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Database: UniProt
Entry: V9W2Q3_9BACL
LinkDB: V9W2Q3_9BACL
Original site: V9W2Q3_9BACL 
ID   V9W2Q3_9BACL            Unreviewed;       657 AA.
AC   V9W2Q3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   Name=parE {ECO:0000313|EMBL:AHD05271.1};
GN   ORFNames=ERIC2_c14460 {ECO:0000313|EMBL:AHD05271.1};
OS   Paenibacillus larvae subsp. larvae DSM 25430.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD05271.1, ECO:0000313|Proteomes:UP000029431};
RN   [1] {ECO:0000313|EMBL:AHD05271.1, ECO:0000313|Proteomes:UP000029431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD05271.1,
RC   ECO:0000313|Proteomes:UP000029431};
RX   PubMed=24599066;
RA   Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA   Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT   "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT   Mechanisms of Paenibacillus larvae.";
RL   PLoS ONE 9:E90914-E90914(2014).
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; CP003355; AHD05271.1; -; Genomic_DNA.
DR   RefSeq; WP_023482724.1; NZ_CP019652.1.
DR   AlphaFoldDB; V9W2Q3; -.
DR   KEGG; plv:ERIC2_c14460; -.
DR   PATRIC; fig|697284.3.peg.1380; -.
DR   eggNOG; COG0187; Bacteria.
DR   HOGENOM; CLU_006146_1_2_9; -.
DR   Proteomes; UP000029431; Chromosome.
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:AHD05271.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029431}.
FT   DOMAIN          440..554
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          403..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   657 AA;  73014 MW;  AF34BF1360A0069F CRC64;
     MAEQLDLYDN QTTLSSDYDA DAIQVLEGLT AVRKRPGMYI GSTSSSGLHH LVWEIVDNAV
     DEHLAKHCSK IDVTIHKEGS ITVYDNGRGI PTGMHKMGIP TPQVVFTILH AGGKFGGGGY
     KKSGGLHGVG ASVTNALSEW LEVEIFRDGQ IYKQRFEYWV DEAGKEHVGE PVTSLEIIGK
     TSKSGTKITF KPDVRVFKGG IQFNYDTLAE RLQELAFLNS GLEIFLKDER TGSEDHFLYS
     GGASEFVRFL NEGKDVLHDV IHFEAEKDDI EVEIAMQYNI GYTETLVSFV NSIPTRGGGT
     HETGFKTAFT RVMNEYARKN SILKEKDKNL EGTDLREGLM AVINIKMSDV EFVGQTKDQL
     GSATARSAVD AVVSEKMAVF LEENPQVAQM MLKKAVQSAK AREAARKARE EVRSGKKGRS
     ESSNLNGKLT PAQSKDVTRN ELFIVEGDSA GGSAKQGRDS KYQAILPLKG KPMNPEKAKL
     LDILKNDEYK AIISAIGAGV GSEFELSETN YNKIIIMTDA DTDGAHIQVL LLTFFYRYMK
     PLVDAGKVYI AQPPLYKISK KSGKRTSVHY AWTDEELSKL TQKAGKNFEL QRYKGLGEMN
     PEQLWETTMN PGTRILLQVQ IEDAAKAERR VSTLMGDKVD PRKRWIIDNV DFTEFEE
//
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