DNA replication terminus site-binding protein - Escherichia coli (strain K12)

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P16525 (TUS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 16, 2012. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA replication terminus site-binding protein
Short name=Ter-binding protein

Gene names

Name:	tus
Synonyms:	tau
Ordered Locus Names:	b1610, JW1602

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP MF_00483
Subunit structure	Monomer.
Subcellular location	Cytoplasm HAMAP MF_00483.
Sequence similarities	Belongs to the tus family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Cytoplasm
Ligand	DNA-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA replication termination Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 309

309

DNA replication terminus site-binding protein HAMAP MF_00483

PRO_0000049413

Experimental info

Sequence conflict

85 – 102

NRSSK…LCYQV → SQQQGHCPSAWLLCSGS in CAA27699. Ref.6

Sequence conflict

121 – 122

KT → EA in CAA27699. Ref.6

Sequence conflict

134

L → I in CAA27699. Ref.6

Sequence conflict

150

L → V in CAA27699. Ref.6

Secondary structure

309

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P16525 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: EC495E4D8E9DE887
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FASTA

309

35,783

        10         20         30         40         50         60 
MARYDLVDRL NTTFRQMEQE LAIFAAHLEQ HKLLVARVFS LPEVKKEDEH NPLNRIEVKQ 

        70         80         90        100        110        120 
HLGNDAQSLA LRHFRHLFIQ QQSENRSSKA AVRLPGVLCY QVDNLSQAAL VSHIQHINKL 

       130        140        150        160        170        180 
KTTFEHIVTV ESELPTAARF EWVHRHLPGL ITLNAYRTLT VLHDPATLRF GWANKHIIKN 

       190        200        210        220        230        240 
LHRDEVLAQL EKSLKSPRSV APWTREEWQR KLEREYQDIA ALPQNAKLKI KRPVKVQPIA 

       250        260        270        280        290        300 
RVWYKGDQKQ VQHACPTPLI ALINRDNGAG VPDVGELLNY DADNVQHRYK PQAQPLRLII 


PRLHLYVAD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2687269] [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: 2646639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 3541901] [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: 8857533] [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: 8547250] [Abstract] Cited for: STRUCTURE BY NMR OF 223-244.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

DNECTS. B32161.

RefSeq

NP_416127.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ECR	X-ray	2.70	A	1-309	[»]
1SUT	NMR	-	A	223-241	[»]
2EWJ	X-ray	2.70	A	1-309	[»]
2I05	X-ray	2.60	A	1-309	[»]
2I06	X-ray	2.20	A	1-309	[»]

ProteinModelPortal

P16525.

SMR

P16525. Positions 5-309.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-11056N.

IntAct

P16525. 2 interactions.

MINT

MINT-584635.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002421; EBESCP00000002421; EBESCG00000001971.
EBESCT00000017934; EBESCP00000017225; EBESCG00000016990.

GeneID

945135.

GenomeReviews

Gene locus JW1602 in contig AP009048_GR.
Gene locus b1610 in contig U00096_GR.

KEGG

eco:b1610.

PATRIC

32118522. VBIEscCol129921_1681.

Organism-specific databases

EchoBASE

EB1031.

EcoGene

EG11038. tus.

Phylogenomic databases

eggNOG

NOG04361.

HOGENOM

HOG000280323.

K10748.

OMA

QVQYACP.

ProtClustDB

PRK02951.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11038-MONOMER.

Gene expression databases

Genevestigator

P16525.

Family and domain databases

Gene3D

G3DSA:3.50.14.10. Rep_term_tus. 2 hits.

HAMAP

MF_00483. Rep_term_tus.
[Tree]

InterPro

IPR008865. DNA_replication_term_site-bd.
[Graphical view]

Pfam

PF05472. Ter. 1 hit.
[Graphical view]

SUPFAM

SSF56596. Rep_term_tus. 1 hit.

TIGRFAMs

TIGR02648. Rep_term_tus. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P16525.

Entry information

Entry name

TUS_ECOLI

Accession

Primary (citable) accession number: P16525
Secondary accession number(s): Q59400

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 16, 2012
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents