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Database: UniProt
Entry: Q6IZU0_PSESX
LinkDB: Q6IZU0_PSESX
Original site: Q6IZU0_PSESX 
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
//
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