ID A0A2K0X264_9BIFI Unreviewed; 688 AA.
AC A0A2K0X264;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=BFS08_04540 {ECO:0000313|EMBL:PNP88623.1};
OS Gardnerella sp. KA00735.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=1973156 {ECO:0000313|EMBL:PNP88623.1, ECO:0000313|Proteomes:UP000236541};
RN [1] {ECO:0000313|Proteomes:UP000236541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00735 {ECO:0000313|Proteomes:UP000236541};
RA Bumgarner R.E., Fredricks D.N., Srinivasan S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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:PNP88623.1}.
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DR EMBL; NBMV01000002; PNP88623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0X264; -.
DR Proteomes; UP000236541; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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 InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR011557; GyrB.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
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; TIGR01059; gyrB; 1.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE 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|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PNP88623.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 466..580
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 76254 MW; C9E54DB1473B4674 CRC64;
MEDDSIEKIN DEHKLDDAQL DDSLAPEHYD ASDLRVLEGL EAVRIRPGMY IGSTGPRGLH
HLVYEIVDNS VDEALAGYAS HIEVTILPDN AIRVVDDGRG IPVDEVPGEG VSGVETVMTK
LHAGGKFGGG GYAVSGGLHG VGISVVNALS TRVDIEVRRQ GFHWTQTYIN QHPTAPLAKG
EPMAEGESTG TSVTFWPDAA IFETTIYDFE TLRSRFQQMA FLNKGLKISL TDLRKPDEAG
DEVAGDAESS NEDKHRSVSY RYEHGIKDYV DYLVKSRKAV PVEPDVIDFE AEDLEIGISA
EIAMQWTVAY SEAVHTFANT ISTTEGGTHE EGFRAALTTL VNRYAREKNI LKEKDTNLSG
DDVREGLTAV VSVKLTTPQF EGQTKTKLGN SEAKTFVQRV MTEKLGDWFD AHPSEAKNII
QKSIEASRAR LAAKKARENT RRKSIFETAG MPDKLKDCQS NNPEECELFI VEGDSAGGSA
IQGRDPITQA ILPLRGKILN TERASIDRMM KSETIESLIT AVGGGYGEDF DLSKVRYHKV
IIMADADVDG AHIATLNLTL FFRYMRPMIT AGYVYVAMPP LYRLKWSKGA HDFVYTDAER
DRVLAEGKAA GRQLPKGEGI QRYKGLGEMS YQELWETTMD PDHRILKQIH IEDAARADET
FSMLMGDEVE PRRLFIQRNA HDARFIDA
//
