ID W8Q6V2_9PSED Unreviewed; 634 AA.
AC W8Q6V2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00938};
DE AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
GN Name=parE {ECO:0000256|HAMAP-Rule:MF_00938};
GN ORFNames=CD58_02705 {ECO:0000313|EMBL:AHL31870.1};
OS Pseudomonas brassicacearum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=930166 {ECO:0000313|EMBL:AHL31870.1, ECO:0000313|Proteomes:UP000019521};
RN [1] {ECO:0000313|EMBL:AHL31870.1, ECO:0000313|Proteomes:UP000019521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF41 {ECO:0000313|EMBL:AHL31870.1,
RC ECO:0000313|Proteomes:UP000019521};
RX PubMed=24812222;
RA Loewen P.C., Switala J., Fernando W.G., de Kievit T.;
RT "Genome Sequence of Pseudomonas brassicacearum DF41.";
RL Genome Announc. 2:e00390-14(2014).
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:0000256|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:0000256|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-Rule:MF_00938};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC Rule:MF_00938}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00938}.
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DR EMBL; CP007410; AHL31870.1; -; Genomic_DNA.
DR RefSeq; WP_025211525.1; NZ_CP007410.1.
DR AlphaFoldDB; W8Q6V2; -.
DR KEGG; pbc:CD58_02705; -.
DR PATRIC; fig|930166.5.peg.526; -.
DR eggNOG; COG0187; Bacteria.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000019521; 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: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; 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; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF4; DNA TOPOISOMERASE 4 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; PR01098; TOPISMRASE4B.
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 {ECO:0000256|HAMAP-Rule:MF_00938};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00938};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00938};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00938};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00938}.
FT DOMAIN 416..529
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT BINDING 9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 114..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 450
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 501
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 619
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ SEQUENCE 634 AA; 69399 MW; 7F4FF13E61856E06 CRC64;
MATPSASSYN ADAIEVLSGL DPVRKRPGMY TDTSRPNHLA QEVIDNSVDE ALAGHAKSVQ
VILHADHSLE VSDDGRGMPV DIHPEEGVSG VELILTKLHA GGKFSNKNYQ FSGGLHGVGI
SVVNALSNQV RVRVKRDGNE YQMTFADGYK ATELEVIGTV GKRNTGTSVY FAPDPKYFDS
PKFSVSRLKH VLKAKAVLCP GLLVSFEDKA TGEKVEWHYE DGLRSYLVDA VSGFERLPDE
PFCGSLAGNK EAVDWALLWL PEGGESVQES YVNLIPTAQG GTHVNGLRQG LLDAMREFCE
FRNLLPRGVK LAPEDVWERI AFVLSMKMQE PQFSGQTKER LSSREAAAFV SGVVKDAFSL
WLNANPETGL ALAELAINNA GRRLKASKKV ERKRITQGPA LPGKLADCAG QDPMRSELFL
VEGDSAGGSA KQARDKEFQA ILPLRGKILN TWEVDGSEVL ASQEVHNIAV AIGVDPGAAD
MSQLRYGKIC ILADADSDGL HIATLLCALF VQHFRPLVDA GHVYVAMPPL YRIDLGKEIY
YALDEAERDG ILDRLVAEKK RGKPQVTRFK GLGEMNPPQL RETTMDPNTR RLVQLTLDDF
EATSEMMDML LAKKRAGDRK SWLESKGDLA EVLA
//
