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Database: UniProt
Entry: A0A1H9J3W3_9ACTN
LinkDB: A0A1H9J3W3_9ACTN
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ID   A0A1H9J3W3_9ACTN        Unreviewed;       708 AA.
AC   A0A1H9J3W3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-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=SAMN05421756_10682 {ECO:0000313|EMBL:SEQ81456.1};
OS   Microlunatus flavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=1036181 {ECO:0000313|EMBL:SEQ81456.1, ECO:0000313|Proteomes:UP000198504};
RN   [1] {ECO:0000313|Proteomes:UP000198504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6856 {ECO:0000313|Proteomes:UP000198504};
RA   Varghese N., Submissions S.;
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; FOFA01000006; SEQ81456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9J3W3; -.
DR   STRING; 1036181.SAMN05421756_10682; -.
DR   Proteomes; UP000198504; 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   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          482..596
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   708 AA;  76344 MW;  84BB2D85ABA1E87E CRC64;
     MTATPVASTR RGAARNAGPE LESRDYEARH LLVLEGLEAV RKRPAMYIGS TDTRGLMHCL
     WEIIDNSVDE ALGGFGRAIE VTLRDDGGIT VTDQGRGIPV DKEPRTGLSG VEVVFTKLHA
     GGKFGAGSYN ATGGLHGVGS SVVNALSARL DVEVDRDGAT WAMSFRRGVP GTFDGAGPTA
     PFTPGGPLTK VGRVAKGRTG TRVTYWPDRQ IFLAEAGLSI EDLHNRARQT SFLVPGLAIT
     VTDARDGAAA ADGPAVEVFK HEGGIGEFCE YLAPDAAVTD VLRLQGTGQF TETVPMLDDA
     GHMEPTDVDR ELEVDVAVRW GTGYDTTVRS YVNIIATPKG GTHVAGFERA LVRAVTGALA
     PTRLLKTGEE VVKDDVLEGL TAVVTVRLAE PQFEGQTKEV LGTPAVSRLV AKVVETELGT
     FLESKSGVGK QQARSVLEKV VSASRARVAA RQQRENQRRK NALESSSLPT KLVDCRAIGD
     RSELFIVEGN SALGTAKEAR SSEFQALLPI RGKILNTQKA STGDMLKNVE CASIIQVVGA
     GSGRTFDLDA ARYGKIIFMA DADSDGAHIR CLLATLFFRY MRPLVDAGRV FTAVPPLHRF
     ELTNPKKGQE KFIYTYTDAE YQRTAAELTK RGVRFKEPQR YKGLGEMDAD QLAQTTMDPR
     HRTLRRMTVD DGLIAETTFE MLMGNDVAPR KTFIIDGAYA LDASAIDV
//
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