ID A0A1I2AVA0_9RHOB Unreviewed; 651 AA.
AC A0A1I2AVA0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04488523_107208 {ECO:0000313|EMBL:SFE47914.1};
OS Sulfitobacter brevis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=74348 {ECO:0000313|EMBL:SFE47914.1, ECO:0000313|Proteomes:UP000198977};
RN [1] {ECO:0000313|EMBL:SFE47914.1, ECO:0000313|Proteomes:UP000198977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11443 {ECO:0000313|EMBL:SFE47914.1,
RC ECO:0000313|Proteomes:UP000198977};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOMW01000007; SFE47914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2AVA0; -.
DR STRING; 74348.SAMN04488523_107208; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000198977; Unassembled WGS sequence.
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 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00938};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00938};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00938};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00938}; Reference proteome {ECO:0000313|Proteomes:UP000198977};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00938}.
FT DOMAIN 432..546
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 466
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 518
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 635
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ SEQUENCE 651 AA; 71887 MW; DA7B3A0EBEF6B605 CRC64;
MTDLLSGKPT KEYDASSIQV LEDMEHVRLR PGMYIGGKDD RALHHMVAEI IDNSMDEAVA
GHATWIELEL HGNGHVTVRD NGRGIPIDPH PKDPTKSALE IIFCTLNAGG KFSGDSYETS
GGLHGVGSSV VNALSDHLRV EVARNRELFA MEFSRGIPQG KLEKIGAAPN RRGTAVTFHP
DPDIFGALTL KPARLFAMAR SKAYLFSGVE IRWKCEIADG DTPQEATFHF PGGLSDYLNE
TLGSATTYAE KPFGGMVDFR DKFNTPGKVE WSINWTPSRD GFIQSYCNTI PTPEGGTHEA
GFWAAILKGI KAYGELVGNR KASQITRDDL ITGGCALVSC FIREPEFVGQ TKDRLATVDA
QRMVENAVRD HFDHWLTSDT KSAGAILDFI VLRAEERLRR RQEKETARKT ATKKLRLPGK
LTDCTSKTRE GTELFIVEGD SAGGSGKGAR NRHNQALLPL KGKILNVLGA ASNKLTTNAE
ISDLCEALGV GMGSRFNLDD LRYDKIIIMT DADVDGAHIA ALLMTFFYTQ MRPLIDAGHL
YLACPPLYRL TQGAKRIYVA DDIEKNYWME KGLGGKGKID LQRFKGLGEM DAKDLKETTM
DPDTRKLIRV SVQEDVPGET SDLVERLMGK KPELRYAYIQ ENAQFVEELD V
//
