ID TOP1_ECOLI Reviewed; 865 AA. AC P06612; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 18-APR-2012, entry version 132. DE RecName: Full=DNA topoisomerase 1; DE EC=5.99.1.2; DE AltName: Full=DNA topoisomerase I; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Swivelase; DE AltName: Full=Untwisting enzyme; GN Name=topA; Synonyms=supX; OrderedLocusNames=b1274, JW1266; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87141163; PubMed=3029379; DOI=10.1016/0022-2836(86)90129-4; RA Tse-Dinh Y.-C., Wang J.C.; RT "Complete nucleotide sequence of the topA gene encoding Escherichia RT coli DNA topoisomerase I."; RL J. Mol. Biol. 191:321-331(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. RA Lynch D.A., Wang J.C.; RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97251357; 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., RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to 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 MEDLINE=97426617; 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., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 698-865. RX MEDLINE=87194810; PubMed=3032952; RA Ostrowski J., Jagura-Burdzy G., Kredich N.M.; RT "DNA sequences of the cysB regions of Salmonella typhimurium and RT Escherichia coli."; RL J. Biol. Chem. 262:5999-6005(1987). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-590. RX MEDLINE=94159070; PubMed=8114910; DOI=10.1038/367138a0; RA Lima C.D., Wang J.C., Mondragon A.; RT "Three-dimensional structure of the 67K N-terminal fragment of E. coli RT DNA topoisomerase I."; RL Nature 367:138-146(1994). RN [8] RP STRUCTURE BY NMR OF 745-865. RX MEDLINE=95298771; PubMed=7779808; DOI=10.1021/bi00023a008; RA Yu L., Zhu C.-X., Tse-Dinh Y.-C., Fesik S.W.; RT "Solution structure of the C-terminal single-stranded DNA-binding RT domain of Escherichia coli topoisomerase I."; RL Biochemistry 34:7622-7628(1995). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-596 OF MUTANT ASN-111 IN RP COMPLEX WITH DNA. RX PubMed=21482796; DOI=10.1073/pnas.1100300108; RA Zhang Z., Cheng B., Tse-Dinh Y.C.; RT "Crystal structure of a covalent intermediate in DNA cleavage and RT rejoining by Escherichia coli DNA topoisomerase I."; RL Proc. Natl. Acad. Sci. U.S.A. 108:6939-6944(2011). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA CC introduced during the DNA replication and transcription by CC transiently cleaving and rejoining one strand of the DNA duplex. CC Introduces a single-strand break via transesterification at a CC target site in duplex DNA. The scissile phosphodiester is attacked CC by the catalytic tyrosine of the enzyme, resulting in the CC formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the CC expulsion of a 3'-OH DNA strand. The free DNA strand than CC undergoes passage around the unbroken strand thus removing DNA CC supercoils. Finally, in the religation step, the DNA 3'-OH attacks CC the covalent intermediate to expel the active-site tyrosine and CC restore the DNA phosphodiester backbone. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC -!- SIMILARITY: Contains 1 Toprim domain. 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; X04475; CAA28164.1; -; Genomic_DNA. DR EMBL; M15041; AAA23641.1; -; Genomic_DNA. DR EMBL; U00096; AAC74356.1; -; Genomic_DNA. DR EMBL; AP009048; BAA14811.1; -; Genomic_DNA. DR PIR; E64875; ISECTP. DR RefSeq; NP_415790.1; NC_000913.2. DR PDB; 1CY0; X-ray; 2.45 A; A=1-597. DR PDB; 1CY1; X-ray; 2.30 A; A=1-597. DR PDB; 1CY2; X-ray; 2.30 A; A=1-597. DR PDB; 1CY4; X-ray; 2.55 A; A=1-597. DR PDB; 1CY6; X-ray; 2.50 A; A=1-597. DR PDB; 1CY7; X-ray; 2.40 A; A=1-597. DR PDB; 1CY8; X-ray; 2.45 A; A=1-597. DR PDB; 1CY9; X-ray; 1.80 A; A/B=214-477. DR PDB; 1CYY; X-ray; 2.15 A; A/B=214-477. DR PDB; 1ECL; X-ray; 1.90 A; A=1-597. DR PDB; 1MW8; X-ray; 1.90 A; X=1-592. DR PDB; 1MW9; X-ray; 1.67 A; X=1-592. DR PDB; 1YUA; NMR; -; A=745-865. DR PDB; 3PWT; X-ray; 1.90 A; A=1-596. DR PDBsum; 1CY0; -. DR PDBsum; 1CY1; -. DR PDBsum; 1CY2; -. DR PDBsum; 1CY4; -. DR PDBsum; 1CY6; -. DR PDBsum; 1CY7; -. DR PDBsum; 1CY8; -. DR PDBsum; 1CY9; -. DR PDBsum; 1CYY; -. DR PDBsum; 1ECL; -. DR PDBsum; 1MW8; -. DR PDBsum; 1MW9; -. DR PDBsum; 1YUA; -. DR PDBsum; 3PWT; -. DR ProteinModelPortal; P06612; -. DR SMR; P06612; 2-638, 745-865. DR DIP; DIP-11011N; -. DR IntAct; P06612; 65. DR MINT; MINT-1218330; -. DR ECO2DBASE; I115.0; 6TH EDITION. DR EnsemblBacteria; EBESCT00000004769; EBESCP00000004769; EBESCG00000003893. DR EnsemblBacteria; EBESCT00000004770; EBESCP00000004770; EBESCG00000003893. DR EnsemblBacteria; EBESCT00000004771; EBESCP00000004771; EBESCG00000003893. DR EnsemblBacteria; EBESCT00000004772; EBESCP00000004772; EBESCG00000003893. DR EnsemblBacteria; EBESCT00000004773; EBESCP00000004773; EBESCG00000003893. DR EnsemblBacteria; EBESCT00000016049; EBESCP00000015340; EBESCG00000015109. DR GeneID; 945862; -. DR GenomeReviews; AP009048_GR; JW1266. DR GenomeReviews; U00096_GR; b1274. DR KEGG; eco:b1274; -. DR PATRIC; 32117806; VBIEscCol129921_1323. DR EchoBASE; EB1006; -. DR EcoGene; EG11013; topA. DR eggNOG; COG0551; -. DR HOGENOM; HBG512935; -. DR KO; K03168; -. DR OMA; EEYWSID; -. DR ProtClustDB; PRK07561; -. DR BioCyc; EcoCyc:EG11013-MONOMER; -. DR BioCyc; MetaCyc:EG11013-MONOMER; -. DR EvolutionaryTrace; P06612; -. DR Genevestigator; P06612; -. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IGI:EcoliWiki. DR Gene3D; G3DSA:1.10.460.10; Topo_IA_cen_sub1; 2. DR Gene3D; G3DSA:2.70.20.10; Topo_IA_cen_sub2; 2. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013825; Topo_IA_cen_sub2. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd. DR InterPro; IPR013498; Topo_IA_Znf. DR InterPro; IPR005733; TopoI_bac-type. DR InterPro; IPR013263; TopoI_Znr_bac. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; Topo_IA; 1. DR Pfam; PF08272; Topo_Zn_Ribbon; 2. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 2. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; Topo_IA_core; 1. DR TIGRFAMs; TIGR01051; TopA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; DNA-binding; Isomerase; KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat; KW Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1 865 DNA topoisomerase 1. FT /FTId=PRO_0000145147. FT DOMAIN 3 140 Toprim. FT ZN_FING 599 630 C4-type 1. FT ZN_FING 662 689 C4-type 2. FT ZN_FING 711 736 C4-type 3. FT ACT_SITE 319 319 O-(5'-phospho-DNA)-tyrosine intermediate. FT CONFLICT 787 787 P -> R (in Ref. 6; AAA23641). FT STRAND 4 9 FT HELIX 11 17 FT HELIX 18 20 FT STRAND 25 29 FT STRAND 34 36 FT HELIX 67 71 FT TURN 75 79 FT TURN 87 89 FT HELIX 90 100 FT STRAND 104 108 FT HELIX 114 127 FT HELIX 131 133 FT STRAND 134 136 FT HELIX 144 152 FT HELIX 159 186 FT HELIX 197 213 FT STRAND 218 227 FT STRAND 233 241 FT HELIX 251 263 FT STRAND 266 278 FT HELIX 286 297 FT HELIX 301 313 FT STRAND 316 318 FT HELIX 329 342 FT HELIX 345 347 FT STRAND 361 363 FT HELIX 377 379 FT HELIX 385 400 FT STRAND 406 417 FT STRAND 420 431 FT HELIX 433 437 FT STRAND 458 470 FT HELIX 479 488 FT TURN 494 496 FT HELIX 497 506 FT STRAND 509 513 FT STRAND 516 519 FT HELIX 521 533 FT TURN 535 538 FT HELIX 540 554 FT HELIX 560 571 FT HELIX 573 578 FT HELIX 582 584 FT STRAND 755 762 FT STRAND 764 767 FT STRAND 769 773 FT STRAND 776 778 FT STRAND 780 783 FT TURN 784 787 FT HELIX 797 802 FT TURN 803 806 FT HELIX 812 816 FT STRAND 827 832 FT TURN 833 836 FT STRAND 837 842 FT STRAND 853 855 SQ SEQUENCE 865 AA; 97350 MW; 8C13F767FE5B178C CRC64; MGKALVIVES PAKAKTINKY LGSDYVVKSS VGHIRDLPTS GSAAKKSADS TSTKTAKKPK KDERGALVNR MGVDPWHNWE AHYEVLPGKE KVVSELKQLA EKADHIYLAT DLDREGEAIA WHLREVIGGD DARYSRVVFN EITKNAIRQA FNKPGELNID RVNAQQARRF MDRVVGYMVS PLLWKKIARG LSAGRVQSVA VRLVVERERE IKAFVPEEFW EVDASTTTPS GEALALQVTH QNDKPFRPVN KEQTQAAVSL LEKARYSVLE REDKPTTSKP GAPFITSTLQ QAASTRLGFG VKKTMMMAQR LYEAGYITYM RTDSTNLSQD AVNMVRGYIS DNFGKKYLPE SPNQYASKEN SQEAHEAIRP SDVNVMAESL KDMEADAQKL YQLIWRQFVA CQMTPAKYDS TTLTVGAGDF RLKARGRILR FDGWTKVMPA LRKGDEDRIL PAVNKGDALT LVELTPAQHF TKPPARFSEA SLVKELEKRG IGRPSTYASI ISTIQDRGYV RVENRRFYAE KMGEIVTDRL EENFRELMNY DFTAQMENSL DQVANHEAEW KAVLDHFFSD FTQQLDKAEK DPEEGGMRPN QMVLTSIDCP TCGRKMGIRT ASTGVFLGCS GYALPPKERC KTTINLVPEN EVLNVLEGED AETNALRAKR RCPKCGTAMD SYLIDPKRKL HVCGNNPTCD GYEIEEGEFR IKGYDGPIVE CEKCGSEMHL KMGRFGKYMA CTNEECKNTR KILRNGEVAP PKEDPVPLPE LPCEKSDAYF VLRDGAAGVF LAANTFPKSR ETRAPLVEEL YRFRDRLPEK LRYLADAPQQ DPEGNKTMVR FSRKTKQQYV SSEKDGKATG WSAFYVDGKW VEGKK //