ID A0A0K1NGC4_9BURK Unreviewed; 658 AA.
AC A0A0K1NGC4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ADJ79_07725 {ECO:0000313|EMBL:AKU68132.1};
OS Ottowia sp. oral taxon 894.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ottowia.
OX NCBI_TaxID=1658672 {ECO:0000313|EMBL:AKU68132.1, ECO:0000313|Proteomes:UP000056623};
RN [1] {ECO:0000313|Proteomes:UP000056623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W10237 {ECO:0000313|Proteomes:UP000056623};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012073; AKU68132.1; -; Genomic_DNA.
DR RefSeq; WP_050716498.1; NZ_CP012073.1.
DR AlphaFoldDB; A0A0K1NGC4; -.
DR STRING; 1658672.ADJ79_07725; -.
DR KEGG; oto:ADJ79_07725; -.
DR PATRIC; fig|1658672.3.peg.1989; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000056623; 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 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 427..544
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT BINDING 6
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 70
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 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 461
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 516
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 643
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ SEQUENCE 658 AA; 71455 MW; 2950D27D6AE6EB15 CRC64;
MSTPAYAESS IRVLKGLEPV RQRPGMYTRT DTPLHIIQEV IDNAADEALA GFCKRIKLTL
HADGSVSVED DGRGIPFGLH PEENAPVAEL VFTRLHAGGK FDKGAGGAYS FSGGLHGVGV
SVTNALSTRL EATIWRDGQV AHLAFAGGDV AEPLTVRPAH DGGAAAGDRK QGTTVRVWPD
ARYFESAALP LAELTHLLRS KAVLMPGVSV TFIDEKRGTR QSWQYKGGLR DYLMQTLPAD
AVIPVFEGAG HAGRDDGSFA EGEGAEWAVA FTEEGQPVRE SYVNLIPTPA GGTHDSGLRD
GLFHAVKNFI ELHALLPKGV KLMPEDVFAR ASYVLSAKVL DPQFQGQIKE RLNSRDALRL
VSGYVRPALE LWLNAHVEHG KRLAELAIRA AQTRQRASQK VEKRKGSGVA VLPGKLTDCE
SRDTARNEIF LVEGDSAGGS AKMGRDKETQ AILPLRGKVL NTWEVERDLL FKNTEIHDIA
VALGVDPHGA GDTPDLLGLR YGKVCILSDA DVDGSHIQVL LLTLFFRHFP ALIHAGHVFV
ARPPLFRIDA PARGKKPAAK LYALDQAELD ATLDKLRKEG VPEGKWTISR FKGLGEMNAE
QLWETTLNPD TRRLMPVRLG PLGEAATAEH MNRLMGKGEA AARRELMERH GDAVEVDV
//
