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9.B.1.1.4
Ste24 endopeptidase, CAAX PP of 407 aas and 7 TMSs.  The crystal structure has been solved showing that the Ste24p core structure is a ring of seven TMSs enclosing a voluminous cavity containing the active site and substrate-binding groove. The cavity is large enough to hold hundreds of water molecules, and is accessible to the external milieu by means of gaps between splayed transmembrane helices (Sanders and Hutchison 2018). Possibly cleavage proceeds by means of a processive mechanism of substrate insertion, translocation, and ejection (Pryor et al. 2013). The active site is just under the interfacial lid of the barrel, with substrate entry and product exit through fenestrations located near the upper end of the barrel, just under the water-bilayer interface (Sanders and Hutchison 2018).

Accession Number:J0MMU8
Protein Name:Ste24 endopeptidase
Length:407
Molecular Weight:46329.00
Species:Helicobacter pylori Hp A-16 [992055]
Number of TMSs:7
Substrate Unknown

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FASTA formatted sequence
1:	MLDIWIDMII CIFYLLFFTT PYIVGDILQL KFIRQKLCEK PVLLPQKDYE EAGHYAIRKM 
61:	QLSIISQILD GIIFAGWVFF GLTHLEDLTH YLNLPETLGY LVFALLFLAI QSVLALPISY 
121:	YTTMHLDKEF GFSKVSLSLF FKDFFKGLSL TLGVGLLLIY TLIMIIEHVE HWEISSFFVV 
181:	FVFMILANLF YPKIAQLFNQ FTPLNNRDLE SQIESMMDKV GFKSEGIFVM DASKRDGRLN 
241:	AYFGGLGKNK RVVLFDTLIS KVGTEGLLAI LGHELGHFKN KDLLKSLGIM GGLLALVFAL 
301:	IAHLPPLVFE GFNVSQTPAS LIAILLLFLP VFSFYAMPLI GFFSRKNEYN ADKFGASLSS 
361:	KETLAKALVS IVNENKAFPY SHPFYVFLHF THPPLLERLK ALDYEIE