ID A0A1J4V3V5_9BACT Unreviewed; 699 AA.
AC A0A1J4V3V5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=AUJ44_03670 {ECO:0000313|EMBL:OIO31844.1};
OS Candidatus Nomurabacteria bacterium CG1_02_47_685.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1805282 {ECO:0000313|EMBL:OIO31844.1, ECO:0000313|Proteomes:UP000183206};
RN [1] {ECO:0000313|EMBL:OIO31844.1, ECO:0000313|Proteomes:UP000183206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_47_685 {ECO:0000313|EMBL:OIO31844.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO31844.1}.
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DR EMBL; MNVO01000055; OIO31844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4V3V5; -.
DR STRING; 1805282.AUJ44_03670; -.
DR Proteomes; UP000183206; 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 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: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:OIO31844.1};
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 448..562
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 600..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..618
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 77449 MW; CA57252AD0CE5F1F CRC64;
MAKKATNGHH YQADDIQVLE GLEPVRKRPG MYIGSTGVEG LHHLVWEIFD NGRDEAMGGF
ADHIEVAFLP ENRVRVVDNG RGIPVDVHKK TKVSALETVM TTLHAGGKFG GDGYAKATGG
LHGVGASVVN ALSSYMKVEV HKDGGYYVQE YNKGKKKANV KKVGKTDFSG TIVTFDADPE
IFQEIKYNWK ETTSHLRQQA YLVRGMWITV IDARECKEEK TLMRVAGDNG TTYLTNLGID
IPSESYYFEG GLVSLVKFYN RGLKPVHKNV FYVEKEIDGV FVEIAVQYAD DISARDFAFA
NNTYNAEGGM HVTGFRTALT RKLNDYARKN NFLKDADENL TADDVREGIT AVISVKLKEI
QFEGQTKGKL GSVEARGAVE KVFGEGFLNF LEEHPDDARS IINKVILAFR ARKAAKAAKD
SVLRKGALEG VTLPGKLADC QTSKKDEAEL FVVEGDSAGG SAKMGRDRRT QAILPLWGKI
LNSEKSRLDK VVTARGVREL IIAIGTAVGD TFDISKLRYG KIIIATDADV DGAHIRTLLL
TLFYRYLKPV VEAGNVFIAM PPLYKIKKGK EVTYVYSEED KIKVLGKDAV ALEEAVLTDE
SVTEENEQTE EDLNEEGEEI ETTKTKKQKI SIQRYKGLGE MNPEELWETT MNPLSRVLKK
VTINDAQDAN RAFDVLMGVD VMSRKLFIQA NAKKATIDV
//
