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Category: Proteolysis
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Category: Proteolysis

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3. Information processing

3.3. Protein synthesis, modification and degradation

3.3.7. Proteolysis

3.3.7.1. Protein quality control

NameFunction
htrAprotein quality control
htrBprotein quality control
htrCunknown
wprAprotein quality control

3.3.7.2. Extracellular feeding proteases

NameFunction
aprEprotein degradation
bprprotein degradation
eprprotein degradation
mprprotein degradation
nprBprotection of B. subtilis biofilms against competitors
nprEdegradation of proteins
vprprotein degradation

additional information

  • A mutant strain with deletions of all feeding proteases and the three major protein quality control proteases ([[gene|76FA52D5A5F9FCA14BA9B45872FE3D99D89B211B]], [[gene|796216BE9CD6DADFEADC29497253C81BF496A2ED]], [[gene|DC0FDCA3FA6742B023E6877CE9554AA1D47012BB]]) (BRB14) is available in [SW|Colin Harwood]'s lab [PubMed|24115457]

    • 3.3.7.3. Proteolysis during sporulation/ germination

    NameFunction
    gprdegradation of SASPs
    spoIIGAmaturation of [protein|3CB24D493B3282278B7DC61CE3C793DFA815F9E2|SigE]
    spoIVFBprocessing of pro-sigma-K to active [protein|24F7FD5C7C3A68BB2760ABB8CBD8FBD65E5FF7D4|SigK]
    tepAdegradation of SASPs
    ylzJcontrol of TepA activity

    3.3.7.4. Additional proteins involved in proteolysis

    NameFunction
    clpCprotein degradation, positive regulator of autolysin ([protein|6A21293823151C6980BF52B31A4B249A8440F2E1|LytC] and [protein|29219315D31BA4ADE41687EFF17FE41D6C23D157|LytD]) synthesis
    clpEprotein degradation
    clpPprotein degradation
    clpQprotein degradation
    clpXprotein degradation
    clpYprotein degradation
    ctpAunknown
    ctpBcontrol of [protein|24F7FD5C7C3A68BB2760ABB8CBD8FBD65E5FF7D4|SigK] activation
    ctsRregulation of protein degradation
    ddcPdegradation of [protein|7BF591DCDC9635C605D76135481A8A9DB63EE861|YneA]
    ftsHcell division, sporulation initiation
    htpXquality control of membrane proteins
    immAcontrol of [protein|DD1C8F3A4809785BD6A6047D39B42AB2C605E161|ImmR] activity
    ipicontrol of intracellular proteolysis
    ispAprotein degradation
    lonAprotein quality control, control of swarming motility
    lonBprotein quality control
    mecAcontrol of [protein|search|ComK ]degradation, regulation of competence
    mlpAcontrol of proteolyticc activity
    prpmaturation of [protein|4626C659D6F1A81CCC94030F1CBAF7FEC3DE19CA|ribosomal protein L27]
    prsWcontrol of [SW|SigW] activity
    rasPcontrol of [SW|cell division], and [protein|D04629D798E458AD538809BB2B150B7FA81D2C7E|SigV] and [protein|3D974DD2967C7F8FD4E3C2AF42617B8AE9F0296D|SigW] activity
    yabGmodification of spore coat proteins
    yirBcontrol of [protein|2C6386E9A63F410558D168798D077DF91590F454|Spx] proteolysis
    yjbHstimulation of [protein|2C6386E9A63F410558D168798D077DF91590F454|Spx] degradation
    ypbHunknown
    ypwAunknown
    yqgPcell division
    yraAdetoxification of methylglyoxal
    yydHcontrol of [protein|49E70A20CC05DBE485953C0AE34E634EFB33C3B2|LiaR]-[protein|9A1871BD853254EEA8B4E78CA187F9315CBDF43D|LiaS] activity

    important reviews

  • 19421188,23375660,23479438,22688815,24099006,24115457