1.C.12.1.13 Intermedilysin of 532 aas and 1 N-terminal TMS, ILY or Ply. It binds to membranes containing the human protein CD59 but forms pores only if the
membrane contains sufficient cholesterol (Heuck et al. 2007). CD59 is required for the specific coordination of intermedilysin (ILY) monomers and for
triggering collapse of an oligomeric prepore. Movement of Domain 2 with respect to Domain 3 of ILY
is essential for forming a late prepore intermediate that releases CD59, while the role of
cholesterol may be limited to insertion of the TMSs (Boyd et al. 2016). The pore-forming regions are initially folded up on the surfaces of the
soluble precursors. To create the transmembrane pores, these regions
must extend and refold into membrane-inserted beta-barrels (Tilley and Saibil 2006). The intermedilysin cytolytic activity depends on heparan sulfates and the membrane composition (Drabavicius and Daelemans 2021).
|
Accession Number: | Q9LCB8 |
Protein Name: | Intermedilysin |
Length: | 532 |
Molecular Weight: | 58423.00 |
Species: | Streptococcus intermedius [1338] |
Number of TMSs: | 1 |
Substrate |
molecule |
---|
1: MKTKQNIARK LSRVVLLSTL VLSSAAPISA AFAETPTKPK AAQTEKKTEK KPENSNSEAA
61: KKALNDYIWG LQYDKLNILT HQGEKLKNHS SREAFHRPGE YVVIEKKKQS ISNATSKLSV
121: SSANDDRIFP GALLKADQSL LENLPTLIPV NRGKTTISVN LPGLKNGESN LTVENPSNST
181: VRTAVNNLVE KWIQNYSKTH AVPARMQYES ISAQSMSQLQ AKFGADFSKV GAPLNVDFSS
241: VHKGEKQVFI ANFRQVYYTA SVDSPNSPSA LFGSGITPTD LINRGVNSKT PPVYVSNVSY
301: GRAMYVKFET TSKSTKVQAA IDAVVKGAKL KAGTEYENIL KNTKITAVVL GGNPGEASKV
361: ITGNIDTLKD LIQKGSNFSA QSPAVPISYT TSFVKDNSIA TIQNNTDYIE TKVTSYKDGA
421: LTLNHDGAFV ARFYVYWEEL GHDADGYETI RSRSWSGNGY NRGAHYSTTL RFKGNVRNIR
481: VKVLGATGLA WEPWRLIYSK NDLPLVPQRN ISTWGTTLHP QFEDKVVKDN TD