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⊟Summary[edit | edit source]
- pan ID?: SAUPAN005335000
- symbol?: rsbV
- synonym:
- description?: anti-sigma B factor antagonist
- anti-sigma B factor antagonist
- anti-sigma factor antagonist
- anti-anti-sigma factor RsbV
- anti-sigma-B factor, antagonist
- anti-sigma B factor antagonist RsbV
- STAS domain-containing protein
- anti-sigma-B factor antagonist (Anti-anti-sigma-B factor)
- anti-sigma F factor antagonist
- anti-sigma F factor antagonist (spoIIAA-2)
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5513223..5513549
- synteny block?: BlockID0041320
- occurrence?: in 100% of 34 strains
rsbV : anti-sigma-B factor antagonist [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_2007 (rsbV)
08BA02176:
C248_2077 (rsbV)
11819-97:
MS7_2083 (rsbV)
6850:
RSAU_001906 (rsbV)
71193:
ST398NM01_2107
ECT-R 2:
ECTR2_1922
ED133:
SAOV_2108c (rsbV)
ED98:
SAAV_2119 (rsbV)
HO 5096 0412:
SAEMRSA15_19760 (rsbV)
JH1:
SaurJH1_2140
JH9:
SaurJH9_2103
JKD6008:
SAA6008_02105 (rsbV)
JKD6159:
SAA6159_01981 (rsbV)
JSNZ:
JSNZ_002027
LGA251:
SARLGA251_18690 (rsbV)
M013:
M013TW_2025
MRSA252:
SAR2154 (rsbV)
MSHR1132:
SAMSHR1132_18910
MSSA476:
SAS1971
Mu3:
SAHV_2051 (rsbV)
Mu50:
SAV2066 (rsbV)
MW2:
MW1990 (rsbV)
RF122:
SAB1951c (rsbV)
ST398:
SAPIG2107
T0131:
SAT0131_02223
TCH60:
HMPREF0772_11129 (rsbV)
TW20:
SATW20_22060 (rsbV)
USA300_TCH1516:
USA300HOU_2061 (rsbV)
VC40:
SAVC_09210
⊟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 MNLNIETTTQDKFYEVKVGGELDVYTVPELEEVLTPMRQDGTRDIYVNLENVSYMDSTGL
N315 MNLNIETTTQDKFYEVKVGGELDVYTVPELEEVLTPMRQDGTRDIYVNLENVSYMDSTGL
NCTC8325 MNLNIETTTQDKFYEVKVGGELDVYTVPELEEVLTPMRQDGTRDIYVNLENVSYMDSTGL
Newman MNLNIETTTQDKFYEVKVGGELDVYTVPELEEVLTPMRQDGTRDIYVNLENVSYMDSTGL
USA300_FPR3757 MNLNIETTTQDKFYEVKVGGELDVYTVPELEEVLTPMRQDGTRDIYVNLENVSYMDSTGL
************************************************************
COL GLFVGTLKALNQNDKELYILGVSDRIGRLFEITGLKDLMHVNEGTEVE
N315 GLFVGTLKALNQNDKELYILGVSDRIGRLFEITGLKDLMHVNEGTEVE
NCTC8325 GLFVGTLKALNQNDKELYILGVSDRIGRLFEITGLKDLMHVNEGTEVE
Newman GLFVGTLKALNQNDKELYILGVSDRIGRLFEITGLKDLMHVNEGTEVE
USA300_FPR3757 GLFVGTLKALNQNDKELYILGVSDRIGRLFEITGLKDLMHVNEGTEVE
************************************************
- ↑ Syeda Durr-E-Shahwar, Atia-Tul-Wahab, M Iqbal Choudhary, Almas Jabeen
Cloning, purification, structural, and functional characterization of methicillin-resistant Staphylococcus aureus (MRSA252) RsbV protein.
Int J Biol Macromol: 2019, 134;962-966
[PubMed:31075336] [WorldCat.org] [DOI] (I p)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)