ID C7AUL0_9PSED Unreviewed; 362 AA.
AC C7AUL0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN Name=gyrB {ECO:0000313|EMBL:ACT64288.1};
OS Pseudomonas sp. R14-24-07.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=658634 {ECO:0000313|EMBL:ACT64288.1};
RN [1] {ECO:0000313|EMBL:ACT64288.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R14-24-07 {ECO:0000313|EMBL:ACT64288.1};
RX PubMed=20008172; DOI=10.1128/AEM.02009-09;
RA Mavrodi D.V., Peever T.L., Mavrodi O.V., Parejko J.A., Raaijmakers J.M.,
RA Lemanceau P., Mazurier S., Heide L., Blankenfeldt W., Weller D.M.,
RA Thomashow L.S.;
RT "Diversity and evolution of the phenazine biosynthesis pathway.";
RL Appl. Environ. Microbiol. 76:866-879(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; FJ652710; ACT64288.1; -; Genomic_DNA.
DR AlphaFoldDB; C7AUL0; -.
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 CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 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; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
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 Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 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 301..362
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACT64288.1"
FT NON_TER 362
FT /evidence="ECO:0000313|EMBL:ACT64288.1"
SQ SEQUENCE 362 AA; 39853 MW; F51C69A7C66304BB CRC64;
GVGVSVVNAL SEELILTVRR SGKIWEQTYV HGVPQEPMKI VGDSETTGTQ IHFKPSAETF
KNIHFSWDIL AKRIRELSFL NSGVGIVLKD ERSGKEELFK YEGGLRAFVE YLNTNKTAVN
QVFHFNIQRE DGIGVEIALQ WNDSFNENLL CFTNNIPQRD GGTHLVGFRS ALTRNLNTYI
EAEGLAKKHK VATTGDDARE GLTAIISVKV PDPKFSSQTK DKLVSSEVKT AVEQEMGKYF
SDFLLENPNE AKLVVGKMID AARAREAARK AREMTRRKGA LDIAGLPGKL ADCQEKDPAL
SELYLVEGDS AGGSAKQGRN RRTQAILPLK GKILNVEKAR FDKMISSQEV GTLITALGCG
IG
//
