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⊟Summary[edit | edit source]
- pan ID?: SAUPAN005334000
- symbol?: rsbW
- synonym:
- description?: anti-sigma B factor RsbW
- anti-sigma B factor RsbW
- serine-protein kinase RsbW
- anti-sigma-B factor serine-protein kinase RsbW
- anti-sigma B factor
- anti-sigma-B factor, serine-protein kinase
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5512742..5513221
- synteny block?: BlockID0041310
- occurrence?: in 100% of 34 strains
rsbW : anti-sigma-B factor and RsbV-specific serine-protein kinase [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_2006 (rsbW)
08BA02176:
C248_2076 (rsbW)
11819-97:
MS7_2082 (rsbW)
6850:
RSAU_001905 (rsbW)
71193:
ST398NM01_2106
ECT-R 2:
ECTR2_1921 (rsbW)
ED133:
SAOV_2107c (rsbW)
ED98:
SAAV_2118 (rsbW)
HO 5096 0412:
SAEMRSA15_19750 (rsbW)
JH1:
SaurJH1_2139
JH9:
SaurJH9_2102
JKD6008:
SAA6008_02104 (rsbW)
JKD6159:
SAA6159_01980 (rsbW)
JSNZ:
JSNZ_002026 (rsbW)
LGA251:
SARLGA251_18680 (rsbW)
M013:
M013TW_2024
MRSA252:
SAR2153 (rsbW)
MSHR1132:
SAMSHR1132_18900
MSSA476:
SAS1970
Mu3:
SAHV_2050 (rsbW)
Mu50:
SAV2065 (rsbW)
MW2:
MW1989 (rsbW)
RF122:
SAB1950c (rsbW)
ST398:
SAPIG2106 (rsbW)
T0131:
SAT0131_02222 (mnhA)
TCH60:
HMPREF0772_11130 (rsbW)
TW20:
SATW20_22050 (rsbW)
USA300_TCH1516:
USA300HOU_2060 (rsbW)
VC40:
SAVC_09205
⊟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 ----------MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEA
N315 ----------MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEA
NCTC8325 MLMKERRSNNMQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEA
Newman ----------MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEA
USA300_FPR3757 ----------MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEA
**************************************************
COL VTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDF
N315 VTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDF
NCTC8325 VTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDF
Newman VTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDF
USA300_FPR3757 VTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDF
************************************************************
COL LREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS
N315 LREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS
NCTC8325 LREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS
Newman LREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS
USA300_FPR3757 LREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS
*************************************************
- ↑ Debabrata Sinha, Rajkrishna Mondal, Avisek Mahapa, Keya Sau, Rajagopal Chattopadhyaya, Subrata Sau
A staphylococcal anti-sigma factor possesses a single-domain, carries different denaturant-sensitive regions and unfolds via two intermediates.
PLoS One: 2018, 13(4);e0195416
[PubMed:29621342] [WorldCat.org] [DOI] (I e)Debabrata Sinha, Tushar Chakraborty, Debasmita Sinha, Asim Poddar, Rajagopal Chattopadhyaya, Subrata Sau
Understanding the structure, stability, and anti-sigma factor-binding thermodynamics of an anti-anti-sigma factor from Staphylococcus aureus.
J Biomol Struct Dyn: 2021, 39(17);6539-6552
[PubMed:32755297] [WorldCat.org] [DOI] (I p)Debasmita Sinha, Debabrata Sinha, Nilanjan Banerjee, Priya Rai, Soham Seal, Tushar Chakraborty, Subhrangsu Chatterjee, Subrata Sau
A conserved arginine residue in a staphylococcal anti-sigma factor is required to preserve its kinase activity, structure, and stability.
J Biomol Struct Dyn: 2022, 40(11);4972-4986
[PubMed:33356973] [WorldCat.org] [DOI] (I p)