ID V8I9B1_STRMT Unreviewed; 647 AA.
AC V8I9B1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=U757_01925 {ECO:0000313|EMBL:ETD96798.1};
OS Streptococcus mitis 21/39.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1415765 {ECO:0000313|EMBL:ETD96798.1, ECO:0000313|Proteomes:UP000018717};
RN [1] {ECO:0000313|EMBL:ETD96798.1, ECO:0000313|Proteomes:UP000018717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21/39 {ECO:0000313|EMBL:ETD96798.1,
RC ECO:0000313|Proteomes:UP000018717};
RA Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Karpova I.Y.,
RA Semashko T.A., Larin A.K., Ischenko D.S., Savinova T.A., Dubovickaya V.A.,
RA Sidorenko S.V., Govorun V.M.;
RT "Genome sequencing of Streptococcus mitis strains.";
RL Submitted (NOV-2013) 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}.
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:ETD96798.1}.
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DR EMBL; AYRR01000002; ETD96798.1; -; Genomic_DNA.
DR RefSeq; WP_023942986.1; NZ_AYRR01000002.1.
DR AlphaFoldDB; V8I9B1; -.
DR PATRIC; fig|1415765.3.peg.382; -.
DR Proteomes; UP000018717; 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 Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00939}.
FT DOMAIN 427..541
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 391..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 118..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 461
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 513
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 629
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
SQ SEQUENCE 647 AA; 71637 MW; 6A0E5D651E546B51 CRC64;
MSKKEININN YNDDAIQVLE GLDAVRKRPG MYIGSTDGAG LHHLVWEIVD NAVDEALSGF
GDRIDVTINK DGSLTVQDHG RGMPTGMHAM GIPTVEVIFT ILHAGGKFGQ GGYKTSGGLH
GVGSSVVNAL SSWLEVEITR DGAIYKQRFE NGGKPVTTLK KIGTAPKSKT GTKVTFMPDA
TIFSTTDFKY NTISERLNES AFLLKNVTLS LTDKRTDEGI EFHYENGVQD FVSYLNEDKE
TLTPVLYFEG EDNGFQVEVA LQYNDGFSDN ILSFVNNVRT KDGGTHETGL KSAITKVMND
YARKTGLLKE KDKNLEGSDY REGLAAVLSI LVPEEHLQFE GQTKDKLGSP LARPVVDGIV
ADKLTFFLME NGELASNLIR KAIKARDARE AARKARDESR NGKKNKKDKG LLSGKLTPAQ
SKNPAKNELY LVEGDSAGGS AKQGRDRKFQ AILPLRGKVI NTAKAKMADI LKNEEINTMI
YTIGAGVGAD FSIEDANYDK IIIMTDADTD GAHIQTLLLT FFYRYMRPLV EAGHVYIALP
PLYKMSKGKG KKEEVAYAWT DGELEELRKQ FGKGATLQRY KGLGEMNADQ LWETTMNPET
RTLIRVTIED LARAERRVNV LMGDKVEPRR KWIEDNVKFT LEEATVF
//
