ID A0A1G6GQU9_9ACTN Unreviewed; 691 AA.
AC A0A1G6GQU9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=GA0111570_104248 {ECO:0000313|EMBL:SDB84115.1};
OS Raineyella antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Raineyella.
OX NCBI_TaxID=1577474 {ECO:0000313|EMBL:SDB84115.1, ECO:0000313|Proteomes:UP000199086};
RN [1] {ECO:0000313|EMBL:SDB84115.1, ECO:0000313|Proteomes:UP000199086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZ-22 {ECO:0000313|EMBL:SDB84115.1,
RC ECO:0000313|Proteomes:UP000199086};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMYF01000004; SDB84115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6GQU9; -.
DR STRING; 1577474.GA0111570_104248; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000199086; 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:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199086};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 465..579
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 691 AA; 75915 MW; 0BBBD0B60320E6CB CRC64;
MPSTSRPDEP RTYDARSLMV LEGLEAVRKR PAMYIGSTDT KGLMHCLWEI IDNAVDEALG
GFGESIEVVL GHDGSITVTD HARGIPVDTE PRTGLSGVEV VLTKLHAGGK FGSGSYGASG
GLHGVGASVV NALSTRLDVE VARNGARWTM SFQSGIPGTF AGDGPDAPFT PGGGLVKSGR
VPKGTTGTRI RYWPDRHIFL KDAKLSLADL HNRARQTSFL VPGLKIEVTD ERGEEPSTEV
FLHEGGISEF CEYLAQDQPL TDVIRLQGHD TFEETVPVLD EKGHMAPADV TRDLGVDIAL
RWGTGYDTLT KSFVNIIATP SGGTHVQGYD RGLVRAVGKA LEGTRLLKSG EEVSKEDILE
GLTTVVTVRL AEPQFEGQTK EVLGTPAVSR IVTRVVESEL GKYFSSPRRD DKQASRTVLE
KIVAASRTRV QARIHKEAQR RKNALESSTL PAKLKDCRST DVDKCELFIV EGDSALGTAQ
RARNAEYQAL LPIRGKILNV QKASITDMLK NLECASIIQV VGAGSGRSFD VDGIRYGKVI
FMADADSDGA HIRTLLATLF FRYMRPMIEH GHVYSAVPPL HRFELINPKK GQEKYVYTYS
DAEYERKLAE FTKKGIRFKE PQRYKGLGEM DADQLMETTM DPRHRTLRRL TLDDAEGAEG
VFEMLMGTEV APRKEFIIDG AYRLDQEHID I
//
