ID A0A3S0JB34_9BACT Unreviewed; 648 AA.
AC A0A3S0JB34;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=EJV47_23195 {ECO:0000313|EMBL:RTQ46062.1};
OS Hymenobacter gummosus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1776032 {ECO:0000313|EMBL:RTQ46062.1, ECO:0000313|Proteomes:UP000282184};
RN [1] {ECO:0000313|EMBL:RTQ46062.1, ECO:0000313|Proteomes:UP000282184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52166 {ECO:0000313|EMBL:RTQ46062.1,
RC ECO:0000313|Proteomes:UP000282184};
RA Nie L.;
RT "Hymenobacter gummosus sp. nov., isolated from a spring.";
RL Submitted (DEC-2018) 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:RTQ46062.1}.
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DR EMBL; RXOF01000017; RTQ46062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0JB34; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000282184; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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; 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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RTQ46062.1}.
FT DOMAIN 421..531
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 73390 MW; F250527636069F19 CRC64;
MAEQLSLESA TTAPADHGYN EDSIRSLDWR EHIRLRPGMY IGKLGDGSSP DDGIYILVKE
VIDNSIDEHM MGYGRTIEVK ITEQRVTVRD YGRGIPLGKV VDVVSKINTG GKYDSKVFQK
SVGLNGVGTK AVNALSTNFV VQSVRDGMMK SAEFQNGKLI SDPKPIKTSQ RNGTMMAFEP
DPSIFRNFRF IPDFLESQFW NYAYLNAGLT INFNGQKYHS ENGLRDLLER KTDPEAIRYP
VIHLKGTDIE MALTHGNDYG EEYYSFVNGQ YTTQGGTHLA AFREGIVKTV REHYGKEYDA
TDIRASIVGA IAIRVQEPVF ESQTKTKLGS IVMEPEGALT VRNFVVDFVK EHLDNYLHKN
PDTKEALKKR IEQSERERKD MAGVKKLANQ RAKKASLHNR KLRDCRFHFD EGKAPEKEAL
TTLFITEGDS ASGSITKSRN VELEAVFSLR GKPLNCFGMK KKIVYENEEL NLLQHALNIE
EGLEGLRYNR VVIATDADVD GMHIRLLLLT FFLQFFPDLV RNGHVYILET PLFRVRNKKQ
TIYCYDEKEK QAAIKKLGRN PEITRFKGLG EISPDEFGKF IGDNIRLEPV ILQSDRSIQK
LLTYYMGKNT PARQEFIIDN LRMEKDLVTS DTLPASETIV PAAEAELV
//