ID A0A345PGS7_9BACI Unreviewed; 651 AA.
AC A0A345PGS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00939};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00939};
DE AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00939};
GN Name=parE {ECO:0000256|HAMAP-Rule:MF_00939,
GN ECO:0000313|EMBL:AXI09207.1};
GN ORFNames=CUC15_09820 {ECO:0000313|EMBL:AXI09207.1};
OS Oceanobacillus zhaokaii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=2052660 {ECO:0000313|EMBL:AXI09207.1, ECO:0000313|Proteomes:UP000253908};
RN [1] {ECO:0000313|Proteomes:UP000253908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=160 {ECO:0000313|Proteomes:UP000253908};
RA Zhu W.;
RL Submitted (NOV-2017) 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_00939}.
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_00939};
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_00939}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00939}.
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DR EMBL; CP024848; AXI09207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345PGS7; -.
DR KEGG; ocn:CUC15_09820; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000253908; 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_00939; ParE_type2; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005740; ParE_type2.
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; IPR006171; TOPRIM_domain.
DR NCBIfam; TIGR01058; parE_Gpos; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF12; 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; 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 {ECO:0000256|HAMAP-Rule:MF_00939};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00939};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00939};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00939};
KW Reference proteome {ECO:0000313|Proteomes:UP000253908};
KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00939}.
FT DOMAIN 422..536
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 381..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 115..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 456
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 508
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 624
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
SQ SEQUENCE 651 AA; 73078 MW; EABF8576942ACEA1 CRC64;
MTNQPTQYTD ESIQVLEGLD AVRKRPGMYI GSTDSRGLHH LVFEIVDNAV DEALSGYGNE
IKVTIHKDNS ISVEDSGRGI PTGVHSSGKP TAEVIFTVLH AGGKFGQGGY KTSGGLHGVG
ASVVNALSEW LEVTIFRDGQ SFKQRFENGG KPVTTLEKQG PTKKSGTIIH FKPDALIFSS
LIYDYEIISE RLRESAFLLK GITIELYDQR TEEKELFHYP NGIEAFVSYL NEEKDTLSPI
VSFEGEQQEI EVEFAFQYND GYSETMLSFV NHVRTRDGGT HESGARTAIT RTINEYARRI
GILKEKDKNL EGSDIREGMT AVVSVRVPED KLQFEGQTKG RLGTIEARSV VDSIVSEHLS
YFLEENPDIA GMITRKSLKA KEARDAARKA REEARTGKQR KKRDTLLSGK LTPAQSRNPK
RNELYLVEGD SAGGSAKQGR DRKFQAVLPL RGKVINTEKA KLEDVMKNEE ISTIIHTIGA
GVGSDFDLED VQYDKVIIMT DADTDGAHIQ VLLLTFFYRY MRKLIEAGKV FIGLPPLFKI
SKGKGKSEKV VYAWEEEEMK RAVQEFKNGY TVQRYKGLGE MNADQLWDTT MNPETRTLIR
VTIDDFARAD RRITTLMGDK VEPRRKWIES NVEFGLEEDA TILENEKIIK E
//
