ID O84668 PRELIMINARY; PRT; 605 AA. AC O84668; DT 01-NOV-1998 (TrEMBLrel. 08, Created) DT 01-NOV-1998 (TrEMBLrel. 08, Last sequence update) DT 01-OCT-2003 (TrEMBLrel. 25, Last annotation update) DE DNA Gyrase Subunit B. GN Name=gyrB_2; OrderedLocusNames=CT661; OS Chlamydia trachomatis. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=D / UW-3 / Cx; RX MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., RA Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: RT Chlamydia trachomatis."; RL Science 282:754-759(1998). CC -!- FUNCTION: DNA gyrase negatively supercoils closed circular double- CC stranded DNA in an ATP-dependent manner and also catalyzes the CC interconversion of other topological isomers of double-stranded CC DNA rings, including catenanes and knotted rings (By similarity). CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. 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; AE001336; AAC68256.1; -. DR PIR; G71487; G71487. DR HSSP; P06982; 1KZN. DR GO; GO:0005524; F:ATP binding; IEA. DR GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA. DR GO; GO:0006265; P:DNA topological change; IEA. DR InterPro; IPR003594; ATPbind_ATPase. DR InterPro; IPR011558; DNA_gyrase_B. DR InterPro; IPR001241; DNA_topoisoII. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF02518; HATPase_c; 1. DR PRINTS; PR00418; TPI2FAMILY. DR ProDom; PD149633; DNA_gyrase_B; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. KW ATP-binding; Complete proteome; Isomerase; Topoisomerase. SQ SEQUENCE 605 AA; 68259 MW; 71BD6AC922A952F5 CRC64; MRKKTAYSES SIISLASLDH IRLRAGMYIG RLGDGSQAED GIYTLFKEVV DNAIDEFVMG YGHTIHITGD AHELSIRDEG RGIPLGKVID CVSKINTGAK YTQDVFHFSV GLNGVGLKAV NALSQHFSVR SVRNKKFLKA SFSKGILLHT EQGATQDPDG TEVVFSPDHE LFENFSFQVE FLKKKIRQYT YLHPGLTIIY NGERIVSTRG LLDLFEEEVQ TPLLYSPITF QHSDLAFLFS HTETSSEQYF SFVNGQETTD GGTHLVAFKE GIVKGVNEFF GKNFSSQDIR EGLAGCIAIK IASPIFESQT KNKLGNTNIR AELAKRVKEA VLSSLKKNPS SAERIQEKIK LNEKTRKNAQ FLKQELKDKQ KKLHYKIPKL RDCKFHLTDN SLYGKNSSIF ITEGESASAS ILASRNPLTQ AVFSLRGKPM NVFSSKEETI YKNDELFYLT TALGLHKDSL QNLRYNQVIL ATDADVDGMH IRNLMITFFL KTFLPLVASN HLFILETPLF KVRHKDATFY CYSEEEKLST IEHIGKKESS LEITRFKGLG EISPKEFKSF IGADMRLTPV SLPDTETLDT LLQFYMGKNT KERKLFIIEN LVTNL //