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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).

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

Cross database links:

Structure:
4C2C   4C2D   4C2E   4C2F   4C2G   4C2H     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
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