Tetracyclin repressor-like, C-terminal domain; 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 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. 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. This entry represents the C-terminal domain present in the Pseudomonas aeruginosa PsrA which regulates the fadBA5 beta-oxidation operon. Functional analysis of PsrA indicated its importance in regulating b-oxidative enzymes. It has also been suggested that PsrA, a member of the TetR family of repressors, could affect global gene expression including activation of rpoS.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916367207  106 YVLPAFISSYGEAGGGARFTRMRAVLSAEGNPEAREIIAQAFDTTTCAFIDAIEGCLPGADRTAIVWRSQFLLGSLYYTL 185
Cdd:pfam17939   1 FVRPLLELSQTGGEGGRAFARLLARLYSEPDEELRELIAEEYDPVARRFIAALRRALPDLPREELFWRLHFMLGALLFTL 80

                          90       100
                  ....*....|....*....|....*...
gi 916367207  186 INPERITRLSDGATDGGDHERAIEELVA 213
Cdd:pfam17939  81 ADTGRLDILSGGLCSSADLEALIERLVP 108

Tetracyclin repressor-like, C-terminal domain; 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 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. 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. This entry represents the C-terminal domain present in the Pseudomonas aeruginosa PsrA which regulates the fadBA5 beta-oxidation operon. Functional analysis of PsrA indicated its importance in regulating b-oxidative enzymes. It has also been suggested that PsrA, a member of the TetR family of repressors, could affect global gene expression including activation of rpoS.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916367207  106 YVLPAFISSYGEAGGGARFTRMRAVLSAEGNPEAREIIAQAFDTTTCAFIDAIEGCLPGADRTAIVWRSQFLLGSLYYTL 185
Cdd:pfam17939   1 FVRPLLELSQTGGEGGRAFARLLARLYSEPDEELRELIAEEYDPVARRFIAALRRALPDLPREELFWRLHFMLGALLFTL 80

                          90       100
                  ....*....|....*....|....*...
gi 916367207  186 INPERITRLSDGATDGGDHERAIEELVA 213
Cdd:pfam17939  81 ADTGRLDILSGGLCSSADLEALIERLVP 108

Bacterial regulatory proteins, tetR family;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 916367207   24 ILEIAEHLFAERGFGSVPLREIARAAGVHVGSVTYHFGDKLGLLEAI 70
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47

ScbR family autoregulator-binding transcription factor;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 916367207  20 TRQSILEIAEHLFAERGFGSVPLREIARAAGVHVGSVTYHFGDKLGLLEAI 70
Cdd:NF041196   7 TRRAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAV 57

Tetracyclin repressor-like, C-terminal domain; 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 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. 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. This entry represents the C-terminal domain present in the Pseudomonas aeruginosa PsrA which regulates the fadBA5 beta-oxidation operon. Functional analysis of PsrA indicated its importance in regulating b-oxidative enzymes. It has also been suggested that PsrA, a member of the TetR family of repressors, could affect global gene expression including activation of rpoS.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916367207  106 YVLPAFISSYGEAGGGARFTRMRAVLSAEGNPEAREIIAQAFDTTTCAFIDAIEGCLPGADRTAIVWRSQFLLGSLYYTL 185
Cdd:pfam17939   1 FVRPLLELSQTGGEGGRAFARLLARLYSEPDEELRELIAEEYDPVARRFIAALRRALPDLPREELFWRLHFMLGALLFTL 80

                          90       100
                  ....*....|....*....|....*...
gi 916367207  186 INPERITRLSDGATDGGDHERAIEELVA 213
Cdd:pfam17939  81 ADTGRLDILSGGLCSSADLEALIERLVP 108

Bacterial regulatory proteins, tetR family;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 916367207   24 ILEIAEHLFAERGFGSVPLREIARAAGVHVGSVTYHFGDKLGLLEAI 70
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47

DNA-binding transcriptional repressor AcrR; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 916367207  19 DTRQSILEIAEHLFAERGFGSVPLREIARAAGVHVGSVTYHFGDKLGLLEAIYTT 73
Cdd:PRK10668  11 ETRQHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLFSEIWEL 65

HTH-type transcriptional repressor FabR;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 916367207  20 TRQSILEIA-EHLFAERGFGSVPLREIARAAGVHVGSVTYHFGD--KLGL 66
Cdd:PRK11202  12 TRRALIDAAfSQLSAERSFSSLSLREVAREAGIAPTSFYRHFRDmdELGL 61

putative DNA-binding transcriptional regulator; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 916367207  21 RQSILEIAEHLFAERGFGSVPlREIARAAGVHVGSVTYHFGDKLGLLEAI 70
Cdd:PRK11552  15 KQQLIAAALAQFGEYGLHATT-RDIAAQAGQNIAAITYYFGSKEDLYLAV 63

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 916367207   18 ADTRQSILEIAEHLFAERGFGSVPLREIARAAGVHVGSVTYHFGDKLGLLEAI 70
Cdd:pfam13419  10 LDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKI 62