ID A0A3M9MQY1_9BACT Unreviewed; 623 AA.
AC A0A3M9MQY1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=EFA69_15970 {ECO:0000313|EMBL:RNI27615.1};
OS Rufibacter immobilis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1348778 {ECO:0000313|EMBL:RNI27615.1, ECO:0000313|Proteomes:UP000271010};
RN [1] {ECO:0000313|EMBL:RNI27615.1, ECO:0000313|Proteomes:UP000271010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCC P1 {ECO:0000313|EMBL:RNI27615.1,
RC ECO:0000313|Proteomes:UP000271010};
RA Yang Y.;
RT "Rufibacter latericius sp. nov., isolated from water in Baiyang Lake.";
RL Submitted (NOV-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:RNI27615.1}.
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DR EMBL; RJJE01000017; RNI27615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9MQY1; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000271010; 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 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; 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:RNI27615.1}.
FT DOMAIN 410..520
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 623 AA; 71321 MW; 4A80AE918B073B4B CRC64;
MAELTDVSYN EDSIRSLDWR EHIRLRPGMY IGKLGDGSSP DDGIYILVKE VIDNSIDEHM
MGHGRTIEVK ISDHKVVVRD YGRGIPLGKV IDCVSKINTG GKYDSRAFQK SVGLNGVGTK
AVNALSTHFR IQSVREGQTK VAEFVRGELV NDEPLQETNQ RNGTTTTFVP DDTIFKNYHF
IPEFLENQIW NYVYLNAGLT IHFNGQKYYS ENGLKDLLSR KIDEESMRYP IIHLKGEDIE
FALTHGNDYG EEYYSFVNGQ YTTQGGTHLA AFREAVVKTV REFYKKDYDA TDIRGSIVGA
IAIRVQEPVF ESQTKTKLGS INVAHDGPTV RNFVNDFVKE HLDNYLHKNP TVAEALKKRI
EQSERERKDM AGIKKLANQR AKKANLHNKK LRDCRFHLGE GKEQEKEALT TLFITEGDSA
SGSITKSRNV ELEAVFSLRG KPLNCFGLKK KIVYENEEFN LLQHALNIEE GLEGLRYNRV
VIATDADVDG MHIRLLMMTF FLQFFPDLVK NGHLYILETP LFRVRNKKET IYCYDEQEKQ
NAMRKLGKNP EITRFKGLGE ISPEEFGKFI GENIRLEPVI LGKTEQNLQK ILSYYMGKNT
PERQQFIIEN LKIEKDIVEE VYA
//