Protein Family Models

This family includes metalloproteases such as TdlD from E. coli K-12, with a characteristic HEXXXH motif, and also homologs such as PmbA (also called TldE) in which the metal-binding and active site motif HEXXXH is replaced. This HMM, which describes the C-terminal half of proteins such as TldD and PmbA, covers the HEXXXH region in its most N-terminal 25 positions of the model.

Date:

2024-10-16

This entry represents a group of metalloproteases. The tertiary structure of the Escherichia coli TdlD/TdlE complex has been solved, and shows that the TdlD subunit is the active peptidase, binding a single zinc ion at an HEXXXH motif in which the glutamic acid is a substrate-binding residue and the two histidines are zinc ligands. The third zinc ligand is a cysteine, C-terminal to the HEXXXH motif. The TldE (also known as PmbA) by itself has no catalytic activity, does not bind zinc, and does not carry the HEXXXH motif [1]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [2-3]. [1]. 28943336. The Origins of Specificity in the Microcin-Processing Protease TldD/E. Ghilarov D, Serebryakova M, Stevenson CEM, Hearnshaw SJ, Volkov DS, Maxwell A, Lawson DM, Severinov K;. Structure. 2017;25:1549-1561. [2]. 22950735. An archaeal protein evolutionarily conserved in prokaryotes is a zinc-dependent metalloprotease. Hu Y, Peng N, Han W, Mei Y, Chen Z, Feng X, Liang YX, She Q;. Biosci Rep. 2012;32:609-618. [3]. 12029038. The highly conserved TldD and TldE proteins of Escherichia coli are involved in microcin B17 processing and in CcdA degradation. Allali N, Afif H, Couturier M, Van Melderen L;. J Bacteriol. 2002;184:3224-3231. (from Pfam)

Date:

2024-10-16

This entry represents a group of metalloproteases. The tertiary structure of the Escherichia coli TdlD/TdlE complex has been solved, and shows that the TdlD subunit is the active peptidase, binding a single zinc ion at an HEXXXH motif in which the glutamic acid is a substrate-binding residue and the two histidines are zinc ligands. The third zinc ligand is a cysteine, C-terminal to the HEXXXH motif. The TldE (also known as PmbA) by itself has no catalytic activity, does not bind zinc, and does not carry the HEXXXH motif [1]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [2-3]. [1]. 28943336. The Origins of Specificity in the Microcin-Processing Protease TldD/E. Ghilarov D, Serebryakova M, Stevenson CEM, Hearnshaw SJ, Volkov DS, Maxwell A, Lawson DM, Severinov K;. Structure. 2017;25:1549-1561. [2]. 22950735. An archaeal protein evolutionarily conserved in prokaryotes is a zinc-dependent metalloprotease. Hu Y, Peng N, Han W, Mei Y, Chen Z, Feng X, Liang YX, She Q;. Biosci Rep. 2012;32:609-618. [3]. 12029038. The highly conserved TldD and TldE proteins of Escherichia coli are involved in microcin B17 processing and in CcdA degradation. Allali N, Afif H, Couturier M, Van Melderen L;. J Bacteriol. 2002;184:3224-3231. (from Pfam)

Date:

2024-10-16

metalloprotease PmbA is involved in CcdA degradation, suppressing the inhibitory activity of the carbon storage regulator (CsrA), proteolytic processing of the antibiotic microcin B17, and in sensitivity to the DNA gyrase inhibitor LetD

Date:

2015-11-06

Protease involved in proteolytic processing of the antibiotic Microcin B17

Gene:

pmbA

Date:

2021-07-30