HMM Summary Page: TIGR00054

FunctionRIP metalloprotease RseP
Gene SymbolrseP
Trusted Cutoff147.55
Domain Trusted Cutoff147.55
Noise Cutoff70.00
Domain Noise Cutoff70.00
Isology Typeequivalog
EC Number3.4.24.-
HMM Length421
Mainrole CategoryProtein fate
Subrole CategoryDegradation of proteins, peptides, and glycopeptides
Gene Ontology TermGO:0004222: metalloendopeptidase activity molecular_function
GO:0006508: proteolysis biological_process
AuthorAnolik RT, Haft DH
Entry DateApr 20 1999 2:04PM
Last ModifiedFeb 14 2011 3:27PM
CommentMembers of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by an HMM built to force a match to the full length of the seed alignment. A model that detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain.
ReferencesSE TIGR AL clustalw DR PFAM; PF00595; PDZ; DR PROSITE; PDOC00129; Neutral zinc metallopeptidases, zinc-binding region signature RN [1] RM PMID: 15496982 RT RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences. RA Akiyama Y, Kanehara K, Ito K RL EMBO J. 2004 Nov 10;23(22):4434-42. RN [2] RM PMID: 15686556 RT A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant. RA Chen JC, Viollier PH, Shapiro L RL Mol Microbiol. 2005 Feb;55(4):1085-103.