Protein Domain : IPR011075

Type:  Domain Name:  Tetracycline transcriptional regulator, TetR-related, C-terminal
Description:  The antibiotic tetracycline has a broad spectrum of activity, acting to inhibit bacterial protein synthesis by binding to the 30S ribosomal subunit, which prevents the association of the aminoacyl-tRNA to the ribosomal acceptor A site. Tetracycline binding is reversible, therefore diluting out the antibiotic can reverse its effects. Tetracycline resistance genes are often located on mobile elements, such as plasmids, transposons and/or conjugative transposons, which can sometimes be transferred between bacterial species. In certain cases, tetracycline can enhance the transfer of these elements, thereby promoting resistance amongst a bacterial colony. There are three types of tetracycline resistance: tetracycline efflux, ribosomal protection, and tetracycline modification [, ]: Tetracycline efflux proteins belong to the major facilitator superfamily. Efflux proteins are membrane-associated proteins that recognise and export tetracycline from the cell. They are found in both Gram-positive and Gram-negative bacteria []. There are at least 22 different tetracycline efflux proteins, grouped according to sequence similarity: Group 1 are Tet(A), Tet(B), Tet(C), Tet(D), Tet(E), Tet(G), Tet(H), Tet(J), Tet(Z) and Tet(30); Group 2 are Tet(K) and Tet(L); Group 3 are Otr(B) and Tcr(3); Group 4 is TetA(P); Group 5 is Tet(V). In addition, there are the efflux proteins Tet(31), Tet(33), Tet(V), Tet(Y), Tet(34), and Tet(35).Ribosomal protection proteins are cytoplasmic proteins that display homology with the elongation factors EF-Tu and EF-G. Protection proteins bind the ribosome, causing an alteration in ribosomal conformation that prevents tetracycline from binding. There are at least ten ribosomal protection proteins: Tet(M), Tet(O), Tet(S), Tet(W), Tet(32), Tet(36), Tet(Q), Tet(T), Otr(A), and TetB(P). Both Tet(M) and Tet(O) have ribosome-dependent GTPase activity, the hydrolysis of GTP providing the energy for the ribosomal conformational changes. Tetracycline modification proteins include the enzymes Tet(37) and Tet(X), both of which inactivate tetracycline. In addition, there are the tetracycline resistance proteins Tet(U) and Otr(C).The expression of several of these tet genes is controlled by a family of tetracycline transcriptional regulators known as TetR. 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 []. The TetR proteins identified in over 115 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. 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 []. 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. Other members of the TetR family of transcriptional regulators carry this C-terminal domain. These include:QacR from Staphylococcus aureus, a multidrug binding protein that represses transcription of the qacA multidrug transporter gene []Ethr, a repressor from Mycobacterium tuberculosisimplicated in ethionamide drug resistance []CprB, a gamma-butyrolactone autoregulator/receptor from Streptomyces coelicolorthat acts as a DNA-binding protein []YcdC, a hypothetical transcriptional regulator from Escherichia coliYsiA, YfiR, and YxaF, hypothetical transcriptional regulators from Bacillus subtilisYbiH, a hypothetical transcriptional regulator from Salmonella typhimurium Short Name:  Tet_transcr_reg_TetR-rel_C

3 Child Features

DB identifier Type Name
IPR015292 Domain Transcription regulator YbiH, C-terminal
IPR013571 Domain Transcription regulator QacR, C-terminal
IPR013572 Domain Transcription regulator MAATS, C-terminal

0 Contains

1 Cross References

Identifier
SSF48498

1 Found In

DB identifier Type Name
IPR019915 Family Transcription regulator, pyrimidine utilisation, RutR

0 GO Annotation

0 Ontology Annotations

1 Parent Features

DB identifier Type Name
IPR015893 Domain Tetracycline transcriptional regulator, TetR-like, C-terminal

51 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
415948 D8RXL9 PAC:15401799 Selaginella moellendorffii 112  
64357 D8R754 PAC:15401935 Selaginella moellendorffii 265  
30367.m000020 B9TG54 PAC:16824381 Ricinus communis 382  
30288.m000025 B9TGI9 PAC:16824323 Ricinus communis 94  
30901.m000032 B9TIJ4 PAC:16824686 Ricinus communis 193  
31036.m000037 B9TGT0 PAC:16824767 Ricinus communis 199  
31795.m000031 B9TG38 PAC:16825191 Ricinus communis 188  
33704.m000034 B9TDJ3 PAC:16825963 Ricinus communis 94  
34270.m000027 B9TM14 PAC:16826160 Ricinus communis 209  
35811.m000039 B9TDR6 PAC:16826735 Ricinus communis 154  
36563.m000017 B9TPN4 PAC:16826942 Ricinus communis 153  
50659.m000017 B9TJR0 PAC:16828291 Ricinus communis 276  
28993.m000042 B9TBH4 PAC:16802120 Ricinus communis 208  
13957 I0Z4K8 PAC:27390212 Coccomyxa subellipsoidea C-169 286  
Cagra.2757s0001.1.p PAC:28901583 Capsella grandiflora 252  
Kalax.0020s0151.1.p PAC:32583669 Kalanchoe laxiflora 486  
Pp3s30_515V3.1.p PAC:32948514 Physcomitrium patens 192  
Pp3s32_450V3.2.p PAC:32948369 Physcomitrium patens 432  
Pp3s32_450V3.1.p PAC:32948368 Physcomitrium patens 432  
Pp3s30_170V3.1.p PAC:32948481 Physcomitrium patens 335  
Pp3s34_337V3.1.p PAC:32948255 Physcomitrium patens 224  
Pp3s70_170V3.1.p PAC:32963366 Physcomitrium patens 194  
Pp3s58_150V3.1.p PAC:32929807 Physcomitrium patens 586  
Pp3s96_70V3.1.p PAC:32966545 Physcomitrium patens 198  
Brdisv1pangenome1006944m.p PAC:33623590 Brachypodium distachyon Pangenome 355  
Brdisv1pangenome1007171m.p PAC:33657775 Brachypodium distachyon Pangenome 472  
Brdisv1pangenome1008811m.p PAC:33620473 Brachypodium distachyon Pangenome 531  
Brdisv1pangenome1011018m.p PAC:33641356 Brachypodium distachyon Pangenome 293  
Brdisv1BdTR11A1041986m.p PAC:35696908 Brachypodium distachyon BdTR11a 472  
Brdisv1BdTR11A1039951m.p PAC:35691994 Brachypodium distachyon BdTR11a 532  

8 Publications

First Author Title Year Journal Volume Pages PubMed ID
            7707374
            16887689
            15837373
            1423217
            15944459
            11739955
            15236969
            14757054