GenomeNet

Database: UniProt
Entry: D0G7R8_PSECI
LinkDB: D0G7R8_PSECI
Original site: D0G7R8_PSECI 
ID   D0G7R8_PSECI            Unreviewed;       175 AA.
AC   D0G7R8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 39.
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:BAI48971.1};
OS   Pseudomonas cichorii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=36746 {ECO:0000313|EMBL:BAI48971.1};
RN   [1] {ECO:0000313|EMBL:BAI48971.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MAFF 301374 {ECO:0000313|EMBL:BAI48976.1}, MAFF 302152
RC   {ECO:0000313|EMBL:BAI48980.1}, and MAFF 730054
RC   {ECO:0000313|EMBL:BAI48971.1};
RA   Tanaka M., Wali U., Koyanagi M., Kajihara S., Hikida Y., Ohnishi K.,
RA   Kiba A., Hikichi Y.;
RT   "Involvement of aldehyde dehydrogenase gene in virulence of Pseudomonas
RT   cichorii on eggplant and its genetic diversity among Pseudomonas spp.";
RL   Submitted (NOV-2009) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB530820; BAI48971.1; -; Genomic_DNA.
DR   EMBL; AB530825; BAI48976.1; -; Genomic_DNA.
DR   EMBL; AB530829; BAI48980.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0G7R8; -.
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   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; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR000565; Topo_IIA_B.
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   PRINTS; PR01159; DNAGYRASEB.
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   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          90..174
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAI48971.1"
FT   NON_TER         175
FT                   /evidence="ECO:0000313|EMBL:BAI48971.1"
SQ   SEQUENCE   175 AA;  20016 MW;  DB5D56C7B502E2BB CRC64;
     QLTVRRSGKI WEQTYVHGVP QEPMKIVGES DSTGTQIHFK PSADTFKNIH FSWDILAKRI
     RELSFLNSGV GIFLKDERSG KEELFKYEGG LRAFVEYLNT NKTAVNQVFH FNVQRDDGVG
     VEIALQWNDS FNENLLCFTN NIPQRDGGTH LVGFRSALTR NLNNYIEQEG LAKKH
//
DBGET integrated database retrieval system