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Database: UniProt
Entry: Q8VUR6_9RHOB
LinkDB: Q8VUR6_9RHOB
Original site: Q8VUR6_9RHOB 
ID   Q8VUR6_9RHOB            Unreviewed;       307 AA.
AC   Q8VUR6;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 77.
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:BAB83771.1};
OS   Phaeovulum veldkampii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Phaeovulum.
OX   NCBI_TaxID=33049 {ECO:0000313|EMBL:BAB83771.1};
RN   [1] {ECO:0000313|EMBL:BAB83771.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 11550T {ECO:0000313|EMBL:BAB83771.1};
RA   Uchino Y., Hamada T., Sugiyama J., Yokota A.;
RT   "Proposal of Pseudorhodobacter ferrugineus gen. nov. comb. nov. from non-
RT   photosynthetic marine Agrobacterium ferrugineum.";
RL   Submitted (JUL-2001) 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   -!- 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; AB065366; BAB83771.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VUR6; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; cd16928; HATPase_GyrB-like; 1.
DR   CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR   Gene3D; 3.30.230.10; -; 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; IPR013506; Topo_IIA_bsu_dom2.
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   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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          3..149
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAB83771.1"
FT   NON_TER         307
FT                   /evidence="ECO:0000313|EMBL:BAB83771.1"
SQ   SEQUENCE   307 AA;  33695 MW;  5A4B71BFEFF96383 CRC64;
     DTDDGSGLHH MVYEVVDNGI DEALAGHANY VHVKIHADSS VSVRDNGRGI PTDIHAGEGV
     SAAEVIMTQL HAGGKFDQNS YKVSGGLHGV GVSVVNALSE WLELRIWRNG KEHYAKFVHG
     DTVEPLRVVG DAAPGEKGTE VRFLASTQTF SNLDYVFKTL ENRLRELAFL NSGVRIILED
     ERPVEPLRTE LMYEGGVREF VRYLDRSKAS VMAEPIFITG ERGGIGVEVA MWWNDSYHET
     VLPFTNNIPQ RDGGTHLAGF RGALTRTINA YAQSSGIAKK EKVDFTGDDA REGLTCVLSV
     KVPDPKF
//
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