ID A0A1P8Q4T3_9LACO Unreviewed; 666 AA.
AC A0A1P8Q4T3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=BTM29_09915 {ECO:0000313|EMBL:APX72845.1};
OS Companilactobacillus allii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1847728 {ECO:0000313|EMBL:APX72845.1, ECO:0000313|Proteomes:UP000187499};
RN [1] {ECO:0000313|Proteomes:UP000187499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WiKim39 {ECO:0000313|Proteomes:UP000187499};
RA Jung M.Y., Lee S.H.;
RL Submitted (DEC-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_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; CP019323; APX72845.1; -; Genomic_DNA.
DR RefSeq; WP_076616922.1; NZ_RHNV01000001.1.
DR AlphaFoldDB; A0A1P8Q4T3; -.
DR STRING; 1847728.BTM29_09915; -.
DR KEGG; lalw:BTM29_09915; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000187499; 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:UP000187499};
KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00939}.
FT DOMAIN 423..537
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 385..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 113..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 457
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 509
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 625
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
SQ SEQUENCE 666 AA; 74401 MW; F67054933BA56E35 CRC64;
MPKSSYDDSS IQILEGLEAV RKRPGMYIGS TDSRGLHHLV YEIVDNAVDE ALSGYGKEIN
VSINHDNSIT VVDHGRGMPT GMHASGKPTI EVILTVLHAG GKFSENSYKT SGGLHGVGSS
VVNALSEWMT VRVVRDHKVY EERFENGGHP VGTLRKTGTT KEENGTTISF KPDASIFQTT
KFNYDTLAER LRESAFLLKG VKFTITDLRG DEEHGDVFHY EDGIQSFVKY LNEGKDTIGG
IFYIEGENSD IEIEFSGQYN DGYSENIISF VNNVRTTDGG THESGMKSGL TKAFNDYARK
VGLLKESSKN LEGSDVREGL SAIISVRIPE EILQFEGQTK GKLGTAQARS AVDQLVYEQM
SFYLMENGEQ AQTLVKKALK AREAREAARK ARETTRNGKK NKKTDGLLSG KLTPAQSKNA
KKNELFLVEG DSAGGSAKQG RDRKFQAILP LRGKVLNTQK AKLDEIYKNE EINTMIYTIG
AGVGADFKLE DRNYDKIIIM TDADDDGSHI QILLLTFFYR YMRPLVDAGH VYIALPPLYK
LQKGKGDKTK MQYCWTPDEL QEAIKKMGKG YELQRFKGLG EMNADQLWNT TMDPESRILI
RVNIDDTALA ERRVTTLMGD KVKPRREWIE KNVRFNGTEE GDNILEKVDD TDPVDNKIVD
DLLNKE
//
