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Database: UniProt
Entry: A0A1H4KUW6_9BACL
LinkDB: A0A1H4KUW6_9BACL
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ID   A0A1H4KUW6_9BACL        Unreviewed;       657 AA.
AC   A0A1H4KUW6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=SAMN05443246_1335 {ECO:0000313|EMBL:SEB62016.1};
OS   Paenibacillus sp. GP183.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1882751 {ECO:0000313|EMBL:SEB62016.1, ECO:0000313|Proteomes:UP000199177};
RN   [1] {ECO:0000313|EMBL:SEB62016.1, ECO:0000313|Proteomes:UP000199177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP183 {ECO:0000313|EMBL:SEB62016.1,
RC   ECO:0000313|Proteomes:UP000199177};
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};
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DR   EMBL; FNSW01000001; SEB62016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4KUW6; -.
DR   STRING; 1882751.SAMN05443246_1335; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000199177; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IPR005740; ParE_type2.
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   NCBIfam; TIGR01058; parE_Gpos; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF12; DNA TOPOISOMERASE 4 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   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SEB62016.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199177}.
FT   DOMAIN          440..554
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          402..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   657 AA;  72655 MW;  5E88B7AB4DE7F5EF CRC64;
     MAEQLDIFTN QGALDANYGA DEIQVLEGLV AVRKRPGMYI GSTSTSGLHH LIWEIVDNAV
     DEHLAKYCTK IGVIIHKDQS ITVTDNGRGI PTGMHKIGIP TPQVVFTILH AGGKFGGAGY
     KKSGGLHGVG ASVTNALSEW LEVEIYRDGK IHKQRFEYWV DADGKEHVGE PVGGLEILGN
     TNRTGTKVTF KPDRRVFQSG ITINYDSLSE RLQEIAFLNS GLQVSLKDER TDNQETFQYE
     GGAKQFVEFL NEDKTVLHSV IHFASEKDDI EVEVALQYND GYTETLASFV NSIPTRGGGT
     HETGFKTAYT RVMNEYARKA GLLKEKDKNL DGTDLREGMM AVINIKMGEV EFVGQTKDQL
     GSASARGAVD AIVTDKMSVF LEENPQVGQM MLKKAVQASK AREAARKARE EIRSGKKGRS
     ESSNLNGKLT PAQSKDLMSN ELFIVEGDSA GGSAKQGRDS KHQAILPLKG KPMNPEKAKL
     LDVMKNDEYK AIIAAIGAGV GSEFDLDECN YGKIIIMTDA DTDGAHIQVL LLTFFYRYMK
     QLIDGGKVYI AQPPLFKLTK KAGKNTAVRY AWTDDQLAAM TKEFGKQSEL QRYKGLGEMN
     PDQLWETTMN PESRTLLQVQ IEDAAKAERR VSTLMGDKVD PRKRWIIENV DFTEYVE
//
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