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Database: UniProt
Entry: Q19RB6_9BACL
LinkDB: Q19RB6_9BACL
Original site: Q19RB6_9BACL 
ID   Q19RB6_9BACL            Unreviewed;       493 AA.
AC   Q19RB6;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 83.
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:ABF82591.1};
OS   Exiguobacterium sp. Indian Stream.
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=383718 {ECO:0000313|EMBL:ABF82591.1};
RN   [1] {ECO:0000313|EMBL:ABF82591.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Indian Stream {ECO:0000313|EMBL:ABF82591.1};
RX   PubMed=17156079; DOI=10.1111/j.1574-6941.2006.00233.x;
RA   Rodrigues D.F., Tiedje J.M.;
RT   "Multi-locus real-time PCR for quantitation of bacteria in the environment
RT   reveals Exiguobacterium to be prevalent in permafrost.";
RL   FEMS Microbiol. Ecol. 59:489-499(2007).
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; DQ490866; ABF82591.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q19RB6; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; 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, ECO:0000313|EMBL:ABF82591.1};
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          396..493
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABF82591.1"
FT   NON_TER         493
FT                   /evidence="ECO:0000313|EMBL:ABF82591.1"
SQ   SEQUENCE   493 AA;  54260 MW;  08F67AD7D7C3BC4A CRC64;
     GMYIGSTASK GLHHLVWEIV DNSIDEALAG YCDTIKVTIE PGNSILVEDN GRGIPVDIQE
     KMGRPAVEVI LTVLHAGGKF GGGGYKVSGG LHGVGASVVN ALSTKLEVFV KRNEKLYYQA
     YHRGVPVADL EIIGTSEETG TMIRFFPDDE IFQETLEYDY DLLATRLREL AFLNKGLTIE
     ITDDRADEPI TRSFHYEGGI KSYVEHLNRS KEVVHEEPVY VHGNRDGIEV EVALQYNDGF
     AANIYSFTNN IPTHEGGTHE TGFKTALTRV INDYAKKFGL MKEADGTLSG EDVREGMTAI
     VSIKHPNPQF EGQTKTKLGN SDARTATDTL FSSAFEQFMM ENPTSARAIV EKGMMASRAR
     MAAKRARELT RRKGVLEVSS LPGKLADCSS RDATISEIYI VEGDSAGGSA KSGRDRHFQA
     ILPIRGKILN VEKARLDKIL GSNEIRTIIT ALGTSIGSEF NIEKARYHKV IIMTDADVDG
     AHIRTLLLTF FYR
//
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