9.A.31.1.1 The putative peptide antibiotic-like killing factor (SdpC) exporter, SdpAB. However, Pérez Morales et al. 2013 concluded that SdpAB are not required for secretion, translation, or stability of SdpC, and that they may participate in a posttranslation step in the production
of SDP. The mature form of the SDP toxin contains a disulfide bond. Their data indicate that while the disulfide bond does increase activity of
SDP, it is not essential for SDP activity, and that the
disulfide bond is formed independently of SdpAB. Thus, SDP production is a multistep process in which SdpAB
are required for SDP production, likely by controlling, directly or
indirectly, cleavage of SDP from the pro-SdpC precursor (Pérez Morales et al. 2013).
|
Accession Number: | O34889 |
Protein Name: | YvaW |
Length: | 158 |
Molecular Weight: | 18651.00 |
Species: | Bacillus subtilis [1423] |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
Substrate |
|
---|
RefSeq: |
NP_391255.1
|
Entrez Gene ID: |
938629
|
BioCyc: |
SUBTI:BSU33750-MONOMER
|
KEGG: |
bsu:BSU33750
|
[1] “The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.” Kunst F. et.al. 9384377
[2] “Cannibalism by sporulating bacteria.” Gonzalez-Pastor J.E. et.al. 12817086
[3] “Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.” Strauch M.A. et.al. 17720793
|
1: MTICFLLFSS YYFSNISPQN PLFKKNFLQQ LSPQGFGFYS KSPTEENISF HTKENLKLPN
61: ALPNNFFGIK REGRVQAIEL GKIVENIDPK NWKTCENNNS CTNLEKQIKP IKVIKNEDYI
121: HLSKGEYLIY RQKPLSWYWI DFKQTTSFER KVLKIKIV