Protein Family Models

This domain is found N-terminal in Carboxy-terminal processing protease CtpB and related proteins. This enzyme is involved in signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. This domain contains auto-cleavage site at which it is proteolytically cleaved. The remaining part in the mature enzyme is involved in dimerisation [1]. Paper describing PDB structure 4c2c. [1]. 24243021. CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis. Mastny M, Heuck A, Kurzbauer R, Heiduk A, Boisguerin P, Volkmer R, Ehrmann M, Rodrigues CD, Rudner DZ, Clausen T;. Cell. 2013;155:647-658. (from Pfam)

Date:

2024-10-16

This entry represents the PDZ domain from a wide variety of proteins. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

The serine endopeptidases in this family include C-terminal processing proteases such as the periplasmic protease Prc from Escherichia coli, involved in processing penicillin-binding protein (PBP) 3, and carboxyl-terminal processing protease CtpA from Pseudomonas aeruginosa.

Date:

2024-08-14

This domain is composed of three alpha helices [1]. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation [2]. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins [3]. The domain is found to bind peptidoglycan experimentally [4]. This paper gives the crystal structure for this domain. However no function is given for this domain. [1]. 7121588. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution. Dideberg O, Charlier P, Dive G, Joris B, Frere JM, Ghuysen JM;. Nature 1982;299:469-470. [2]. 1683402. Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2. Foster SJ;. J Gen Microbiol 1991;137:1987-1998. [3]. 7656014. The NMR structure of the inhibited catalytic domain of human stromelysin-1. Gooley PR, O'Connell JF, Marcy AI, Cuca GC, Salowe SP, Bush BL, Hermes JD, Esser CK, Hagmann WK, Springer JP, et al;. Nat Struct Biol 1994;1:111-118. [4]. 17697255. Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages phiKZ and EL. Briers Y, Volckaert G, Cornelissen A, Lagaert S, Michiels CW, Hertveldt K, Lavigne R;. Mol Microbiol. 2007;65:1334-1344. (from Pfam)

Date:

2024-10-16

PDZ domains are found in diverse signaling proteins. Review article. [1]. 9204764. PDZ domains: targeting signalling molecules to sub-membranous sites. Ponting CP, Phillips C, Davies KE, Blake DJ. Bioessays 1997;19:469-479. [2]. 8674113. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R;. Cell. 1996;85:1067-1076. Extension of PDZ family. [3]. 9041651. Evidence for PDZ domains in bacteria, yeast, and plants. Ponting CP;. Protein Sci 1997;6:464-468. [4]. 19738200. Rapid evolution of functional complexity in a domain family. Ernst A, Sazinsky SL, Hui S, Currell B, Dharsee M, Seshagiri S, Bader GD, Sidhu SS;. Sci Signal. 2009;2:ra50. (from Pfam)

Date:

2024-10-16

peptidase family S41 such as C-terminal processing protease (CTPase or CtpA) that contains the PDZ domain; active site consists of a serine/lysine catalytic dyad

Date:

2021-02-02

Carboxy-terminal processing proteases (EC 3.4.21.102) have paralogs in some species, and different gene symbols in different lineages, such as prc in Escherichia coli K-12, ctpA, ctpB, and ctpC in Synechocystis sp. PCC 6803, and cptA and ctpB in Bacillus subtilis.

Date:

2023-10-20