ID Q8RSC9_9CAUL Unreviewed; 400 AA.
AC Q8RSC9;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 87.
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:BAB86980.1};
OS Brevundimonas bacteroides.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=74311 {ECO:0000313|EMBL:BAB86980.1};
RN [1] {ECO:0000313|EMBL:BAB86980.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 15254 {ECO:0000313|EMBL:BAB86980.1};
RA Hamada T.;
RT "Use of gyrB gene, pufL and pufM genes and 16S rRNA sequence analysis to
RT investigate phylogeny of photosynthetic bacteria.";
RL Submitted (JUN-1998) 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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; AB014909; BAB86980.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RSC9; -.
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; 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; 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; 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:BAB86980.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 323..400
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAB86980.1"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:BAB86980.1"
SQ SEQUENCE 400 AA; 44177 MW; 0310BD13B375584E CRC64;
SYKVSGGLHG VGVSVVNALS DWLKLVIFRN GKRHEMRFER GDTVESLRVT GDAPIRTDGA
KAGQTLSGTQ VTFYPSVTTF SHIDFDLKTL EHRLRELAFL NSGVVIKLAD HRHAEPFEEI
LHYEGGVEAF VRHLDKSKSP ILKDVIVIRG KKEGVELDLA LWWNDSYHET MLCFTNNIPQ
RDGGTHLSAF RASLTRVMGA YMESSGALKK EKVAPTGEDA REGLTCVLSV KVPDPKFSSQ
TKDKLVSSEV RPAVEALCSE GLSTWFEEHP VEAKLITAKI IEAASAREAA RKARDLTRRK
SAMDISSLPG KLADCQERDP AKSELFIVEG DSAGGSAKQA RNRENQAVLP LRGKILNVER
ARFDRMLSSD LIGTLILALG TGIGRDDFNA DKLRYHKIIL
//
