ID A0A0G1N689_9BACT Unreviewed; 651 AA.
AC A0A0G1N689;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 40.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=UX22_C0002G0004 {ECO:0000313|EMBL:KKU15812.1};
OS Candidatus Jorgensenbacteria bacterium GW2011_GWA2_45_9.
OC Bacteria; Candidatus Jorgensenbacteria.
OX NCBI_TaxID=1618663 {ECO:0000313|EMBL:KKU15812.1, ECO:0000313|Proteomes:UP000034727};
RN [1] {ECO:0000313|EMBL:KKU15812.1, ECO:0000313|Proteomes:UP000034727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU15812.1}.
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DR EMBL; LCLJ01000002; KKU15812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1N689; -.
DR PATRIC; fig|1618663.3.peg.68; -.
DR Proteomes; UP000034727; 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:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
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 CDD; cd03366; TOPRIM_TopoIIA_GyrB; 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 InterPro; IPR034160; TOPRIM_GyrB.
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};
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 434..548
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 651 AA; 72021 MW; DB0B1405F6858738 CRC64;
MKKTEKKEEK NNGVVSYDAK DIYVLEGLDP VRKRPGMYIG TTSADGLHHL IWEVVDNSID
EAMGGYAKNI RMELLKDNKV AVTDDGRGIP VDIHKQTKKS ALETVLTTLH AGGKFGGESY
KVSGGLHGVG VSVVNALSTW LRAEVNRDGN VYAQEYKRGK PMTPVKKIGK SRGAGTGTKI
TFSPDPEIFS KIEFDFNKIV GHLRHQAYLT KGVNIEIIDE RGEYPVFYGF CFDGGLRSFI
RALTAGQSGE KIQDNVFYVQ KESEGIEVEA AFTYTSEMES QEMSFANNIY TMDGGMHLTG
FRTALTRTLN DYARQSGVIK DVNDNLTGDD VREGLVALVS VRIREPQFEG QTKARLGNAE
ARTAVDAVVS EALKEFLERY SADAKSIIGK NLLAAKARKA AKAAKDTVLR KGMLEGMTLP
GKLADCSSRN PAESELFIVE GDSAGGSCKQ GRDRRTQAVL PLRGKILNVE KSRIDKILLN
KEIRSLVVAL GTAISDKFDL SKLRYHKVVI MSDADVDGEH ICTLLLTLFF RYFPQVIENG
HLFIAQPPLF RIQKGKEVHY VYSDAEREKA VKIFGGAGES VNVQRYKGLG EMNPDQLWET
TMNPGNRMLK KVTVENSIEA SRLFDILMGE EVEPRKNFIQ AHAAAAKNID I
//
