ID A0A0R1XFJ1_9LACO Unreviewed; 675 AA.
AC A0A0R1XFJ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=FC91_GL001837 {ECO:0000313|EMBL:KRM28373.1};
OS Schleiferilactobacillus harbinensis DSM 16991.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM28373.1, ECO:0000313|Proteomes:UP000050949};
RN [1] {ECO:0000313|EMBL:KRM28373.1, ECO:0000313|Proteomes:UP000050949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM28373.1,
RC ECO:0000313|Proteomes:UP000050949};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM28373.1}.
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DR EMBL; AZFW01000032; KRM28373.1; -; Genomic_DNA.
DR RefSeq; WP_027827412.1; NZ_AZFW01000032.1.
DR AlphaFoldDB; A0A0R1XFJ1; -.
DR GeneID; 78509035; -.
DR PATRIC; fig|1122147.4.peg.1905; -.
DR eggNOG; COG0187; Bacteria.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000050949; 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:UP000050949};
KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00939}.
FT DOMAIN 425..539
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 391..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..409
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 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 459
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 511
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT SITE 627
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
SQ SEQUENCE 675 AA; 75199 MW; 39956914BDC2005D CRC64;
MPQSASDYND SSIQVLHGLE AVRKRPGMYI GSTDSHGLHH LVYEIVDNAV DEALAGFGKD
INVQILPDGG ISVQDHGRGM PTGMHPSGKP TIEVILTVLH AGGKFTQNTY KTSGGLHGVG
ASVVNALSTK LTVRVVRDGK AYYEEFKDGG HPVGTLKMVG RVKEPNGTTI QFWPDKSVFT
TTKFNYDTLA ERLRESAFLL KGISISLTDE RPGQEQQDVF KYDDGIKSFV KYLNEDKDTM
GDIMDFTGKD KGIEVEFAGQ YNDGYSENII SFVNNVRTGD GGSHEVGLKG GYTKAFNDYA
HKVNLLKERD KNLEGSDVRE GLSGVLSVRI PEELLQFEGQ TKGKLGTPEA RPVVENVIYE
QLSFYLLENG EFAQELVRKA LKARDAREAA RKARTDMRNG KKRKKTEGIL SGKLTPAQSK
NAKKNELYLV EGDSAGGSAK QGRDRRFQAI LPLRGKVLNT QKAKLADIFK NEEINTMIYT
IGAGVGPEFN IKDSNYDKII IMTDADTDGA HIQILLLTFF YRYMRPLIDA GKIYIALPPL
YKLQKGSGAK TRIEYAWTEH ELTDDIQKMG KGYSLQRFKG LGEMNADQLW ETTMNPETRT
LIRVKITDAA LAERRVTTLM GDRVEPRRQW IERNVRFNMA DEGSLLDNTV MDGEEAVAHE
KEDEKILTAL KEHHA
//
