ID PARE_RICCN Reviewed; 662 AA. AC Q92IW1; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000255|HAMAP-Rule:MF_00938}; DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00938}; DE AltName: Full=Topoisomerase IV subunit B {ECO:0000255|HAMAP-Rule:MF_00938}; GN Name=parE {ECO:0000255|HAMAP-Rule:MF_00938}; OrderedLocusNames=RC0309; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). CC -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It CC relaxes supercoiled DNA. Performs the decatenation events required CC during the replication of a circular DNA molecule. {ECO:0000255|HAMAP- CC Rule:MF_00938}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent breakage, passage and rejoining of double- CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00938}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00938}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00938}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00938}; CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges CC with both the protein and the DNA. Can also accept other divalent metal CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|HAMAP-Rule:MF_00938}; CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP- CC Rule:MF_00938}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00938}. 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; AE006914; AAL02847.1; -; Genomic_DNA. DR PIR; E97738; E97738. DR RefSeq; WP_010976968.1; NC_003103.1. DR AlphaFoldDB; Q92IW1; -. DR SMR; Q92IW1; -. DR GeneID; 928839; -. DR KEGG; rco:RC0309; -. DR PATRIC; fig|272944.4.peg.354; -. DR HOGENOM; CLU_006146_4_1_5; -. DR Proteomes; UP000000816; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR CDD; cd16928; HATPase_GyrB-like; 1. DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR HAMAP; MF_00938; ParE_type1; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR000565; Topo_IIA_B. DR InterPro; IPR013759; Topo_IIA_B_C. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR005737; TopoIV_B_Gneg. DR InterPro; IPR006171; TOPRIM_domain. DR NCBIfam; TIGR01055; parE_Gneg; 1. DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1. DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 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 PRINTS; PR01159; DNAGYRASEB. DR PRINTS; PR00418; TPI2FAMILY. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding; KW Nucleotide-binding; Topoisomerase. FT CHAIN 1..662 FT /note="DNA topoisomerase 4 subunit B" FT /id="PRO_0000273117" FT DOMAIN 439..553 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 60 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 87 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 129..135 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 359 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 445 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 518 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 518 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT BINDING 520 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT SITE 470 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT SITE 473 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT SITE 525 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" FT SITE 641 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00938" SQ SEQUENCE 662 AA; 73827 MW; D84CB42C32308088 CRC64; MSDLFSFNKE KKNKLVDNNY SAKDIEVLEG LEPVRKRPGM YIGGTDSNAM HHLVSEVLDN AMDEAVAGFA SIITITMHHD HSITIFDNGR GIPIDNHPKF PDKSALEVIL TTLHSGGKFS NNVYHTAGGL HGVGISVVNA LSKHLEIKVY KQGKLYSQSY SKGEKLTDLI CEEASKRLRG TSINFTPDPE IFSEKLHFNP KKIYELARSK AYLYRGVTIE WACEVEVQSD IPKKALISFP NGLKDYLSSK ITLDNLVIPG IFAGNIESKS DRIKLEWAIC WQNNDSSAFV QSYCNTVPTP QGGTHEQGLK SAILRGLKAY GEMIGNKKAA NLTIEDILET ASVVLSIFIA EPSFQGQTKE KLVSNGVSKP VENIIKDHFD HFLSSDKALA TNLLEHVISI AEFRISKKNE KNISRKNATQ KLRLPGKLAD CTRTSPEGTE LFIVEGDSAG GSAKQARNRE TQAVLPLWGK VLNVASSTLE KIVNNQAIQD LEIALACGSL KNYKKENLRY EKIIIMTDAD VDGAHIASLL MTFFFLRMPK LVEEGHLYLA KPPLYRLTQS NKTYYAGDEE EKAKLMDKLL KASKAKIEVG RFKGLGEMMP AQLKETTMHP EKRSLLKVTL ADFQNVDKIV DDLMGKKPEK RFQFIYEQAL VKMDKIISEL DI //