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 03-AUG-2022, entry version 144.
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 / 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 [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 / NRRL NRS-744 / 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; DOI=10.1128/jb.180.14.3671-3680.1998;
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;
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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 AlphaFoldDB; P17906; -.
DR SMR; P17906; -.
DR STRING; 224308.BSU04740; -.
DR jPOST; P17906; -.
DR PaxDb; P17906; -.
DR PRIDE; P17906; -.
DR EnsemblBacteria; CAB12281; CAB12281; BSU_04740.
DR GeneID; 938155; -.
DR KEGG; bsu:BSU04740; -.
DR PATRIC; fig|224308.179.peg.502; -.
DR eggNOG; COG2208; Bacteria.
DR InParanoid; P17906; -.
DR OMA; YMIGIED; -.
DR PhylomeDB; P17906; -.
DR BioCyc; BSUB:BSU04740-MON; -.
DR BRENDA; 3.1.3.3; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
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;
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:0007829|PDB:3W42"
FT STRAND 8..17
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 35..48
FT /evidence="ECO:0007829|PDB:3W42"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:3W42"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3W42"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:3W42"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3W42"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3W42"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:3W42"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:3W42"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3W42"
FT STRAND 191..198
FT /evidence="ECO:0007829|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
