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Database: UniProt
Entry: D1L8K8_PSECA
LinkDB: D1L8K8_PSECA
Original site: D1L8K8_PSECA 
ID   D1L8K8_PSECA            Unreviewed;       169 AA.
AC   D1L8K8;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 35.
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:ACY64544.1};
OS   Pseudomonas cannabina.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=86840 {ECO:0000313|EMBL:ACY64544.1};
RN   [1] {ECO:0000313|EMBL:ACY64544.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CFBP 2341 {ECO:0000313|EMBL:ACY64544.1};
RX   PubMed=20227217; DOI=10.1016/j.syapm.2010.02.001;
RA   Bull C.T., Manceau C., Lydon J., Kong H., Vinatzer B.A.,
RA   Fischer-Le Saux M.;
RT   "Pseudomonas cannabina pv. cannabina pv. nov., and Pseudomonas cannabina
RT   pv. alisalensis (Cintas Koike and Bull, 2000) comb. nov., are members of
RT   the emended species Pseudomonas cannabina (ex Sutic & Dowson 1959) Gardan,
RT   Shafik, Belouin, Brosch, Grimont & Grimont 1999.";
RL   Syst. Appl. Microbiol. 33:105-115(2010).
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; GQ859258; ACY64544.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1L8K8; -.
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..168
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACY64544.1"
FT   NON_TER         169
FT                   /evidence="ECO:0000313|EMBL:ACY64544.1"
SQ   SEQUENCE   169 AA;  19374 MW;  9C31B3B14C9DDB52 CRC64;
     LLTVRRSGKI WEQTYVHGVP QEPMKIVGES DTTGTQIHFK PSADTFKNIH FSWDILAKRI
     RELSFLNSGV GIVLKDERSG KEELFKYEGG LRAFVEYLNT NKTPVNEVFH FNVQRDDGIG
     VEIALQWNDS FNENLLCFTN NIPQRDGGTH LVGFRSALTR NLNNYIEQE
//
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