ID A0A2A4YXA1_9PROT Unreviewed; 743 AA.
AC A0A2A4YXA1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ECO:0000313|EMBL:PCI98925.1};
GN ORFNames=COB13_12610 {ECO:0000313|EMBL:PCI98925.1};
OS OCS116 cluster bacterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; OCS116 cluster.
OX NCBI_TaxID=2030921 {ECO:0000313|EMBL:PCI98925.1, ECO:0000313|Proteomes:UP000218076};
RN [1] {ECO:0000313|Proteomes:UP000218076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-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_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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCI98925.1}.
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DR EMBL; NVUS01000018; PCI98925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4YXA1; -.
DR Proteomes; UP000218076; 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 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; 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_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|HAMAP-Rule:MF_00938};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00938}.
FT DOMAIN 522..636
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 211..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 556
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 608
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 725
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ SEQUENCE 743 AA; 81244 MW; 29B1E5115CFF834D CRC64;
MTDDLFGGLL PTSDGSKPSK KPNENKARTP DPLVQAAAQK STSAPAETPI AAQNPVEATE
SVAPTPSAPD AGSANISTSN DEIDMPVPAA APIGKTKGEE DYGAADIEIL EGLEPVRHRP
GMYIGGTDEK ALHHLFAEII DNSMDEVVAG HASWIDISLD ADGYVTVTDN GRGMPIDPHP
KFENKSALEV IFTILHAGGK FNSDVYETSG GLHGVGASVV NALSDDLIVE VARGQQLYRQ
TFSRGIPQGG LEHLGPIKNR RGTKVRFRPD HQIFGAKAKF RASRVYKMAR AKAYLYGGVQ
IRWSCAPELI GENDTTPLKE TFHFPNGLSD YLETRIQGKT RITEEIFRGK TTKDGGHGSV
EWAIAWYLGD GFVNSYCNTV PTIDGGTHEA GMRAALLKGL KAYGDLKNVK KAAQIIGDDV
LTGVGILLSV FIREPEFQGQ TKEKLSSSEA NRIVETTLRD PFDHWLTTNP RQADRLLEWA
VDRSDERLKR KKDKEVSRKA ATRRLRLPGK LADCSINSAA GTELFIVEGD SAGGSAKQAR
NRKNQAILPL RGKILNVANA TSAKLAQNQQ INDLLLALGV GTGKNYSNSD LRYEKIIIMT
DADVDGAHIA SLLITFFYRE IPDLIKNKHL YLAVPPLYRI TQGAKTLYAR DDDHKDELMK
TEFNGRGKID IGRFKGLGEM MPAQLKETTM LAEKRTLLQV TIDEDEIELT ATVVEQLMGS
KPEARFQFIQ QNAQFADGAE LDI
//
