9.B.174.1.1 The C-terminal processing protease, CtpB (YvjB). Crystal structures reflecting distinct functional states show that CtpB constitutes a ring-like protein scaffold penetrated by two narrow
tunnels. Access to the proteolytic sites sequestered within these
tunnels is controlled by PDZ domains that rearrange upon substrate
binding. Accordingly, CtpB resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism (Mastny et al. 2013). May show limited sequence similarity with 8.A.24.1.1. The transmembrane domain serves as a receptor for the LsbB bacteriocin in Lactococcus lactis (Miljkovic et al. 2016).
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Accession Number: | O35002 |
Protein Name: | Carboxy-terminal processing protease CtpB |
Length: | 480 |
Molecular Weight: | 52798.00 |
Species: | Bacillus subtilis (strain 168) [224308] |
Number of TMSs: | 1 |
Location1 / Topology2 / Orientation3: |
Forespore intermembrane space1 |
Substrate |
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1: MNQKIMAVIA AGSMLFGGAG VYAGINLLEM DKPQTAAVPA TAQADSERDK AMDKIEKAYE
61: LISNEYVEKV DREKLLEGAI QGMLSTLNDP YSVYMDKQTA KQFSDSLDSS FEGIGAEVGM
121: EDGKIIIVSP FKKSPAEKAG LKPNDEIISI NGESMAGKDL NHAVLKIRGK KGSSVSMKIQ
181: RPGTKKQLSF RIKRAEIPLE TVFASEKKVQ GHSVGYIAIS TFSEHTAEDF AKALRELEKK
241: EIEGLVIDVR GNPGGYLQSV EEILKHFVTK DQPYIQIAER NGDKKRYFST LTHKKAYPVN
301: VITDKGSASA SEILAGALKE AGHYDVVGDT SFGKGTVQQA VPMGDGSNIK LTLYKWLTPN
361: GNWIHKKGIE PTIAIKQPDY FSAGPLQLKE PLKVDMNNED VKHAQVLLKG LSFDPGREDG
421: YFSKDMKKAV MAFQDQNKLN KTGVIDTRTA ETLNQQIEKK KSDEKNDLQL QTALKSLFVN