ID A0A1G9E7S2_9ACTN Unreviewed; 688 AA.
AC A0A1G9E7S2;
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=SAMN05421869_11866 {ECO:0000313|EMBL:SDK72171.1};
OS Nonomuraea jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=633440 {ECO:0000313|EMBL:SDK72171.1, ECO:0000313|Proteomes:UP000199202};
RN [1] {ECO:0000313|EMBL:SDK72171.1, ECO:0000313|Proteomes:UP000199202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDK72171.1,
RC ECO:0000313|Proteomes:UP000199202};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNDJ01000018; SDK72171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9E7S2; -.
DR STRING; 633440.SAMN05421869_11866; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000199202; 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:UP000199202};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 461..575
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 688 AA; 75856 MW; 47A36BD892DD4AFB CRC64;
MTLVEAGYTA RHLSVLEGLE AVRKRPGMYI GSTDSRGLMH CLWEIVDNGV DEALAGHCDR
IEVELHADGS IEVRDNGRGI PVDIEPKTGL AGVELVYTKL HAGGKFGGGS YGASGGLHGV
GASVVNALSA RVDVEVDRDG LVHEISFRRG VAGVFEGEGP TAKFKKKSGL RIGGKLPKRV
TGTRVRFWAD KQIFLPDAEV SLDEIHVRLR QTAFLVPGLT LAVFDSRQEE RVEEEFHFDG
GISEFTEFLA RDEAVCDVLR LQGMGHFHET VPVLDDQGHM TPTEVQRELT VDVAVRWGKG
YESTVRSFVN VIATPKGGTH LTGFERGLVR TINELLRETR LLKNGDDPVN KEDISEGLTG
VVTVRVPEPQ FEGQTKEVLG TSAATRIVSH VVSRELKELF ANPPRGYKQP LRAVLEKIVA
AAKARIAARE HRDNQRRKSA LENSALPAKL VDCRSDDVDR SELFIVEGDS ALGTAKLARD
SEFQALLPIR GKILNVQKAS VSDMLKNAEC AAIIQVVGAG SGRSFDIEAA RYGKVILMAD
ADVDGAHIRC LLLTLFHRYM RPMVEAGRVF AAVPPLHRIE LTNPGRGKDK YIYCYSDAEL
HKVLRDLERR GKRWKDPVQR YKGLGEMDAD QLAETTMDPR HRILRRVRIE DAEGAEGIFN
LLMGSDVAPR REFIVNSAAE VDRDHIDA
//
