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P04483 (TETR2_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tetracycline repressor protein class B from transposon Tn10
Gene names
Name:tetR
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to tetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.

Sequence similarities

Contains 1 HTH tetR-type DNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Tetracycline repressor protein class B from transposon Tn10
PRO_0000070613

Regions

Domain3 – 6361HTH tetR-type
DNA binding26 – 4520H-T-H motif Potential

Sites

Metal binding1001Magnesium [Mg-tetracycline] By similarity
Site641Involved in binding magnesium-tetracycline complex By similarity

Experimental info

Mutagenesis641H → Y: 1000-fold reduction of affinity for tetracycline.
Mutagenesis821N → H: 100-fold reduction of affinity for tetracycline.
Mutagenesis1031T → I: <10-fold reduction of affinity for tetracycline.

Secondary structure

....................... 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04483 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: A9FD75972352CC80

FASTA20723,355
        10         20         30         40         50         60 
MSRLDKSKVI NSALELLNEV GIEGLTTRKL AQKLGVEQPT LYWHVKNKRA LLDALAIEML 

        70         80         90        100        110        120 
DRHHTHFCPL EGESWQDFLR NNAKSFRCAL LSHRDGAKVH LGTRPTEKQY ETLENQLAFL 

       130        140        150        160        170        180 
CQQGFSLENA LYALSAVGHF TLGCVLEDQE HQVAKEERET PTTDSMPPLL RQAIELFDHQ 

       190        200 
GAEPAFLFGL ELIICGLEKQ LKCESGS 

« Hide

References

[1]"Nucleotide sequence of the repressor gene of the TN10 tetracycline resistance determinant."
Postle K., Nguyen T.T., Bertrand K.P.
Nucleic Acids Res. 12:4849-4863(1984) [PubMed: 6330687] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A threonine to alanine exchange at position 40 of Tet repressor alters the recognition of the sixth base pair of tet operator from GC to AT."
Altschmied L., Baumeister R., Pfleiderer K., Hillen W.
EMBO J. 7:4011-4017(1988) [PubMed: 3208760] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
[3]"Overlapping divergent promoters control expression of Tn10 tetracycline resistance."
Bertrand K.P., Postle K., Wray L.V. Jr., Reznikoff W.S.
Gene 23:149-156(1983) [PubMed: 6311683] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[4]"Mutations in the Tn10 tet repressor that interfere with induction. Location of the tetracycline-binding domain."
Smith L.D., Bertrand K.P.
J. Mol. Biol. 203:949-959(1988) [PubMed: 3062183] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00694 Genomic DNA. Translation: CAA25291.1.
J01830 Genomic DNA. Translation: AAB59093.1.
PIRRPECTN. A03576.
RefSeqYP_001096449.1. NC_009133.1.
YP_002456171.1. NC_011812.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NS7X-ray2.40A/B/C/D1-187[»]
2NS8X-ray2.55A/B/C/D1-187[»]
2VKVX-ray1.74A1-50[»]
2XGCX-ray2.15A/B1-50[»]
2XGDX-ray2.25A1-50[»]
2XGEX-ray2.14A/B1-50[»]
3FK6X-ray2.10A/B1-12[»]
3FK7X-ray2.06A/B1-12[»]
ProteinModelPortalP04483.
SMRP04483. Positions 2-201.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4924774.
7256840.

Phylogenomic databases

ProtClustDBPRK13756.

Family and domain databases

InterProIPR001647. DNA-bd_HTH_TetR-type.
IPR023772. DNA-bd_HTH_TetR-type_CS.
IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR003012. Tet_transcr_reg_TetR.
IPR015893. Tet_transcr_reg_TetR-like_C.
IPR011075. Tet_transcr_reg_TetR-rel_C.
IPR004111. Tet_transcr_reg_TetR_C.
IPR023773. Tscrpt_reg_HTH_TetR-type.
[Graphical view]
Gene3DG3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
G3DSA:1.10.357.10. TetR_C. 1 hit.
PfamPF02909. TetR_C. 1 hit.
PF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSPR00455. HTHTETR.
PR00400. TETREPRESSOR.
SUPFAMSSF46689. Homeodomain_like. 1 hit.
SSF48498. TetR_like_C. 1 hit.
PROSITEPS01081. HTH_TETR_1. 1 hit.
PS50977. HTH_TETR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTETR2_ECOLX
AccessionPrimary (citable) accession number: P04483
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 28, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families