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Database: UniProt
Entry: O05326_PSESP
LinkDB: O05326_PSESP
Original site: O05326_PSESP 
ID   O05326_PSESP            Unreviewed;       200 AA.
AC   O05326;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 95.
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:BAA19521.1};
OS   Pseudomonas sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306 {ECO:0000313|EMBL:BAA19521.1};
RN   [1] {ECO:0000313|EMBL:BAA19521.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E6 {ECO:0000313|EMBL:BAA19521.1};
RX   PubMed=9546154;
RA   Watanabe K., Yamamoto S., Hino S., Harayama S.;
RT   "Population dynamics of phenol-degrading bacteria in activated sludge
RT   determined by gyrB-targeted quantitative PCR.";
RL   Appl. Environ. Microbiol. 64:1203-1209(1998).
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; AB002237; BAA19521.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05326; -.
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:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR000565; Topo_IIA_B.
DR   PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAA19521.1"
FT   NON_TER         200
FT                   /evidence="ECO:0000313|EMBL:BAA19521.1"
SQ   SEQUENCE   200 AA;  21950 MW;  DC8CD5F525CFF72B CRC64;
     HAGGKFNQNS YKVSGGLHGV GVSCVNALSK WLRLTVRRDG KVHQIEFAKG FVQNRLLETV
     DGFEVSPMKV TGATEKRGTE VHFLPDTEIF QQNHEFHYEI LAKRLRELSF LNNGVRIRLK
     DERSGKEDDF SGAGGVKGFV EFINGTKKVL HPTAFHATGT RPAESYGGIP GTEIGVEVAM
     QWNDATTSRC SASPTTSRSA
//
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