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Database: UniProt
Entry: Q8RSC0_9CAUL
LinkDB: Q8RSC0_9CAUL
Original site: Q8RSC0_9CAUL 
ID   Q8RSC0_9CAUL            Unreviewed;       393 AA.
AC   Q8RSC0;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 91.
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:BAB86989.1};
OS   Brevundimonas subvibrioides.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=74313 {ECO:0000313|EMBL:BAB86989.1};
RN   [1] {ECO:0000313|EMBL:BAB86989.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 15264 {ECO:0000313|EMBL:BAB86989.1};
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; AB014918; BAB86989.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RSC0; -.
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:BAB86989.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          321..393
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAB86989.1"
FT   NON_TER         393
FT                   /evidence="ECO:0000313|EMBL:BAB86989.1"
SQ   SEQUENCE   393 AA;  43585 MW;  4596812757EB75A0 CRC64;
     QNSYKVSGGL HGVGVSVVNA LSDWLKLVIF RNGQRHEMKF ERGDTVESLR VTGEAPMREN
     GKVLSGTQVT FYPSVTTFAH IDFDLKTLEH RLRELAFLNS GVVIKLQDHR GVEPFEEILH
     YEGGVEAFVR HLDKSKTPIL KDVIVIRGKR DNIEIDLALW WNDSYHETML CFTNNIPQRD
     GGTHLSAFRT SLTKVMGAYM ESSGALKKEK VAPTGEDARE GLTCVLSVKV PDPKFSSQTK
     DKLVSSEVRP AVEGLCTDGL NQWFEEHPVE AKAVVAKIIE AASAREAARK ARDLTRRKSA
     LDISSLPGKL ADCQERDPAK SELFIVEGDS AGGSAKQARN RENQAVLPLR GKILNVERAR
     FDRMLSSELI GTLILALGTG IGRDDFNADK LRY
//
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