(data stored in ACNUC7421 zone)

SWISSPROT: RSBX_BACSU

ID   RSBX_BACSU              Reviewed;         199 AA.
AC   P17906;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   11-DEC-2019, entry version 135.
DE   RecName: Full=Phosphoserine phosphatase RsbX;
DE            EC=3.1.3.3;
DE   AltName: Full=Sigma-B negative effector;
GN   Name=rsbX; OrderedLocusNames=BSU04740;
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;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-179.
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   [5]
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   [6]
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   [7]
RP   FUNCTION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=8824586; DOI=10.1101/gad.10.18.2265;
RA   Yang X., Kang C.M., Brody M.S., Price C.W.;
RT   "Opposing pairs of serine protein kinases and phosphatases transmit signals
RT   of environmental stress to activate a bacterial transcription factor.";
RL   Genes Dev. 10:2265-2275(1996).
RN   [8]
RP   FUNCTION.
RC   STRAIN=PY22;
RX   PubMed=9658013;
RA   Smirnova N., Scott J., Voelker U., Haldenwang W.G.;
RT   "Isolation and characterization of Bacillus subtilis sigB operon mutations
RT   that suppress the loss of the negative regulator RsbX.";
RL   J. Bacteriol. 180:3671-3680(1998).
CC   -!- FUNCTION: Negative regulator of sigma-B activity. Dephosphorylates
CC       RsbS. Plays a role both in maintaining low sigma-B activity during
CC       growth and in reestablishing prestress sigma-B activity after
CC       induction. Could have a negative feedback role by indirectly
CC       communicating sigma-B protein levels. {ECO:0000269|PubMed:1592822,
CC       ECO:0000269|PubMed:8468294, ECO:0000269|PubMed:8824586,
CC       ECO:0000269|PubMed:9658013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC         Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC         Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
DR   EMBL; M34995; AAA22714.1; -; Genomic_DNA.
DR   EMBL; AB001488; BAA19311.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12281.1; -; Genomic_DNA.
DR   PIR; D36131; D36131.
DR   RefSeq; NP_388355.1; NC_000964.3.
DR   RefSeq; WP_003246608.1; NZ_JNCM01000031.1.
DR   PDB; 3W40; X-ray; 1.30 A; A/B=1-199.
DR   PDB; 3W41; X-ray; 1.42 A; A=1-199.
DR   PDB; 3W42; X-ray; 1.06 A; A/B=1-199.
DR   PDB; 3W43; X-ray; 1.22 A; A=1-199.
DR   PDB; 3W44; X-ray; 2.30 A; A/B=1-199.
DR   PDB; 3W45; X-ray; 1.70 A; A/B=1-199.
DR   PDBsum; 3W40; -.
DR   PDBsum; 3W41; -.
DR   PDBsum; 3W42; -.
DR   PDBsum; 3W43; -.
DR   PDBsum; 3W44; -.
DR   PDBsum; 3W45; -.
DR   SMR; P17906; -.
DR   STRING; 224308.BSU04740; -.
DR   PaxDb; P17906; -.
DR   PRIDE; P17906; -.
DR   EnsemblBacteria; CAB12281; CAB12281; BSU04740.
DR   GeneID; 938155; -.
DR   KEGG; bsu:BSU04740; -.
DR   PATRIC; fig|224308.179.peg.502; -.
DR   eggNOG; ENOG41064BQ; Bacteria.
DR   eggNOG; ENOG41126YW; LUCA.
DR   HOGENOM; HOG000270275; -.
DR   InParanoid; P17906; -.
DR   KO; K05518; -.
DR   OMA; YMIGIED; -.
DR   PhylomeDB; P17906; -.
DR   BioCyc; BSUB:BSU04740-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004647; F:phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009408; P:response to heat; IEP:CACAO.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   InterPro; IPR039248; Ptase_RsbX.
DR   PANTHER; PTHR35801; PTHR35801; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P17906.
DR   SWISS-2DPAGE; P17906.
KW   3D-structure; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..199
FT                   /note="Phosphoserine phosphatase RsbX"
FT                   /id="PRO_0000057791"
FT   DOMAIN          11..198
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   STRAND          2..6
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          8..17
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          26..33
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          35..48
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   HELIX           49..65
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   TURN            66..68
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   HELIX           71..81
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   TURN            82..84
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          88..96
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   TURN            97..100
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          101..109
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          111..115
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          127..129
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          140..144
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          150..154
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   HELIX           163..169
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   HELIX           173..179
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   HELIX           180..183
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          184..186
FT                   /evidence="ECO:0000244|PDB:3W42"
FT   STRAND          191..198
FT                   /evidence="ECO:0000244|PDB:3W42"
SQ   SEQUENCE   199 AA;  22144 MW;  2AAEFB96FB072E33 CRC64;
     MIQVEENEHI QTLVYQLNKE GKSICGDSFF MKADDKELIC AVADGLGSGS LANESSAAIK
     DLVENYASED VESIIERCNQ AMKNKRGATA SILKINFEQR QFTYCSVGNV RFILHSPSGE
     SFYPLPISGY LSGKPQKYKT HTATYEKGSK FIIHTDGLNV PDIRSHLKKG QSVEEISNSL
     KMYTTSRKDD LTYILGQLS
//

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