ID T0TKZ2_LACLC Unreviewed; 644 AA.
AC T0TKZ2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 08-NOV-2023, entry version 53.
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=LLT6_10255 {ECO:0000313|EMBL:EQC58179.1};
OS Lactococcus cremoris subsp. cremoris TIFN6.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1234876 {ECO:0000313|EMBL:EQC58179.1, ECO:0000313|Proteomes:UP000015854};
RN [1] {ECO:0000313|EMBL:EQC58179.1, ECO:0000313|Proteomes:UP000015854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIFN6 {ECO:0000313|EMBL:EQC58179.1,
RC ECO:0000313|Proteomes:UP000015854};
RX PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA Kleerebezem M., Smid E.J.;
RT "Multifactorial diversity sustains microbial community stability.";
RL ISME J. 7:2126-2136(2013).
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}.
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:EQC58179.1}.
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DR EMBL; ATBB01000041; EQC58179.1; -; Genomic_DNA.
DR AlphaFoldDB; T0TKZ2; -.
DR PATRIC; fig|1234876.3.peg.247; -.
DR Proteomes; UP000015854; 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_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:UP000015854};
KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00939}.
FT DOMAIN 424..538
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 387..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 115..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 458
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 510
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 626
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
SQ SEQUENCE 644 AA; 71634 MW; AE39267D35B7114C CRC64;
MVIDINNYDD SAIQVLEGLD AVRKRPGMYI GSTDGTGLHH LVWEIVDNAV DEALSGFGNK
ITVTINADGS LSVEDEGRGM PVGKHAMGIP TVEVIFTILH AGGKFGQGGY KTSGGLHGVG
SSVVNALSTW LEVEITRDGT VYRQRFENGG HPATTLEKIG KAPKSKTGTK VTFMPDSTIF
STTEFKYNII SERLNESAFL LKEVTISLED KRTDEKEEFH YENGVQDFVA YLNEDKDSLT
PVLYFEGKQD GFEVEVALQY NDGYSENILS FVNNVRTKDG GTHEAGLKTA ITKAMNEYAR
KVNLLKDKDK NLEGSDYREG LTAVLSVLIP EEHLQFEGQT KDKLGSPLAR PVVDSLVSEK
LSFYLMENGE LAQNLIRKAI KAREAREAAR KAREDSRNGK KSKKDKGLLS GKLTPAQTKN
PNKNELYLVE GDSAGGSAKQ GRDRKFQAIL PLRGKVINTE KAKMQDILKN EEINTMIYTI
GAGVGADFTL ADRNYDKVII MTDADTDGAH IQTLLLTFFY RYMKPLVEAG HVYIALPPLY
KMSEGKGKKE KIEYAWTDGE LAELRKQFGK NANLQRYKGL GEMNADQLWE TTMDPETRTL
IQVTIDDAAQ AEKRVSVLMG DKVEPRRKWI ENNVKFTMEE DTAF
//
