ID A0A257TGH0_9BACT Unreviewed; 696 AA.
AC A0A257TGH0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=B7X04_03365 {ECO:0000313|EMBL:OYV83636.1};
OS Parcubacteria group bacterium 21-54-25.
OC Bacteria.
OX NCBI_TaxID=1970248 {ECO:0000313|EMBL:OYV83636.1, ECO:0000313|Proteomes:UP000216537};
RN [1] {ECO:0000313|EMBL:OYV83636.1, ECO:0000313|Proteomes:UP000216537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-54-25 {ECO:0000313|EMBL:OYV83636.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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 -!- 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:OYV83636.1}.
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DR EMBL; NCBJ01000009; OYV83636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257TGH0; -.
DR Proteomes; UP000216537; 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:OYV83636.1};
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 453..567
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 604..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 76263 MW; 2D7F76D71A5B8737 CRC64;
MAKNDEKEAK KRGTTGAAKA YDASSIQVLE GLEPVRKRPG MYIGTTGPEG LHHLVWEIFD
NARDEAMAGR CDTIEVALLP DGYVRVADNG NGIPVGIHPK TKVSALETIM TTLHAGGKFD
NAAYKVSGGL HGVGASVVNA LSEHAKVVVH QDGGMHMQEY KIGKVLAKVK KIGTTKEHGT
IVLFKPDATI FKEGIVWNWD KIVNHLRQQA YLVKGTRISV IDAREADQKR AFDTDRIFVR
EHGFETPSTT FYFEGGLRSL VAFYNKRQAP IHKNIFYVDK EQDNVMVEVA FQYVDDITPR
ITAFANNTYN SEGGTHVTGF KTALTRSLNA YGRAANIIKE KDENFTGDDV LEGITAVISV
KLPEIQFEGQ TKGKLGSTEA QSAVATVFGS ALSSFLEENP DDARAIINKV LLALKARKAA
KAAKDSVLRK GALEGMTLPG KLADCQVKAP EEAELFIVEG DSAGGSSKQG RDRRTQAILP
LRGKILNVER ARIDRMLASV EIRALVVALG TAIGDVFDLT KLRYHKIIIA TDADVDGAHI
RTLLLTLFYR HFRPVVDGGF IYIAQPPLYK IARGKDVRYA YTDAEKDLIL KNMGVAPAEV
GGVAEEGDDA APEEETEETK VKKSTKANIQ RYKGLGEMNP SELWETTMDP TQRVLKRVTI
EDAQEADRIF DVLMGTDVAS RKSFIQSNAK TATLDV
//
