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Protein

DNA replication terminus site-binding protein

Gene

tus

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.

GO - Molecular functioni

  • sequence-specific DNA binding Source: EcoCyc

GO - Biological processi

  • DNA replication termination Source: EcoCyc
  • replication fork arrest involved in DNA replication termination Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11038-MONOMER.
ECOL316407:JW1602-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication terminus site-binding proteinUniRule annotation
Short name:
Ter-binding proteinUniRule annotation
Gene namesi
Name:tusUniRule annotation
Synonyms:tau
Ordered Locus Names:b1610, JW1602
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11038. tus.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309DNA replication terminus site-binding proteinPRO_0000049413Add
BLAST

Proteomic databases

PaxDbiP16525.
PRIDEiP16525.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaBP0ACB03EBI-1124579,EBI-548978

Protein-protein interaction databases

BioGridi4260254. 85 interactions.
DIPiDIP-11056N.
IntActiP16525. 2 interactions.
MINTiMINT-584635.
STRINGi511145.b1610.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2823Combined sources
Beta strandi33 – 408Combined sources
Helixi46 – 483Combined sources
Beta strandi49 – 513Combined sources
Beta strandi54 – 563Combined sources
Beta strandi59 – 624Combined sources
Helixi63 – 7311Combined sources
Helixi79 – 813Combined sources
Beta strandi84 – 863Combined sources
Beta strandi88 – 903Combined sources
Beta strandi96 – 1027Combined sources
Helixi104 – 12926Combined sources
Turni130 – 1323Combined sources
Turni136 – 1383Combined sources
Helixi139 – 1468Combined sources
Helixi152 – 1565Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi176 – 1816Combined sources
Helixi183 – 19311Combined sources
Beta strandi194 – 1974Combined sources
Helixi206 – 22015Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi237 – 2448Combined sources
Beta strandi247 – 2548Combined sources
Beta strandi259 – 2646Combined sources
Helixi265 – 2673Combined sources
Helixi282 – 2843Combined sources
Beta strandi296 – 3005Combined sources
Helixi301 – 3033Combined sources
Beta strandi305 – 3084Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ECRX-ray2.70A1-309[»]
1SUTNMR-A223-244[»]
2EWJX-ray2.70A1-309[»]
2I05X-ray2.60A1-309[»]
2I06X-ray2.20A1-309[»]
4XR0X-ray2.80A1-309[»]
4XR1X-ray2.40A1-309[»]
4XR2X-ray2.35A1-309[»]
4XR3X-ray2.70A1-309[»]
ProteinModelPortaliP16525.
SMRiP16525. Positions 5-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16525.

Family & Domainsi

Sequence similaritiesi

Belongs to the Tus family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105KR1. Bacteria.
ENOG410XSWR. LUCA.
HOGENOMiHOG000280323.
KOiK10748.
OMAiQVQYACP.
OrthoDBiEOG6VHZ89.

Family and domain databases

Gene3Di3.50.14.10. 2 hits.
HAMAPiMF_00483. Rep_term_Tus.
InterProiIPR008865. DNA_replication_term_site-bd.
[Graphical view]
PfamiPF05472. Ter. 1 hit.
[Graphical view]
SUPFAMiSSF56596. SSF56596. 1 hit.
TIGRFAMsiTIGR02648. rep_term_tus. 1 hit.

Sequencei

Sequence statusi: Complete.

P16525-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARYDLVDRL NTTFRQMEQE LAIFAAHLEQ HKLLVARVFS LPEVKKEDEH
60 70 80 90 100
NPLNRIEVKQ HLGNDAQSLA LRHFRHLFIQ QQSENRSSKA AVRLPGVLCY
110 120 130 140 150
QVDNLSQAAL VSHIQHINKL KTTFEHIVTV ESELPTAARF EWVHRHLPGL
160 170 180 190 200
ITLNAYRTLT VLHDPATLRF GWANKHIIKN LHRDEVLAQL EKSLKSPRSV
210 220 230 240 250
APWTREEWQR KLEREYQDIA ALPQNAKLKI KRPVKVQPIA RVWYKGDQKQ
260 270 280 290 300
VQHACPTPLI ALINRDNGAG VPDVGELLNY DADNVQHRYK PQAQPLRLII

PRLHLYVAD
Length:309
Mass (Da):35,783
Last modified:August 1, 1990 - v1
Checksum:iEC495E4D8E9DE887
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 10218NRSSK…LCYQV → SQQQGHCPSAWLLCSGS in CAA27699 (PubMed:3541901).CuratedAdd
BLAST
Sequence conflicti121 – 1222KT → EA in CAA27699 (PubMed:3541901).Curated
Sequence conflicti134 – 1341L → I in CAA27699 (PubMed:3541901).Curated
Sequence conflicti150 – 1501L → V in CAA27699 (PubMed:3541901).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90037 Genomic DNA. Translation: BAA14085.1.
U41101 Genomic DNA. Translation: AAA82083.1.
U00096 Genomic DNA. Translation: AAC74682.1.
AP009048 Genomic DNA. Translation: BAA15348.1.
X04065 Genomic DNA. Translation: CAA27699.1.
PIRiB32161. DNECTS.
RefSeqiNP_416127.1. NC_000913.3.
WP_000135181.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74682; AAC74682; b1610.
BAA15348; BAA15348; BAA15348.
GeneIDi945135.
KEGGiecj:JW1602.
eco:b1610.
PATRICi32118522. VBIEscCol129921_1681.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90037 Genomic DNA. Translation: BAA14085.1.
U41101 Genomic DNA. Translation: AAA82083.1.
U00096 Genomic DNA. Translation: AAC74682.1.
AP009048 Genomic DNA. Translation: BAA15348.1.
X04065 Genomic DNA. Translation: CAA27699.1.
PIRiB32161. DNECTS.
RefSeqiNP_416127.1. NC_000913.3.
WP_000135181.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ECRX-ray2.70A1-309[»]
1SUTNMR-A223-244[»]
2EWJX-ray2.70A1-309[»]
2I05X-ray2.60A1-309[»]
2I06X-ray2.20A1-309[»]
4XR0X-ray2.80A1-309[»]
4XR1X-ray2.40A1-309[»]
4XR2X-ray2.35A1-309[»]
4XR3X-ray2.70A1-309[»]
ProteinModelPortaliP16525.
SMRiP16525. Positions 5-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260254. 85 interactions.
DIPiDIP-11056N.
IntActiP16525. 2 interactions.
MINTiMINT-584635.
STRINGi511145.b1610.

Proteomic databases

PaxDbiP16525.
PRIDEiP16525.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74682; AAC74682; b1610.
BAA15348; BAA15348; BAA15348.
GeneIDi945135.
KEGGiecj:JW1602.
eco:b1610.
PATRICi32118522. VBIEscCol129921_1681.

Organism-specific databases

EchoBASEiEB1031.
EcoGeneiEG11038. tus.

Phylogenomic databases

eggNOGiENOG4105KR1. Bacteria.
ENOG410XSWR. LUCA.
HOGENOMiHOG000280323.
KOiK10748.
OMAiQVQYACP.
OrthoDBiEOG6VHZ89.

Enzyme and pathway databases

BioCyciEcoCyc:EG11038-MONOMER.
ECOL316407:JW1602-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP16525.
PROiP16525.

Family and domain databases

Gene3Di3.50.14.10. 2 hits.
HAMAPiMF_00483. Rep_term_Tus.
InterProiIPR008865. DNA_replication_term_site-bd.
[Graphical view]
PfamiPF05472. Ter. 1 hit.
[Graphical view]
SUPFAMiSSF56596. SSF56596. 1 hit.
TIGRFAMsiTIGR02648. rep_term_tus. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification of a DNA replication terminus (ter) site-binding protein in Escherichia coli and identification of the structural gene."
    Hidaka M., Kobayashi T., Takenaka S., Takeya H., Horiuchi T.
    J. Biol. Chem. 264:21031-21037(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-46.
  2. "tus, the trans-acting gene required for termination of DNA replication in Escherichia coli, encodes a DNA-binding protein."
    Hill T.M., Tecklenburg M.L., Pelletier A.J., Kuempel P.L.
    Proc. Natl. Acad. Sci. U.S.A. 86:1593-1597(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12."
    Woods S.A., Miles J.S., Roberts R.E., Guest J.R.
    Biochem. J. 237:547-557(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-309.
    Strain: K12.
  7. "Structure of a replication-terminator protein complexed with DNA."
    Kamada K., Horiuchi T., Ohsumi K., Shimamoto N., Morikawa K.
    Nature 383:598-603(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  8. "Proline pipe helix: structure of the tus proline repeat determined by 1H NMR."
    Butcher D.J., Nedved M.L., Neiss T.G., Moe G.R.
    Biochemistry 35:698-703(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 223-244.

Entry informationi

Entry nameiTUS_ECOLI
AccessioniPrimary (citable) accession number: P16525
Secondary accession number(s): Q59400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 11, 2016
This is version 138 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.