ID A0A0Q8ZVR6_9FLAO Unreviewed; 622 AA.
AC A0A0Q8ZVR6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=ASE21_09470 {ECO:0000313|EMBL:KRD09943.1};
OS Flavobacterium sp. Root901.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736605 {ECO:0000313|EMBL:KRD09943.1, ECO:0000313|Proteomes:UP000051400};
RN [1] {ECO:0000313|EMBL:KRD09943.1, ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|EMBL:KRD09943.1,
RC ECO:0000313|Proteomes:UP000051400};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KRD09943.1}.
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DR EMBL; LMJB01000006; KRD09943.1; -; Genomic_DNA.
DR RefSeq; WP_057122478.1; NZ_LMJB01000006.1.
DR AlphaFoldDB; A0A0Q8ZVR6; -.
DR STRING; 1736605.ASE21_09470; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000051400; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR CDD; cd01030; TOPRIM_TopoIIA_like; 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 PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 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 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KRD09943.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 412..518
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 622 AA; 71052 MW; 1BC61D12C5E7C2C1 CRC64;
MLEQNQYNED NIRSLDWKEH IRMRPGMYIG KLGDGSSPDD GIYILLKEVL DNCIDEFVMG
AGKTIEVTIK DKTVSVRDYG RGIPLGKVVD VVSKMNTGGK YDSKAFQKSV GLNGVGTKAV
NALSNYFRVE SVRDDKQKAA EFSAGNLVQE EDVIDTTKRK GTKVTFTPDE TIFKNYKFRL
EYVIKMVKNY CYLNNGLTII FNGEKYYSEN GLRDLLEETI NEDDLEYPII HLKDHDIEVA
LTHSKTQYSE EYHSFVNGQN TTQGGTHLAA YREAVVKTIR EFYNKNFEAS DVRKSIVSAI
SIKVMEPVFE SQTKTKLGST DMGSDDGTPA VSVRTFVNDF IKTKLDNYLH KNPPTAEALL
RKILQAERER KELSGIRKLA TDRAKKANLH NKKLRDCRAH LPDTKNPRNL ESTLFITEGD
SASGSITKSR DVNTQAVFSL RGKPLNSYGM TKKIVYENEE FNLLQAALDI EDGLEKLRYN
NIVIATDADV DGMHIRLLLI TFFLQFFPEL IKEGHLYILQ TPLFRVRNKK ETIYCYSEEE
RKEAIEKLKP KPEITRFKGL GEISPDEFKN FIGDTIRLDP VMMDKHTSIE QLLSFYMGKN
TPDRQDFIIK NLKVEIDELE EV
//
