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⊟Summary[edit | edit source]

  • pan ID?: SAUPAN005333000
  • symbol?: sigB
  • synonym:
  • description?: RNA polymerase sigma factor SigB

      descriptions from strain specific annotations:

    • RNA polymerase sigma factor SigB
    • sigma factor B
    • RNA polymerase sigma-B factor
    • RNA polymerase sigma factor B
  • strand?: -
  • coordinates?: 5511996..5512767
  • synteny block?: BlockID0041300
  • occurrence?: in 100% of 34 strains

sigB (rpoF) : RNA polymerase sigma factor SigB [1]

• A crystal structure is available : 8X6G

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]

    COL:
    SACOL2054 (rpoF)
    N315:
    SA1869 (sigB)
    NCTC8325:
    SAOUHSC_02298
    Newman:
    NWMN_1970 (sigB)
    USA300_FPR3757:
    SAUSA300_2022 (rpoF)
    04-02981:
    SA2981_2005 (sigB)
    08BA02176:
    C248_2075 (sigB)
    11819-97:
    MS7_2081 (sigB)
    6850:
    RSAU_001904 (sigB)
    71193:
    ST398NM01_2105
    ECT-R 2:
    ECTR2_1920 (sigB)
    ED133:
    SAOV_2106c (sigB)
    ED98:
    SAAV_2117 (rpoF)
    HO 5096 0412:
    SAEMRSA15_19740 (sigB)
    JH1:
    SaurJH1_2138
    JH9:
    SaurJH9_2101
    JKD6008:
    SAA6008_02103 (sigB)
    JKD6159:
    SAA6159_01979 (sigB)
    JSNZ:
    JSNZ_002025 (sigB)
    LGA251:
    SARLGA251_18670 (sigB)
    M013:
    M013TW_2023
    MRSA252:
    SAR2152 (sigB)
    MSHR1132:
    SAMSHR1132_18890
    MSSA476:
    SAS1969
    Mu3:
    SAHV_2049 (sigB)
    Mu50:
    SAV2064 (sigB)
    MW2:
    MW1988 (sigB)
    RF122:
    SAB1949c (sigB)
    ST398:
    SAPIG2105 (sigB)
    T0131:
    SAT0131_02221 (mnhB)
    TCH60:
    HMPREF0772_11131 (sigB)
    TW20:
    SATW20_22040 (sigB)
    USA300_TCH1516:
    USA300HOU_2059 (fliA)
    VC40:
    SAVC_09200

⊟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             MAKESKSANEISPEQINQWIKEHQENKNTDAQDKLVKHYQKLIESLAYKYSKGQSHHEDL
    N315            MAKESKSANEVSPEQINQWIKEHQENKNTDAQDKLVKHYQKLIESLAYKYSKGQSHHEDL
    NCTC8325        MAKESKSANEISPEQINQWIKEHQENKNTDAQDKLVKHYQKLIESLAYKYSKGQSHHEDL
    Newman          MAKESKSANEISPEQINQWIKEHQENKNTDAQDKLVKHYQKLIESLAYKYSKGQSHHEDL
    USA300_FPR3757  MAKESKSANEISPEQINQWIKEHQENKNTDAQDKLVKHYQKLIESLAYKYSKGQSHHEDL
                    **********:*************************************************

    COL             VQVGMVGLIGAINRFDMSFERKFEAFLVPTVIGEIKRYLRDKTWSVHVPRRIKEIGPRIK
    N315            VQVGMVGLIGAINRFDMSFERKFEAFLVPTVIGEIKRYLRDKTWSVHVPRRIKEIGPRIK
    NCTC8325        VQVGMVGLIGAINRFDMSFERKFEAFLVPTVIGEIKRYLRDKTWSVHVPRRIKEIGPRIK
    Newman          VQVGMVGLIGAINRFDMSFERKFEAFLVPTVIGEIKRYLRDKTWSVHVPRRIKEIGPRIK
    USA300_FPR3757  VQVGMVGLIGAINRFDMSFERKFEAFLVPTVIGEIKRYLRDKTWSVHVPRRIKEIGPRIK
                    ************************************************************

    COL             KVSDELTAELERSPSISEIADRLEVSEEEVLEAMEMGQSYNALSVDHSIEADKDGSTVTL
    N315            KVSDELTAELERSPSISEIANRLEVSEEEVLEAMEMGQSYNALSVDHSIEADKDGSTVTL
    NCTC8325        KVSDELTAELERSPSISEIADRLEVSEEEVLEAMEMGQSYNALSVDHSIEADKDGSTVTL
    Newman          KVSDELTAELERSPSISEIADRLEVSEEEVLEAMEMGQSYNALSVDHSIEADKDGSTVTL
    USA300_FPR3757  KVSDELTAELERSPSISEIADRLEVSEEEVLEAMEMGQSYNALSVDHSIEADKDGSTVTL
                    ********************:***************************************

    COL             LDIMGQQDDHYDLTEKRMILEKILPILSDREREIIQCTFIEGLSQKETGERIGLSQMHVS
    N315            LDIMGQQDDHYDLTEKRMILEKILPILSDREREIIQCTFIEGLSQKETGERIGLSQMHVS
    NCTC8325        LDIMGQQDDHYDLTEKRMILEKILPILSDREREIIQCTFIEGLSQKETGERIGLSQMHVS
    Newman          LDIMGQQDDHYDLTEKRMILEKILPILSDREREIIQCTFIEGLSQKETGERIGLSQMHVS
    USA300_FPR3757  LDIMGQQDDHYDLTEKRMILEKILPILSDREREIIQCTFIEGLSQKETGERIGLSQMHVS
                    ************************************************************

    COL             RLQRTAIKKLQEAAHQ
    N315            RLQRTAIKKLQEAAHK
    NCTC8325        RLQRTAIKKLQEAAHQ
    Newman          RLQRTAIKKLQEAAHQ
    USA300_FPR3757  RLQRTAIKKLQEAAHQ
                    ***************:

  1. ↑ 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)    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)
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