TUS_ECOLI
ID TUS_ECOLI Reviewed; 309 AA.
AC P16525; Q59400;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=DNA replication terminus site-binding protein {ECO:0000255|HAMAP-Rule:MF_00483};
DE Short=Ter-binding protein {ECO:0000255|HAMAP-Rule:MF_00483};
GN Name=tus {ECO:0000255|HAMAP-Rule:MF_00483}; Synonyms=tau;
GN OrderedLocusNames=b1610, JW1602;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-46.
RX PubMed=2687269; DOI=10.1016/s0021-9258(19)30040-7;
RA Hidaka M., Kobayashi T., Takenaka S., Takeya H., Horiuchi T.;
RT "Purification of a DNA replication terminus (ter) site-binding protein in
RT Escherichia coli and identification of the structural gene.";
RL J. Biol. Chem. 264:21031-21037(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2646639; DOI=10.1073/pnas.86.5.1593;
RA Hill T.M., Tecklenburg M.L., Pelletier A.J., Kuempel P.L.;
RT "tus, the trans-acting gene required for termination of DNA replication in
RT Escherichia coli, encodes a DNA-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1593-1597(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-309.
RC STRAIN=K12;
RX PubMed=3541901; DOI=10.1042/bj2370547;
RA Woods S.A., Miles J.S., Roberts R.E., Guest J.R.;
RT "Structural and functional relationships between fumarase and aspartase.
RT Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of
RT Escherichia coli K12.";
RL Biochem. J. 237:547-557(1986).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8857533; DOI=10.1038/383598a0;
RA Kamada K., Horiuchi T., Ohsumi K., Shimamoto N., Morikawa K.;
RT "Structure of a replication-terminator protein complexed with DNA.";
RL Nature 383:598-603(1996).
RN [8]
RP STRUCTURE BY NMR OF 223-244.
RX PubMed=8547250; DOI=10.1021/bi952419l;
RA Butcher D.J., Nedved M.L., Neiss T.G., Moe G.R.;
RT "Proline pipe helix: structure of the tus proline repeat determined by 1H
RT NMR.";
RL Biochemistry 35:698-703(1996).
CC -!- FUNCTION: Trans-acting protein required for termination of DNA
CC replication. Binds to DNA replication terminator sequences (terA to
CC terF) to prevent the passage of replication forks. The termination
CC efficiency will be affected by the affinity of this protein for the
CC terminator sequence.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the Tus family. {ECO:0000255|HAMAP-
CC Rule:MF_00483}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D90037; BAA14085.1; -; Genomic_DNA.
DR EMBL; U41101; AAA82083.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74682.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15348.1; -; Genomic_DNA.
DR EMBL; X04065; CAA27699.1; -; Genomic_DNA.
DR PIR; B32161; DNECTS.
DR RefSeq; NP_416127.1; NC_000913.3.
DR RefSeq; WP_000135181.1; NZ_SSZK01000001.1.
DR PDB; 1ECR; X-ray; 2.70 A; A=1-309.
DR PDB; 1SUT; NMR; -; A=223-244.
DR PDB; 2EWJ; X-ray; 2.70 A; A=1-309.
DR PDB; 2I05; X-ray; 2.60 A; A=1-309.
DR PDB; 2I06; X-ray; 2.20 A; A=1-309.
DR PDB; 4XR0; X-ray; 2.80 A; A=1-309.
DR PDB; 4XR1; X-ray; 2.40 A; A=1-309.
DR PDB; 4XR2; X-ray; 2.35 A; A=1-309.
DR PDB; 4XR3; X-ray; 2.70 A; A=1-309.
DR PDBsum; 1ECR; -.
DR PDBsum; 1SUT; -.
DR PDBsum; 2EWJ; -.
DR PDBsum; 2I05; -.
DR PDBsum; 2I06; -.
DR PDBsum; 4XR0; -.
DR PDBsum; 4XR1; -.
DR PDBsum; 4XR2; -.
DR PDBsum; 4XR3; -.
DR AlphaFoldDB; P16525; -.
DR SMR; P16525; -.
DR BioGRID; 4260254; 85.
DR BioGRID; 849524; 1.
DR DIP; DIP-11056N; -.
DR IntAct; P16525; 2.
DR MINT; P16525; -.
DR STRING; 511145.b1610; -.
DR jPOST; P16525; -.
DR PaxDb; P16525; -.
DR PRIDE; P16525; -.
DR EnsemblBacteria; AAC74682; AAC74682; b1610.
DR EnsemblBacteria; BAA15348; BAA15348; BAA15348.
DR GeneID; 945135; -.
DR KEGG; ecj:JW1602; -.
DR KEGG; eco:b1610; -.
DR PATRIC; fig|1411691.4.peg.652; -.
DR EchoBASE; EB1031; -.
DR eggNOG; ENOG502Z895; Bacteria.
DR HOGENOM; CLU_078181_0_0_6; -.
DR OMA; QVQYACP; -.
DR PhylomeDB; P16525; -.
DR BioCyc; EcoCyc:EG11038-MON; -.
DR EvolutionaryTrace; P16525; -.
DR PRO; PR:P16525; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0006274; P:DNA replication termination; IDA:EcoCyc.
DR GO; GO:0071807; P:replication fork arrest involved in DNA replication termination; IDA:EcoCyc.
DR Gene3D; 3.50.14.10; -; 1.
DR HAMAP; MF_00483; Rep_term_Tus; 1.
DR InterPro; IPR008865; DNA_replication_term_site-bd.
DR InterPro; IPR036381; Tus_dom1.
DR InterPro; IPR036384; Tus_sf.
DR Pfam; PF05472; Ter; 1.
DR SUPFAM; SSF56596; SSF56596; 1.
DR TIGRFAMs; TIGR02648; rep_term_tus; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA replication;
KW DNA-binding; Reference proteome.
FT CHAIN 1..309
FT /note="DNA replication terminus site-binding protein"
FT /id="PRO_0000049413"
FT CONFLICT 85..102
FT /note="NRSSKAAVRLPGVLCYQV -> SQQQGHCPSAWLLCSGS (in Ref. 6;
FT CAA27699)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..122
FT /note="KT -> EA (in Ref. 6; CAA27699)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="L -> I (in Ref. 6; CAA27699)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="L -> V (in Ref. 6; CAA27699)"
FT /evidence="ECO:0000305"
FT HELIX 6..28
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4XR0"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4XR2"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 104..129
FT /evidence="ECO:0007829|PDB:2I06"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4XR2"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:2I06"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2I06"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:2I06"
SQ SEQUENCE 309 AA; 35783 MW; EC495E4D8E9DE887 CRC64;
MARYDLVDRL NTTFRQMEQE LAIFAAHLEQ HKLLVARVFS LPEVKKEDEH NPLNRIEVKQ
HLGNDAQSLA LRHFRHLFIQ QQSENRSSKA AVRLPGVLCY QVDNLSQAAL VSHIQHINKL
KTTFEHIVTV ESELPTAARF EWVHRHLPGL ITLNAYRTLT VLHDPATLRF GWANKHIIKN
LHRDEVLAQL EKSLKSPRSV APWTREEWQR KLEREYQDIA ALPQNAKLKI KRPVKVQPIA
RVWYKGDQKQ VQHACPTPLI ALINRDNGAG VPDVGELLNY DADNVQHRYK PQAQPLRLII
PRLHLYVAD