Protein Family Models

This domain is found at the C-terminal end of Nucleoid occlusion factor SlmA from Escherichia coli and similar transcriptional repressors from proteobacteria. SlmA is required for the nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. It is organised into two domains, a small N-terminal Pfam:PF00440 and a C-terminal domain (this entry). This domain shows an all-alpha configuration. This region mediates dimerisation [1]. Paper describing PDB structure 3nxc. [1]. 21113127. Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. Tonthat NK, Arold ST, Pickering BF, Van Dyke MW, Liang S, Lu Y, Beuria TK, Margolin W, Schumacher MA;. EMBO J. 2011;30:154-164. Paper describing PDB structure 3vuq. [2]. 23408580. Structure and function of a TetR family transcriptional regulator, SbtR, from thermus thermophilus HB8. Agari Y, Sakamoto K, Yutani K, Kuramitsu S, Shinkai A;. Proteins. 2013;81:1166-1178. Paper describing PDB structure 4gck. [3]. 23754405. SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid. Tonthat NK, Milam SL, Chinnam N, Whitfill T, Margolin W, Schumacher MA;. Proc Natl Acad Sci U S A. 2013;110:10586-10591. Paper describing PDB structure 5haw. [4]. 27091999. Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ. Schumacher MA, Zeng W;. Proc Natl Acad Sci U S A. 2016;113:4988-4993. (from Pfam)

Date:

2024-10-16

TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity [1]. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. This entry represents the C-terminal domain found in a number of different TetR transcription regulator proteins including SlmA proteins found in E. coli. Unlike other TetR proteins, SlmA functions not as a transcription regulator but rather as an NO (nucleoid occlusion) factor [2]. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis [3]. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain [3]. [1]. 15944459. The TetR family of transcriptional repressors. Ramos JL, Martinez-Bueno M, Molina-Henares AJ, Teran W, Watanabe . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

nucleoid occlusion protein SlmA helps mediate nucleoid occlusion, which prevents chromosome fragmentation by binding FtsZ and inhibiting Z-ring formation over the nucleoid

Date:

2023-02-28

FtsZ binding protein; this protein is the first identified nucleoid occlusion factor which works along with the Min system to properly position the FtsZ ring assembly

Gene:

slmA

Date:

2021-08-31