ID TOP1_ECOLI STANDARD; PRT; 865 AA. AC P06612; DT 01-JAN-1988 (Rel. 06, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE DNA TOPOISOMERASE I (EC 5.99.1.2) (OMEGA-PROTEIN) (RELAXING ENZYME) DE (UNTWISTING ENZYME) (SWIVELASE). GN TOPA OR SUPX. OS Escherichia coli. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87141163. 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 REVISIONS, SEQUENCE FROM N.A. RA LYNCH D.A., WANG J.C.; RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE; 97426617. RA BLATTNER F.R., PLUNKETT G. III, BLOCH C.A., PERNA N.T., BURLAND V., RA RILEY M., COLLADO-VIDES J., GLASNER F.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 [4] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 97251357. RA AIBA H., BABA T., FUJITA K., HAYASHI K., INADA T., ISONO K., RA ITOH T., KASAI H., KASHIMOTO K., KIMURA S., KITAKAWA M., RA KITAGAWA M., MAKINO K., MIKI T., MIZOBUCHI K., MORI H., MORI T., RA MOTOMURA K., NAKADE S., NAKAMURA Y., NASHIMOTO H., NISHIO Y., RA OSHIMA T., SAITO N., SAMPEI G., SEKI Y., SIVASUNDARAM S., RA TAGAMI H., TAKEDA J., TAKEMOTO K., TAKEUCHI Y., WADA C., RA 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 [5] RP SEQUENCE OF 698-865 FROM N.A. RX MEDLINE; 87194810. 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-590. RX MEDLINE; 94159070. RA LIMA C.D., WANG J.C., MONDRAGON A.; RT "Three-dimensional structure of the 67K N-terminal fragment of E. RT coli DNA topoisomerase I."; RL Nature 367:138-146(1994). RN [7] RP STRUCTURE BY NMR OF 745-865. RX MEDLINE; 95298771. 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). CC -!- FUNCTION: THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CC CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. CC -!- CATALYTIC ACTIVITY: ATP-INDEPENDENT BREAKAGE OF SINGLE-STRANDED CC DNA, FOLLOWED BY PASSAGE AND REJOINING. CC -!- SUBUNIT: MONOMER. CC -!- MISCELLANEOUS: WHEN A TOPOISOMERASE TRANSIENTLY BREAKS A DNA CC BACKBONE BOND, IT SIMULTANEOUSLY FORMS A PROTEIN-DNA LINK, IN CC WHICH A TYROSYL OXYGEN IN THE ENZYME IS JOINED TO A DNA PHOSPHORUS CC AT ONE END OF THE ENZYME-SEVERED DNA STRAND. CC -!- SIMILARITY: BELONGS TO PROKARYOTIC TYPE I/III TOPOISOMERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; -. DR EMBL; M15041; AAA23641.1; -. DR EMBL; AE000225; AAC74356.1; -. DR EMBL; D90764; CAB20720.1; -. DR EMBL; D90765; CAB20745.1; -. DR PIR; A25786; ISECTP. DR PDB; 1ECL; 31-JUL-95. DR PDB; 1YUA; 08-MAR-96. DR ECO2DBASE; I115.0; 6TH EDITION. DR ECOGENE; EG11013; TOPA. DR PFAM; PF01131; Topoisom_bac; 1. DR PFAM; PF01396; zf-C4_Topoisom; 2. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. KW Isomerase; Topoisomerase; DNA-binding; Zinc-finger; 3D-structure. FT ACT_SITE 319 319 DNA CLEAVAGE. FT ZN_FING 599 630 C4-TYPE (POTENTIAL). FT ZN_FING 662 689 C4-TYPE (POTENTIAL). FT ZN_FING 711 736 C4-TYPE (POTENTIAL). FT CONFLICT 787 787 P -> R (IN REF. 5). SQ SEQUENCE 865 AA; 97349 MW; 0333884D CRC32; 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 //