ID B1M0P2_METRJ Unreviewed; 686 AA.
AC B1M0P2;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
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 OrderedLocusNames=Mrad2831_1003 {ECO:0000313|EMBL:ACB23012.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB23012.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB23012.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) 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; CP001001; ACB23012.1; -; Genomic_DNA.
DR RefSeq; WP_012318005.1; NC_010505.1.
DR AlphaFoldDB; B1M0P2; -.
DR STRING; 426355.Mrad2831_1003; -.
DR KEGG; mrd:Mrad2831_1003; -.
DR PATRIC; fig|426355.14.peg.1044; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_4_1_5; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000006589; 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_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 466..580
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 154..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 500
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 552
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT SITE 668
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ SEQUENCE 686 AA; 74917 MW; 6276FEA0CFC71E07 CRC64;
MSDPARDLFG PGGKGAAARP PEPRRRLDAS ASVATLAAAE PEGGYTASDI EVLEGLEPVR
RRPGMYIGGT DERALHHLFA EVIDNSMDEA VAGHASFIEV ELEESGALVV TDNGRGIPVD
PHPKFPGKSA LEVIMTTLHA GGKFDSKVYE TSGGLHGVGI SVVNALSDLL EVEVARNQTL
YRQTFSRGHA QGALELVGRV QNRRGTRVRF HPDAQIFGSL KFDPRRLFKM ARSKAYLFGG
VEIRWRCAPA LLEGLADVPA EAVHRFPDGL RDYLARDIDG KELVTEAMFS GKITKPGSHG
SLEWAVAWMV AEDGFSHSYC NTIPTPEGGT HEAGLRVALL RGLREHAERV NQAKRMTAVT
TDDVMATCAS MLSVFIREPE FQGQTKDKLA TVEAQRIVET AVRDAFDHWL AASPAQANKL
LDWVIDRAEE RLRRRQEKEV ARKSATRKLR LPGKLADCSA AGTAGSEIFI VEGDSAGGSA
KQARDRATQA ILPLRGKILN VASASRDKLG ANQLISDLTL ALGCGTGTAF RETDLRYEKV
IIMTDADVDG AHIASLLITF FYRQMPKLID RGHLYLAIPP LYRLQQGSKV AYARDDADRE
RIVKTVFKGG KVEIGRFKGL GEMMPAQLKE TTMDPKKRTL LRVAVLDEAR ESTGDTVERL
MGNKPEARFA FISERAAFAE GADLDI
//
