ID   A0A4U7KHM7_9GAMM        Unreviewed;       631 AA.
AC   A0A4U7KHM7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
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:TKY82692.1};
GN   ORFNames=EDI29_09205 {ECO:0000313|EMBL:TKY82692.1};
OS   Pectobacterium polonicum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=2485124 {ECO:0000313|EMBL:TKY82692.1, ECO:0000313|Proteomes:UP000309996};
RN   [1] {ECO:0000313|EMBL:TKY82692.1, ECO:0000313|Proteomes:UP000309996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPMP315 {ECO:0000313|EMBL:TKY82692.1,
RC   ECO:0000313|Proteomes:UP000309996};
RX   PubMed=30973319; DOI=.1099/ijsem.0.003387;
RA   Waleron M., Misztak A., Waleron M., Jonca J., Furmaniak M., Waleron K.;
RT   "Pectobacterium polonicum sp. nov. isolated from vegetable fields.";
RL   Int. J. Syst. Evol. Microbiol. 69:1751-1759(2019).
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:TKY82692.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; RJTN01000006; TKY82692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U7KHM7; -.
DR   EnsemblBacteria; TKY82692; TKY82692; EDI29_09205.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000309996; 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: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_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_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   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; 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          413..526
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         111..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            447
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            498
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            616
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ   SEQUENCE   631 AA;  70217 MW;  9CCF941E2DD34370 CRC64;
     MAQSSYNADA IEVLSGLEPV RRRPGMYTDT TRPNHLGQEV IDNSVDEALA GHARRIDVIL
     HADQSLEVID DGRGMPVDIH PEEGVPAVEL ILCRLHAGGK FSGKNYQFSG GLHGVGISVV
     NALSTRVEVT VRRDGQVYDI AFENGDKVQE LTVTGTCGRR NTGTRVHFWP DEKFFDSPRF
     SVSRLTHLLK AKAVLCPGVE IIFKDKVNNT EQRWCYQDGL NDYLCEAVNG LITLPEKPFL
     GSITGETEAV DWALLWLPEG GELLTESYVN LIPTPMGGTH VNGLRQGLLD AMREFCEFRN
     ILPRGVKLSA DDIWERCAYV LSVKMQEPQF AGQTKERLSS RQCAAFVSGV VKDAFSLWLN
     QNVQAAEQLA ELAISSAQRR MRAAKKVVRK KLTSGPALPG KLADCTSQDL NRTELFLVEG
     DSAGGSAKQA REREFQAIMP LKGKILNTWE VSSDEVLASQ EVHDISVAIG IDPDSTDLSQ
     LRYGKICILA DADSDGLHIA TLLCALFVRH FRALVQGGHV YVAMPPLYRI DLGKEVYYAL
     DEEEKAGVLE QLKRKRGKPN VQRFKGLGEM NPLQLRETTL DPNTRRLVQL TINDEDMDQT
     MAMMDMLLAK KRSEDRRNWL QEKGDKAEIE V
//