RSBQ_BACSU
ID RSBQ_BACSU Reviewed; 269 AA.
AC O07015;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sigma factor SigB regulation protein RsbQ;
GN Name=rsbQ; Synonyms=yvfQ; OrderedLocusNames=BSU34100;
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;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP INDUCTION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=10632888; DOI=10.1046/j.1365-2958.2000.01697.x;
RA Vijay K., Brody M.S., Fredlund E., Price C.W.;
RT "A PP2C phosphatase containing a PAS domain is required to convey signals
RT of energy stress to the sigmaB transcription factor of Bacillus subtilis.";
RL Mol. Microbiol. 35:180-188(2000).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF SER-96 AND HIS-247.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=11591687; DOI=10.1128/jb.183.21.6422-6428.2001;
RA Brody M.S., Vijay K., Price C.W.;
RT "Catalytic function of an alpha/beta hydrolase is required for energy
RT stress activation of the sigma(B) transcription factor in Bacillus
RT subtilis.";
RL J. Bacteriol. 183:6422-6428(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-269.
RC STRAIN=168;
RX PubMed=15632289; DOI=10.1110/ps.041170005;
RA Kaneko T., Tanaka N., Kumasaka T.;
RT "Crystal structures of RsbQ, a stress-response regulator in Bacillus
RT subtilis.";
RL Protein Sci. 14:558-565(2005).
CC -!- FUNCTION: Positive regulator required for energy stress activation of
CC the sigma-B transcription factor. Could be required for RsbP
CC phosphatase activity. {ECO:0000269|PubMed:11591687}.
CC -!- INDUCTION: Induced by entry into stationary phase, but not by carbon
CC and energy starvation. {ECO:0000269|PubMed:10632888}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; Z94043; CAB08011.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15415.1; -; Genomic_DNA.
DR PIR; H70038; H70038.
DR RefSeq; NP_391290.1; NC_000964.3.
DR RefSeq; WP_003228292.1; NZ_JNCM01000033.1.
DR PDB; 1WOM; X-ray; 2.50 A; A/B=5-269.
DR PDB; 1WPR; X-ray; 2.60 A; A/B=5-269.
DR PDBsum; 1WOM; -.
DR PDBsum; 1WPR; -.
DR AlphaFoldDB; O07015; -.
DR SMR; O07015; -.
DR STRING; 224308.BSU34100; -.
DR DrugBank; DB04349; (S)-propane-1,2-diol.
DR DrugBank; DB03297; Benzylsulfonic acid.
DR DrugBank; DB02175; Malonic acid.
DR ESTHER; bacsu-yvfQ; RsbQ-like.
DR PaxDb; O07015; -.
DR PRIDE; O07015; -.
DR EnsemblBacteria; CAB15415; CAB15415; BSU_34100.
DR GeneID; 935930; -.
DR KEGG; bsu:BSU34100; -.
DR PATRIC; fig|224308.179.peg.3697; -.
DR eggNOG; COG0596; Bacteria.
DR InParanoid; O07015; -.
DR OMA; VCPSPCF; -.
DR PhylomeDB; O07015; -.
DR BioCyc; BSUB:BSU34100-MON; -.
DR EvolutionaryTrace; O07015; -.
DR Proteomes; UP000001570; Chromosome.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..269
FT /note="Sigma factor SigB regulation protein RsbQ"
FT /id="PRO_0000097469"
FT ACT_SITE 96
FT /evidence="ECO:0000305"
FT ACT_SITE 219
FT /evidence="ECO:0000305"
FT ACT_SITE 247
FT /evidence="ECO:0000305"
FT MUTAGEN 96
FT /note="S->A: Loss of energy stress signaling."
FT /evidence="ECO:0000269|PubMed:11591687"
FT MUTAGEN 247
FT /note="H->A: Loss of energy stress signaling."
FT /evidence="ECO:0000269|PubMed:11591687"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1WOM"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1WOM"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1WOM"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1WPR"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1WOM"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:1WOM"
FT STRAND 234..247
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:1WOM"
FT HELIX 254..268
FT /evidence="ECO:0007829|PDB:1WOM"
SQ SEQUENCE 269 AA; 30020 MW; 5A02E6C10A340AF4 CRC64;
MNEAILSRNH VKVKGSGKAS IMFAPGFGCD QSVWNAVAPA FEEDHRVILF DYVGSGHSDL
RAYDLNRYQT LDGYAQDVLD VCEALDLKET VFVGHSVGAL IGMLASIRRP ELFSHLVMVG
PSPCYLNDPP EYYGGFEEEQ LLGLLEMMEK NYIGWATVFA ATVLNQPDRP EIKEELESRF
CSTDPVIARQ FAKAAFFSDH REDLSKVTVP SLILQCADDI IAPATVGKYM HQHLPYSSLK
QMEARGHCPH MSHPDETIQL IGDYLKAHV
