ID Q6S9Y9_9BACI Unreviewed; 390 AA.
AC Q6S9Y9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 88.
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:AAS01481.1};
OS Bacillus sp. H-04.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=258057 {ECO:0000313|EMBL:AAS01481.1};
RN [1] {ECO:0000313|EMBL:AAS01481.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H-04 {ECO:0000313|EMBL:AAS01481.1};
RX PubMed=14967230; DOI=10.1016/j.mimet.2003.11.004;
RA La Duc M.T., Satomi M., Agata N., Venkateswaran K.;
RT "gyrB as a phylogenetic discriminator for members of the Bacillus
RT anthracis-cereus-thuringiensis group.";
RL J. Microbiol. Methods 56:383-394(2004).
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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; AY461765; AAS01481.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6S9Y9; -.
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: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; 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; PF01751; Toprim; 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 314..390
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAS01481.1"
FT NON_TER 390
FT /evidence="ECO:0000313|EMBL:AAS01481.1"
SQ SEQUENCE 390 AA; 43469 MW; 4FCC0E19A89CCF83 CRC64;
GGGYKVSGGL HGVGASVVNA LSTELEVFVH REGKIHYQKY ERGIPVADLK VIGDTDQTGT
ITRFKPDPEI FQETTVYDFD TLATRMRESA FLNRNIKLTI EDKRKHKQKK EFHYEGGIKS
YVEHLNRSKQ PIHEEPVYVE GSKDGIQVEV SLQYNEGYTN NIYSFTNNIH TYEGGTHEVG
FKTALTRVIN DYGRKNSILK DADSNLTGED VREGLTAIVS IKHPNPQFEG QTKTKLGNSE
ARTITESVFS EAFEKFLLEN PNVARKIVEK GTMAARARVA AKKARELTRR KSALEVSSLP
GKLADCSSKD PAISEIYIVE DDSAGGSAKQ GRDRHFQAIL PLKGKIINVE KARLDKILSN
DEVRTIITAI GTNIGGDFDI EKARYHKVII
//
