ID O84668_CHLTR Unreviewed; 605 AA. AC O84668; DT 01-NOV-1998, integrated into UniProtKB/TrEMBL. DT 01-NOV-1998, sequence version 1. DT 12-JUN-2007, entry version 43. DE DNA Gyrase Subunit B. GN Name=gyrB_2; OrderedLocusNames=CT_661; OS Chlamydia trachomatis. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA CC breakage and rejoining; the B chain catalyzes ATP hydrolysis. The CC enzyme forms an A2B2 tetramer (By similarity). 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; AE001273; AAC68256.1; -; Genomic_DNA. DR PIR; G71487; G71487. DR HSSP; P06982; 1KZN. DR GenomeReviews; AE001273_GR; CT_661. DR KEGG; ctr:CT661; -. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR InterPro; IPR003594; ATP_bd_ATPase. DR InterPro; IPR014721; Ribosomal_S5_D2-type_fold. DR InterPro; IPR001241; Topo_IIA_B/N. DR InterPro; IPR013759; Topo_IIA_B/N_ab. DR InterPro; IPR013506; Topo_IIA_B_2. DR InterPro; IPR011558; Topo_IIA_B_cons. DR Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1. DR Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1. DR Gene3D; G3DSA:3.40.50.670; Topo_IIA_B/N_ab; 1. 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; Nucleotide-binding; KW Topoisomerase. SQ SEQUENCE 605 AA; 68260 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 //