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Database: UniProt
Entry: A8R799_9BACI
LinkDB: A8R799_9BACI
Original site: A8R799_9BACI 
ID   A8R799_9BACI            Unreviewed;       328 AA.
AC   A8R799;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   08-NOV-2023, entry version 62.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE   Flags: Fragment;
GN   Name=gyrB {ECO:0000313|EMBL:BAF92823.1};
OS   Virgibacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=361280 {ECO:0000313|EMBL:BAF92823.1};
RN   [1] {ECO:0000313|EMBL:BAF92823.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 21758 {ECO:0000313|EMBL:BAF92823.1};
RA   Hua N.P., Naganuma T.;
RT   "Isolation and characterization of functional genes in halophilic
RT   bacteria.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAF92823.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 21758 {ECO:0000313|EMBL:BAF92823.1};
RA   Hua N., Naganuma T.;
RL   Submitted (NOV-2007) 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};
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DR   EMBL; AB367308; BAF92823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8R799; -.
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:0006265; P:DNA topological change; IEA:InterPro.
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; 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   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   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
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.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT   DOMAIN          113..283
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
FT   REGION          38..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAF92823.1"
FT   NON_TER         328
FT                   /evidence="ECO:0000313|EMBL:BAF92823.1"
SQ   SEQUENCE   328 AA;  36695 MW;  42EE2B2CB244B599 CRC64;
     YKVSGGLHGV GASVVNALSE WMEITSFREG QKYFQRFEKG GKPAGPPVNQ GTSRKTGTMV
     HFKPDPAIFS TTTFDEEIIA ERLREAAFLL KGLRITLHDM RSEDRMEFCY PEGLKAFVDY
     LNEDKETLHD VVFFEGEHEQ IEVDFAFQFN DGFAESMLSF VNHVRTKDGG THESGARSAT
     TRVFNDYARK NGLIKEKEKN LEGTDIREGL TAIVSVRIPE EKLQFEGQTK AKLGTSEARS
     AVDSIVSEKL TYFLEENPDV ATSLVKKALK AKEAREAARK ARDESRNGKK KRRKDTLLSG
     KLTPAQSRNP KRNELYLVEG DSAGGSAK
//
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