Transcription Factor

Accessions: 1qpi_A (3D-footprint 20231221)
Names: TETR4_ECOLX, TETRACYCLINE REPRESSOR
Organisms: Escherichia coli
Libraries: 3D-footprint 20231221 1
1 Contreras-Moreira B. 3D-footprint: a database for the structural analysis of protein-DNA complexes. Nucleic acids research 38:D91-7 (2010). [Pubmed]
Uniprot: P0ACT4
Length: 195
Pfam Domains: 7-52 Bacterial regulatory proteins, tetR family
65-190 Tetracyclin repressor, C-terminal all-alpha domain
Sequence:
(in bold interface residues)
1 LNRESVIDAALELLNETGIDGLTTRKLAQKLGIEQPTLYWHVKNKRALLDALAVEILARH 60
61 HDYSLPAAGESWQSFLRNNAMSFRRALLRYRDGAKVHLGTRPDEKQYDTVETQLRFMTEN 120
121 GFSLRDGLYAISAVSHFTLGAVLEQQEHTAALENLPPLLREALQIMDSDDGEQAFLHGLE 180
181 SLIRGFEVQLTALLQ
Interface Residues: 23, 24, 25, 34, 35, 36, 37, 39, 40, 43, 44, 105
3D-footprint Homologues: 7xaq_B, 4gck_A, 5haw_A, 1jt0_C, 6gy3_A, 5vl9_A, 5fmp_B, 5yej_B, 3zql_B, 5gpc_B, 4jl3_B, 1qpi_A, 6en8_C, 7jnp_A, 6wpa_A, 6yl2_A
Binding Motifs: 1qpi_A CcTa
Binding Sites: 1qpi_M
Publications: Orth P, Schnappinger D, Hillen W, Saenger W, Hinrichs W. Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system. Nature structural biology 7:215-9 (2000). [Pubmed]
Related annotations: PaperBLAST

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