSGVA SRMGYTYDEI EDLKIAVSEA CTNAVQHAYK
     EDKNGEVSIR FGVFEDRLEV IVADEGDSFD FDQKQQDLGP YTPSHTVDQL SEGGLGLYLM
     ETLMDEVRVQ NHSGVTVAMT KYLNGERVDH DTTIKNYETN
//

If you have problems or comments...

PBIL Back to PBIL home page