ID O84668_CHLTR Unreviewed; 605 AA. AC O84668; DT 01-NOV-1998, integrated into UniProtKB/TrEMBL. DT 01-NOV-1998, sequence version 1. DT 28-MAR-2018, entry version 120. DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|SAAS:SAAS00924913}; DE EC=5.99.1.3 {ECO:0000256|SAAS:SAAS00924913}; GN Name=gyrB_2 {ECO:0000313|EMBL:AAC68256.1}; GN OrderedLocusNames=CT_661 {ECO:0000313|EMBL:AAC68256.1}; OS Chlamydia trachomatis (strain D/UW-3/Cx). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=272561 {ECO:0000313|EMBL:AAC68256.1, ECO:0000313|Proteomes:UP000000431}; RN [1] {ECO:0000313|EMBL:AAC68256.1, ECO:0000313|Proteomes:UP000000431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx {ECO:0000313|Proteomes:UP000000431}; RX 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 -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|SAAS:SAAS00924961}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00907948}; 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 RefSeq; NP_220180.1; NC_000117.1. DR RefSeq; WP_009872033.1; NC_000117.1. DR ProteinModelPortal; O84668; -. DR EnsemblBacteria; AAC68256; AAC68256; CT_661. DR GeneID; 35555747; -. DR GeneID; 884449; -. DR KEGG; ctr:CT_661; -. DR PATRIC; fig|272561.5.peg.727; -. DR eggNOG; ENOG4105DNX; Bacteria. DR eggNOG; COG0187; LUCA. DR InParanoid; O84668; -. DR KO; K02470; -. DR OMA; DWKEHIR; -. DR BioCyc; CTRA272561:G1G18-703-MONOMER; -. DR Proteomes; UP000000431; Chromosome. DR GO; GO:0009295; C:nucleoid; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central. DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central. DR CDD; cd00075; HATPase_c; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR013759; Topo_IIA_B_C. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR006171; TOPRIM_domain. DR PANTHER; PTHR10169; PTHR10169; 1. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00986; DNA_gyraseB_C; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01751; Toprim; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00924926}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000431}; KW Isomerase {ECO:0000256|SAAS:SAAS00924998}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00924952}; KW Reference proteome {ECO:0000313|Proteomes:UP000000431}; KW Topoisomerase {ECO:0000256|SAAS:SAAS00924964}. FT DOMAIN 397 508 Toprim. {ECO:0000259|PROSITE:PS50880}. FT COILED 345 372 {ECO:0000256|SAM:Coils}. 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 //