Jump to navigation
Jump to search
⊟Summary[edit | edit source]
- pan ID?: SAUPAN005336000
- symbol?: rsbU
- synonym:
- description?: serine phosphatase
- serine phosphatase
- PP2C family protein-serine/threonine phosphatase
- sigma-B regulation protein
- sigmaB regulation protein RsbU
- sigma-B regulation protein serine phosphatase RsbU
- sigma factor B regulator protein
- sigma factor sigB regulation protein
- SpoIIE family protein phosphatase
- phosphoserine phosphatase rsbU (Sigma factor sigBregulation protein rsbU)
- indirect positive regulator of sigma B
- putative sigma factor sigB regulation protein
- Serine phosphatase RsbU, regulator of sigma subunit
- sigma factor B regulation protein
- stage II sporulation E family protein
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5513670..5514469
- synteny block?: BlockID0041330
- occurrence?: in 100% of 34 strains
rsbU : RsbV-specific serine-protein phosphatase [1]
Regulation of SigB is largely dependent on the availability of the anti-sigma factor RsbW. Under normal conditions, RsbW binds SigB and sequesters it in an inactive confirmation. Alternatively, RsbW can bind RsbV, releasing SigB. Thus, RsbV acts as an "anti-anti-sigma factor". RsbW has a second domain that acts as an RsbV-specific kinase. RsbW can't bind to phosphorylated RsbV, thus maintaining a default state of RsbW-SigB sequestration as long as sufficient ATP is around to keep RsbV phosphorylated. When ATP levels drop or when levels of the RsbV-specific phosphatase RsbU increase, RsbW-RsbV binding becomes favored and SigB-dependent transcription is activated.
⊟Orthologs[edit | edit source]
04-02981:
SA2981_2008 (rsbU)
08BA02176:
C248_2078 (rsbU)
11819-97:
MS7_2084 (rsbU)
6850:
RSAU_001907 (rsbU)
71193:
ST398NM01_2108
ECT-R 2:
ECTR2_1923
ED133:
SAOV_2109c
ED98:
SAAV_2120 (rsbU)
HO 5096 0412:
SAEMRSA15_19770 (rsbU)
JH1:
SaurJH1_2141
JH9:
SaurJH9_2104
JKD6008:
SAA6008_02106 (rsbU)
JKD6159:
SAA6159_01982 (rsbU)
JSNZ:
JSNZ_002028
LGA251:
SARLGA251_18700 (rsbU)
M013:
M013TW_2026
MRSA252:
SAR2155 (rsbU)
MSHR1132:
SAMSHR1132_18920
MSSA476:
SAS1972
Mu3:
SAHV_2052 (rsbU)
Mu50:
SAV2067 (rsbU)
MW2:
MW1991 (rsbU)
RF122:
SAB1952c (rsbU)
ST398:
SAPIG2108
T0131:
SAT0131_02224
TCH60:
HMPREF0772_11128 (rsbU)
TW20:
SATW20_22070 (rsbU)
USA300_TCH1516:
USA300HOU_2062 (rsbU)
VC40:
SAVC_09215
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MEEFKQHYKGLIDESLTCQDKVELIKKCEKYTDEVIRKDVLPEDIVDIHKNYILTLNLTR
N315 MEEFKQHYKGLIDESLTCQDKVELIKKCEKYTDEVIRKDVLPEDIVDIHKNYILTLNLTR
Newman MEEFKQHYKGLIDESLTCQDKVELIKKCEKYTDEVIRKDVLPEDIVDIHKNYILTLNLTR
USA300_FPR3757 MEEFKQHYKGLIDESLTCQDKVELIKKCEKYTDEVIRKDVLPEDIVDIHKNYILTLNLTR
************************************************************
COL EDVFKTLDVLQEIVKGFGYSYRDYQRLVDKLQVHDKEIDLASSLQQTMLKTDIPQFDSIQ
N315 EDVFKTLDVLQEIVKGFGYSYRDYQRLVDKLQVHDKEIDLASSLQQTMLKTDIPQFDSIQ
Newman EDVFKTLDVLQEIVKGFGYSYRDYQRLVDKLQVHDKEIDLASSLQQTMLKTDIPQFDSIQ
USA300_FPR3757 EDVFKTLDVLQEIVKGFGYSYRDYQRLVDKLQVHDKEIDLASSLQQTMLKTDIPQFDSIQ
************************************************************
COL IGVISVAAQKVSGDYFNLIDHNDGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQLP
N315 IGVISVAAQKVSGDYFNLIDHNDGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQLP
Newman IGVISVAAQKVSGDYFNLIDHNDGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQLP
USA300_FPR3757 IGVISVAAQKVSGDYFNLIDHNDGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQLP
************************************************************
COL SDGLKRLNRVVEKNINQNMFVTMFYGLYEEMNHLLYCSSAGHEPGYIYRAEKEEFEEISV
N315 SDGLKRLNRVVEKNINQNMFVTMFYGLYEEMNHLLYCSSAGHEPGYIYRAEKEEFEEISV
Newman SDGLKRLNRVVEKNINQNMFVTMFYGLYEEMNHLLYCSSAGHEPGYIYRAEKEEFEEISV
USA300_FPR3757 SDGLKRLNRVVEKNINQNMFVTMFYGLYEEMNHLLYCSSAGHEPGYIYRAEKEEFEEISV
************************************************************
COL RGRVLGISSQTRYQQQEIPIYLDDLIIILTDGVTEARNSEGTFIDKQKLLEYIKKHKHMH
N315 RGRVLGISSQTRYQQQEIPIYLDDLIIILTDGVTEARNSEGTFIDKQKLLEYIKKHKHMH
Newman RGRVLGISSQTRYQQQEIPIYLDDLIIILTDGVTEARNSEGTFIDKQKLLEYIKKHKHMH
USA300_FPR3757 RGRVLGISSQTRYQQQEIPIYLDDLIIILTDGVTEARNSEGTFIDKQKLLEYIKKHKHMH
************************************************************
COL PQDIVQIIYEAILKLQNPNKKDDMTILIIKRVN
N315 PQDIVQIIYEAILKLQNPNKKDDMTILIIKRVN
Newman PQDIVQIIYEAILKLQNPNKKDDMTILIIKRVN
USA300_FPR3757 PQDIVQIIYEAILKLQNPNKKDDMTILIIKRVN
*********************************
- ↑ P Giachino, S Engelmann, M Bischoff
Sigma(B) activity depends on RsbU in Staphylococcus aureus.
J Bacteriol: 2001, 183(6);1843-52
[PubMed:11222581] [WorldCat.org] [DOI] (P p)J GERENDASY
Treatment of complete rectal prolapse with sclerosing agents.
J Int Coll Surg: 1954, 22(3 Pt 1);292-8
[PubMed:13201800] [WorldCat.org] (P p)Olivier Delumeau, Sujit Dutta, Matthias Brigulla, Grit Kuhnke, Steven W Hardwick, Uwe Völker, Michael D Yudkin, Richard J Lewis
Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C.
J Biol Chem: 2004, 279(39);40927-37
[PubMed:15263010] [WorldCat.org] [DOI] (P p)Ing-Marie Jonsson, Staffan Arvidson, Simon Foster, Andrzej Tarkowski
Sigma factor B and RsbU are required for virulence in Staphylococcus aureus-induced arthritis and sepsis.
Infect Immun: 2004, 72(10);6106-11
[PubMed:15385515] [WorldCat.org] [DOI] (P p)Aurélie C Olivier, Sandrine Lemaire, Françoise Van Bambeke, Paul M Tulkens, Eric Oldfield
Role of rsbU and staphyloxanthin in phagocytosis and intracellular growth of Staphylococcus aureus in human macrophages and endothelial cells.
J Infect Dis: 2009, 200(9);1367-70
[PubMed:19817587] [WorldCat.org] [DOI] (I p)