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Protein
Submitted name:

Transcriptional regulator, TetR family

Gene

TM_1030

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-1059-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Transcriptional regulator, TetR familyImported
Gene namesi
Ordered Locus Names:TM_1030Imported
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)Imported
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi243274.TM1030.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z77X-ray2.00A1-200[»]
1ZKGX-ray2.30A/B1-200[»]
2ID6X-ray1.75A1-200[»]
2IEKX-ray1.83A1-200[»]
3IH2X-ray2.30A1-200[»]
3IH3X-ray2.35A1-200[»]
3IH4X-ray2.30A1-200[»]
4I6ZX-ray3.20A/B1-200[»]
4I76X-ray2.10A/B1-200[»]
ProteinModelPortaliQ9X0C0.
SMRiQ9X0C0. Positions 1-200.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

OMAiALKFLMW.
OrthoDBiEOG6ZH2G9.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
1.10.357.10. 1 hit.
InterProiIPR023772. DNA-bd_HTH_TetR-type_CS.
IPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
IPR015893. Tet_transcr_reg_TetR-like_C.
IPR011075. Tet_transcr_reg_TetR-rel_C.
[Graphical view]
PfamiPF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSiPR00455. HTHTETR.
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.

Q9X0C0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSKRDAILK AAVEVFGKKG YDRATTDEIA EKAGVAKGLI FHYFKNKEEL
60 70 80 90 100
YYQAYMSVTE KLQKEFENFL MKNRNRDIFD FMERWIEKKL EYSASHPEEA
110 120 130 140 150
DFLITLVSVD EGLRKRILLD LEKSQRVFFD FVREKLKDLD LAEDVTEEIA
160 170 180 190 200
LKFLMWFFSG FEEVYLRTYQ GKPELLKRDM NTLVEEVKVM LRILKKGMTK
Length:200
Mass (Da):23,801
Last modified:November 1, 1999 - v1
Checksum:iCBF79565CB2D4273
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36107.1.
PIRiE72303.
RefSeqiNP_228836.1. NC_000853.1.
WP_010865247.1. NC_023151.1.
YP_008991874.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36107; AAD36107; TM_1030.
AHD19062; AHD19062; THEMA_09210.
GeneIDi897092.
KEGGitma:TM1030.
tmi:THEMA_09210.
PATRICi23936989. VBITheMar51294_1043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36107.1.
PIRiE72303.
RefSeqiNP_228836.1. NC_000853.1.
WP_010865247.1. NC_023151.1.
YP_008991874.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z77X-ray2.00A1-200[»]
1ZKGX-ray2.30A/B1-200[»]
2ID6X-ray1.75A1-200[»]
2IEKX-ray1.83A1-200[»]
3IH2X-ray2.30A1-200[»]
3IH3X-ray2.35A1-200[»]
3IH4X-ray2.30A1-200[»]
4I6ZX-ray3.20A/B1-200[»]
4I76X-ray2.10A/B1-200[»]
ProteinModelPortaliQ9X0C0.
SMRiQ9X0C0. Positions 1-200.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1030.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36107; AAD36107; TM_1030.
AHD19062; AHD19062; THEMA_09210.
GeneIDi897092.
KEGGitma:TM1030.
tmi:THEMA_09210.
PATRICi23936989. VBITheMar51294_1043.

Phylogenomic databases

OMAiALKFLMW.
OrthoDBiEOG6ZH2G9.

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-1059-MONOMER.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
1.10.357.10. 1 hit.
InterProiIPR023772. DNA-bd_HTH_TetR-type_CS.
IPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
IPR015893. Tet_transcr_reg_TetR-like_C.
IPR011075. Tet_transcr_reg_TetR-rel_C.
[Graphical view]
PfamiPF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSiPR00455. HTHTETR.
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF48498. SSF48498. 1 hit.
PROSITEiPS01081. HTH_TETR_1. 1 hit.
PS50977. HTH_TETR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099Imported.
  2. "Crystal structure of transcriptional regulator (tm1030) at 1.75A resolution."
    Koclega K.D., Chruszcz M., Minor W.
    Submitted (SEP-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
  3. "New crystal form of transcriptional regulator tm1030 from Thermotoga maritima."
    Koclega K.D., Chruszcz M., Minor W.
    Submitted (SEP-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
  4. "Crystal structure of a transcriptional regulator TM1030 from Thermotoga maritima solved by an unusual MAD experiment."
    Koclega K.D., Chruszcz M., Zimmerman M.D., Cymborowski M., Evdokimova E., Minor W.
    J. Struct. Biol. 159:424-432(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
  5. "Crystal structure of TM1030 from Thermotoga maritima at 2.3 A resolution reveals molecular details of its transcription repressor function."
    Premkumar L., Rife C.L., Sri Krishna S., McMullan D., Miller M.D., Abdubek P., Ambing E., Astakhova T., Axelrod H.L., Canaves J.M., Carlton D., Chiu H.J., Clayton T., DiDonato M., Duan L., Elsliger M.A., Feuerhelm J., Floyd R.
    , Grzechnik S.K., Hale J., Hampton E., Han G.W., Haugen J., Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W., Koesema E., Kovarik J.S., Kreusch A., Levin I., McPhillips T.M., Morse A.T., Nigoghossian E., Okach L., Oommachen S., Paulsen J., Quijano K., Reyes R., Rezezadeh F., Rodionov D., Schwarzenbacher R., Spraggon G., van den Bedem H., White A., Wolf G., Xu Q., Hodgson K.O., Wooley J., Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.
    Proteins 68:418-424(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
  7. "Crystal structure of the transcriptional regulator TM1030 with 24bp DNA oligonucleotide."
    Koclega K.D., Chruszcz M., Cooper D.R., Petkowski J.J., Tkaczuk K.L., Joachimiak A., Minor W.
    Submitted (NOV-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS).
  8. "Crystal structure of transcriptional regulator TM1030 with octanol."
    Koclega K.D., Chruszcz M., Cooper D.R., Petkowski J.J., Tkaczuk K.L., Joachimiak A., Minor W.
    Submitted (NOV-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).

Entry informationi

Entry nameiQ9X0C0_THEMA
AccessioniPrimary (citable) accession number: Q9X0C0
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1999
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.