{PDOC51494}
{PS51494; SPOIVB}
{BEGIN}
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* SpoIVB peptidase domain profile *
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The protein  SpoIVB  is  a  serine  peptidase  that  plays a central role in a
regulatory checkpoint   (the   sigma-K   checkpoint)  which  coordinates  gene
expression during  the  later  stages of spore formation in Bacillus subtilis.
SpoIVB signal  by transiting a membrane, undergoing self cleavage, and then by
an unknown mechanism activating a zinc metalloprotease, SpoIVFB, which cleaves
pro-sigma-K to  its  active form, sigma-K, in the outer mother cell chamber of
the developing  cell  [E1]. Homologues of SpoIVB proteins have been identified
in a  number  of  spore-forming  organisms. SpoIVB carries a single PDZ domain
(see <PDOC50106>)  and  a  160-amino-acid  residue  catalytic serine peptidase
domain at the carboxyl terminus of the protein. His, Asp and Ser residues form
the catalytic  triad  of  the SpoIVB serine peptidase domain [1,2]. The SpoIVB
peptidase domain forms peptidase family S55 of clan PA(S) [2] [E1].

For SpoIVB  to  cleave  another  SpoIVB  molecule  in  trans  it must target a
specific region  at  the  COOH  terminus  of the SpoIVB peptidase domain. This
region carries  a Thr-His-Val motif identical to the classical PDZ recognition
motif ([ST]-X-V) normally found at the extreme COOH terminus of PDZ-recognized
proteins [2].

The profile we developed covers the entire SpoIVB peptidase domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: May 2011 / Text revised.

[ 1] Hoa N.T., Brannigan J.A., Cutting S.M.
     "The Bacillus subtilis signaling protein SpoIVB defines a new family
     of serine peptidases."
     J. Bacteriol. 184:191-199(2002).
     PubMed=11741860
[ 2] Dong T.C., Cutting S.M.
     "The PDZ domain of the SpoIVB transmembrane signaling protein enables
     cis-trans interactions involving multiple partners leading to the
     activation of the pro-sigmaK processing complex in Bacillus
     subtilis."
     J. Biol. Chem. 279:43468-43478(2004).
     PubMed=15292188; DOI=10.1074/jbc.M407048200
[E1] https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=s55

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