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Protein

Tetracycline repressor protein class D

Gene

tetR

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei64 – 641Involved in binding magnesium-tetracycline complex
Metal bindingi100 – 1001Magnesium [Mg-tetracycline]

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi26 – 4520H-T-H motifPROSITE-ProRule annotationAdd
BLAST

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 D
Gene namesi
Name:tetR
Encoded oniPlasmid RA10 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 218217Tetracycline repressor protein class DPRO_0000070615Add
BLAST

Proteomic databases

PRIDEiP0ACT4.

Expressioni

Inductioni

By the [Mg-tetracycline]+ complex.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2419Combined sources
Helixi27 – 348Combined sources
Helixi38 – 447Combined sources
Helixi48 – 6316Combined sources
Beta strandi64 – 685Combined sources
Beta strandi70 – 745Combined sources
Helixi75 – 9117Combined sources
Helixi96 – 1005Combined sources
Beta strandi102 – 1043Combined sources
Helixi107 – 1093Combined sources
Helixi110 – 12213Combined sources
Helixi127 – 15630Combined sources
Beta strandi163 – 1653Combined sources
Helixi168 – 17811Combined sources
Beta strandi180 – 1823Combined sources
Helixi183 – 20321Combined sources
Beta strandi204 – 2085Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6IX-ray2.40A6-218[»]
1BJZX-ray2.20A3-208[»]
1ORKX-ray2.40A3-208[»]
1QPIX-ray2.50A4-206[»]
2FJ1X-ray2.20A2-208[»]
2NS7X-ray2.40A/B/C/D188-208[»]
2NS8X-ray2.55A/B/C/D188-208[»]
2O7OX-ray1.89A2-208[»]
2TCTX-ray2.10A2-208[»]
2TRTX-ray2.50A2-218[»]
2VKEX-ray1.62A3-208[»]
2VKVX-ray1.74A51-208[»]
2X6OX-ray2.30A3-208[»]
2X9DX-ray2.51A3-208[»]
2XB5X-ray2.50A2-208[»]
2XGCX-ray2.15A/B51-208[»]
2XGDX-ray2.25A51-208[»]
2XGEX-ray2.14A/B51-208[»]
2XPUX-ray1.55A3-208[»]
2XPVX-ray1.49A3-208[»]
2XPWX-ray1.44A3-208[»]
2XRLX-ray1.85A3-208[»]
3FK6X-ray2.10A/B51-208[»]
3FK7X-ray2.06A/B51-208[»]
3ZQFX-ray2.56A188-208[»]
3ZQGX-ray2.45A188-208[»]
3ZQHX-ray1.60A188-208[»]
3ZQIX-ray1.50A/B188-208[»]
4ABZX-ray1.89A3-208[»]
4AUXX-ray2.25A2-208[»]
4B1RX-ray1.95A3-208[»]
4B3AX-ray1.70A3-208[»]
4D7MX-ray1.75A3-208[»]
4D7NX-ray1.89A3-208[»]
4V2FX-ray2.40A3-208[»]
4V2GX-ray2.70A/B3-208[»]
5FKKX-ray1.75A/B3-208[»]
5FKLX-ray1.90A3-208[»]
5FKMX-ray1.63A3-208[»]
5FKNX-ray1.80A/B3-208[»]
5FKOX-ray1.85A3-208[»]
ProteinModelPortaliP0ACT4.
SMRiP0ACT4. Positions 2-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACT4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 6361HTH tetR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

KOiK18476.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ACT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLNRESVI DAALELLNET GIDGLTTRKL AQKLGIEQPT LYWHVKNKRA
60 70 80 90 100
LLDALAVEIL ARHHDYSLPA AGESWQSFLR NNAMSFRRAL LRYRDGAKVH
110 120 130 140 150
LGTRPDEKQY DTVETQLRFM TENGFSLRDG LYAISAVSHF TLGAVLEQQE
160 170 180 190 200
HTAALTDRPA APDENLPPLL REALQIMDSD DGEQAFLHGL ESLIRGFEVQ
210
LTALLQIVGG DKLIIPFC
Length:218
Mass (Da):24,419
Last modified:January 23, 2007 - v2
Checksum:iB1F0F0EE6B4CF991
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01083 Genomic DNA. Translation: CAA25561.1.
PIRiS07359.
RefSeqiWP_000113282.1. NZ_LVMR01000109.1.
YP_002995714.1. NC_012886.1.
YP_007349483.1. NC_020086.1.

Genome annotation databases

GeneIDi15152832.
8094927.
KEGGipg:15152832.
pg:8094927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01083 Genomic DNA. Translation: CAA25561.1.
PIRiS07359.
RefSeqiWP_000113282.1. NZ_LVMR01000109.1.
YP_002995714.1. NC_012886.1.
YP_007349483.1. NC_020086.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6IX-ray2.40A6-218[»]
1BJZX-ray2.20A3-208[»]
1ORKX-ray2.40A3-208[»]
1QPIX-ray2.50A4-206[»]
2FJ1X-ray2.20A2-208[»]
2NS7X-ray2.40A/B/C/D188-208[»]
2NS8X-ray2.55A/B/C/D188-208[»]
2O7OX-ray1.89A2-208[»]
2TCTX-ray2.10A2-208[»]
2TRTX-ray2.50A2-218[»]
2VKEX-ray1.62A3-208[»]
2VKVX-ray1.74A51-208[»]
2X6OX-ray2.30A3-208[»]
2X9DX-ray2.51A3-208[»]
2XB5X-ray2.50A2-208[»]
2XGCX-ray2.15A/B51-208[»]
2XGDX-ray2.25A51-208[»]
2XGEX-ray2.14A/B51-208[»]
2XPUX-ray1.55A3-208[»]
2XPVX-ray1.49A3-208[»]
2XPWX-ray1.44A3-208[»]
2XRLX-ray1.85A3-208[»]
3FK6X-ray2.10A/B51-208[»]
3FK7X-ray2.06A/B51-208[»]
3ZQFX-ray2.56A188-208[»]
3ZQGX-ray2.45A188-208[»]
3ZQHX-ray1.60A188-208[»]
3ZQIX-ray1.50A/B188-208[»]
4ABZX-ray1.89A3-208[»]
4AUXX-ray2.25A2-208[»]
4B1RX-ray1.95A3-208[»]
4B3AX-ray1.70A3-208[»]
4D7MX-ray1.75A3-208[»]
4D7NX-ray1.89A3-208[»]
4V2FX-ray2.40A3-208[»]
4V2GX-ray2.70A/B3-208[»]
5FKKX-ray1.75A/B3-208[»]
5FKLX-ray1.90A3-208[»]
5FKMX-ray1.63A3-208[»]
5FKNX-ray1.80A/B3-208[»]
5FKOX-ray1.85A3-208[»]
ProteinModelPortaliP0ACT4.
SMRiP0ACT4. Positions 2-208.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP0ACT4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi15152832.
8094927.
KEGGipg:15152832.
pg:8094927.

Phylogenomic databases

KOiK18476.

Miscellaneous databases

EvolutionaryTraceiP0ACT4.

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 nameiTETR4_ECOLX
AccessioniPrimary (citable) accession number: P0ACT4
Secondary accession number(s): P09164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

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.