TABLE 2.
Characteristics of DtxR-like repressors
| Organism | Protein (aa) | % Identity (% similarity)a | C-terminal SH3 domain | Metalb | Amino acid residues in primary metal binding sitec |
|---|---|---|---|---|---|
| C. diphtheriae | MntR (223) | Yes | Mn | D12E105E108H109 | |
| DtxR (226) | 27 (41) | Yes | Fe | M10C102E105H106 | |
| M. tuberculosis | IdeR (230) | 32 (46) | Yes | Fe | M..C.EH |
| S. aureus | MntR (214) | 33 (52) | Yes | Mn | D..E.EH |
| B. subtilis | MntR (142) | 23 (39) | No | Mn | D..E.EH |
| T. pallidum | TroR (153) | 39 (58) | No | Mn | N..E.EH |
a
Compared to MntR of C. diphtheriae.
b
Divalent metals known to activate repressor activity in vivo.
c
Data from reference 6. Residue positions are given for C. diphtheriae MntR and DtxR. Residues for other proteins are at the location corresponding to that found in DtxR.