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Protein

Tetracycline repressor protein class B from transposon Tn10

Gene

tetR

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei64Involved in binding magnesium-tetracycline complexBy similarity1
Metal bindingi100Magnesium [Mg-tetracycline]By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi26 – 45H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Antibiotic resistance, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tetracycline repressor protein class B from transposon Tn10
Gene namesi
Name:tetR
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64H → Y: 1000-fold reduction of affinity for tetracycline. 1 Publication1
Mutagenesisi82N → H: 100-fold reduction of affinity for tetracycline. 1 Publication1
Mutagenesisi103T → I: <10-fold reduction of affinity for tetracycline. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000706131 – 207Tetracycline repressor protein class B from transposon Tn10Add BLAST207

Structurei

Secondary structure

1207
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi6 – 24Combined sources19
Helixi27 – 34Combined sources8
Helixi38 – 44Combined sources7
Helixi48 – 63Combined sources16
Helixi75 – 91Combined sources17
Helixi96 – 100Combined sources5
Helixi107 – 122Combined sources16
Helixi127 – 157Combined sources31
Beta strandi164 – 166Combined sources3
Helixi168 – 180Combined sources13
Helixi182 – 187Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/B1-50[»]
3FK7X-ray2.06A/B1-50[»]
3ZQFX-ray2.56A1-187[»]
3ZQGX-ray2.45A1-187[»]
3ZQHX-ray1.60A1-187[»]
3ZQIX-ray1.50A/B1-187[»]
4AC0X-ray2.45A2-203[»]
ProteinModelPortaliP04483.
SMRiP04483.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04483.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 63HTH tetR-typePROSITE-ProRule annotationAdd BLAST61

Sequence similaritiesi

Contains 1 HTH tetR-type DNA-binding domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.357.10. 1 hit.
InterProiIPR023772. DNA-bd_HTH_TetR-type_CS.
IPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
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.
[Graphical view]
PfamiPF02909. TetR_C. 1 hit.
PF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSiPR00455. HTHTETR.
PR00400. TETREPRESSOR.
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF48498. SSF48498. 1 hit.
PROSITEiPS01081. HTH_TETR_1. 1 hit.
PS50977. HTH_TETR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRLDKSKVI NSALELLNEV GIEGLTTRKL AQKLGVEQPT LYWHVKNKRA
60 70 80 90 100
LLDALAIEML DRHHTHFCPL EGESWQDFLR NNAKSFRCAL LSHRDGAKVH
110 120 130 140 150
LGTRPTEKQY ETLENQLAFL CQQGFSLENA LYALSAVGHF TLGCVLEDQE
160 170 180 190 200
HQVAKEERET PTTDSMPPLL RQAIELFDHQ GAEPAFLFGL ELIICGLEKQ

LKCESGS
Length:207
Mass (Da):23,355
Last modified:August 13, 1987 - v1
Checksum:iA9FD75972352CC80
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00694 Genomic DNA. Translation: CAA25291.1.
J01830 Genomic DNA. Translation: AAB59093.1.
PIRiA03576. RPECTN.
RefSeqiWP_000088605.1. NZ_MBPW01000086.1.
YP_001096449.1. NC_009133.1.

Genome annotation databases

GeneIDi25059028.
4924774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00694 Genomic DNA. Translation: CAA25291.1.
J01830 Genomic DNA. Translation: AAB59093.1.
PIRiA03576. RPECTN.
RefSeqiWP_000088605.1. NZ_MBPW01000086.1.
YP_001096449.1. NC_009133.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/B1-50[»]
3FK7X-ray2.06A/B1-50[»]
3ZQFX-ray2.56A1-187[»]
3ZQGX-ray2.45A1-187[»]
3ZQHX-ray1.60A1-187[»]
3ZQIX-ray1.50A/B1-187[»]
4AC0X-ray2.45A2-203[»]
ProteinModelPortaliP04483.
SMRiP04483.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25059028.
4924774.

Miscellaneous databases

EvolutionaryTraceiP04483.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.357.10. 1 hit.
InterProiIPR023772. DNA-bd_HTH_TetR-type_CS.
IPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
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.
[Graphical view]
PfamiPF02909. TetR_C. 1 hit.
PF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSiPR00455. HTHTETR.
PR00400. TETREPRESSOR.
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF48498. SSF48498. 1 hit.
PROSITEiPS01081. HTH_TETR_1. 1 hit.
PS50977. HTH_TETR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTETR2_ECOLX
AccessioniPrimary (citable) accession number: P04483
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 30, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Transposable element

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.