ID Q6IZU0_PSESX Unreviewed; 160 AA.
AC Q6IZU0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 71.
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:AAT10880.1};
OS Pseudomonas syringae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=317 {ECO:0000313|EMBL:AAT10880.1};
RN [1] {ECO:0000313|EMBL:AAT10880.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cit7 {ECO:0000313|EMBL:AAT10880.1};
RX PubMed=15066790; DOI=10.1128/AEM.70.4.1999-2012.2004;
RA Sarkar S.F., Guttman D.S.;
RT "Evolution of the core genome of Pseudomonas syringae, a highly clonal,
RT endemic plant pathogen.";
RL Appl. Environ. Microbiol. 70:1999-2012(2004).
RN [2] {ECO:0000313|EMBL:BAN05375.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EOC-1 {ECO:0000313|EMBL:BAN05375.1};
RA Sato T.;
RT "Taxonomic Studies on a Bacterium Responsible for Yellow Halo Spot Disease
RT of Cucumber.";
RL Submitted (MAR-2013) 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; AY610800; AAT10880.1; -; Genomic_DNA.
DR EMBL; AB809669; BAN05375.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6IZU0; -.
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..160
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAT10880.1"
FT NON_TER 160
FT /evidence="ECO:0000313|EMBL:AAT10880.1"
SQ SEQUENCE 160 AA; 18283 MW; 80C199F15A8249C7 CRC64;
LLTVRRSGKI WEQTYVHGVP QEPMKIVGES DTTGTQIHFK PSAETFKNIH FSWDILAKRI
RELSFLNSGV GIVLKDERSG KEELFKYEGG LRAFVEYLNT NKTPVNQVFH FNIQRDDGIG
VEIALQWNDS FNENLLCFTN NIPQRDGGTH LVGFRSALTR
//