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Database: UniProt
Entry: A0A0L0LKY1_9BACT
LinkDB: A0A0L0LKY1_9BACT
Original site: A0A0L0LKY1_9BACT 
ID   A0A0L0LKY1_9BACT        Unreviewed;       693 AA.
AC   A0A0L0LKY1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   Name=gyrB {ECO:0000313|EMBL:KND51067.1};
GN   ORFNames=AB202_01490 {ECO:0000313|EMBL:KND51067.1};
OS   Parcubacteria bacterium C7867-007.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1659201 {ECO:0000313|EMBL:KND51067.1, ECO:0000313|Proteomes:UP000037534};
RN   [1] {ECO:0000313|EMBL:KND51067.1, ECO:0000313|Proteomes:UP000037534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7867-007 {ECO:0000313|EMBL:KND51067.1};
RX   PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA   Nelson W.C., Stegen J.C.;
RT   "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT   symbiotic lifestyle.";
RL   Front. Microbiol. 6:713-713(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:KND51067.1}.
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DR   EMBL; LFCQ01000003; KND51067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0LKY1; -.
DR   STRING; 1659201.AB202_01490; -.
DR   PATRIC; fig|1659201.3.peg.291; -.
DR   Proteomes; UP000037534; Unassembled WGS sequence.
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; 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   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:KND51067.1};
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          450..564
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          596..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  75902 MW;  9BE4C809F24DF01F CRC64;
     MAKEGDKTTK KAAKSGDYDA SSITVLEGLD PVRKRPGMYI GTTGPDGLHH LIWEIFDNSR
     DEAMGGFADD IEITLLPGGY VRVVDNGRGI PVGIHPKTKV SALETIMTTL HAGGKFGGED
     SGYKVSGGLH GVGASVVNAL SEHAKVIVHK EGATHMQEYK IGKAMAKVKQ IGKTKHQGSV
     VFFKPDVSIF KDGINWNWDR IVGHIRQQAY LVKGTRMCVI DAREAGMVDS EEVAYVRELG
     LEVPTMTFFF ENGLRSLVAF TNKHQAPAHK NIFYVDATEN EVMVEVAFQY TDDISPRLLA
     FANNTYNPEH GTHVTGFKTA LTRTLNTYAR TAGILKESEE NFTGDDVLEG ITAVVSVKMP
     EIQFEGQTKG KLGSVEAQGA VATVFGGALN TFLEENPDDG RAIVNKVLLA LKARKAAKAA
     KDSVLRKGAL EGMTLPGKLA DCQTKDPAES EIFIVEGDSA GGSAKTGRDR RTQAILPLRG
     KILNIERARL DKMLASEQIK NLVVAMGTAI GDIFDISKLR YHKIIIATDA DVDGAHIRTL
     LLTLFYRHFR PIIDGGFIYI AQPPLYKIKR GKEVMYAYTD EEKFRILGPD AEMAVEASDE
     AQGTEEDGDE TPEEELTTKK GMKVSIQRYK GLGEMNPEEL WETTMNPSNR VLKRVTIEDA
     TDADRIFDIL MGSDVPSRKS FIQSNAKLAN LDV
//
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