ID B6DPV0_9RHOB Unreviewed; 378 AA.
AC B6DPV0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:ACI25158.1};
OS Phaeobacter sp. M23-3.1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=559763 {ECO:0000313|EMBL:ACI25158.1};
RN [1] {ECO:0000313|EMBL:ACI25158.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M23-3.1 {ECO:0000313|EMBL:ACI25158.1};
RX PubMed=18952864; DOI=10.1128/AEM.01738-08;
RA Porsby C.H., Nielsen K.F., Gram L.;
RT "Phaeobacter and Ruegeria species of the Roseobacter clade colonize
RT separate niches in a Danish Turbot (Scophthalmus maximus)-rearing farm and
RT antagonize Vibrio anguillarum under different growth conditions.";
RL Appl. Environ. Microbiol. 74:7356-7364(2008).
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; FJ014965; ACI25158.1; -; Genomic_DNA.
DR AlphaFoldDB; B6DPV0; -.
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 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 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.
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 117..286
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACI25158.1"
FT NON_TER 378
FT /evidence="ECO:0000313|EMBL:ACI25158.1"
SQ SEQUENCE 378 AA; 42083 MW; C471DA4D659E3209 CRC64;
HSYKVSGGLH GVGVSVVNAL SDWLELRIWR DGKEHVARFE RGDTAEHLKV VGDCGDQTGT
EVRFLASTDT FSNLEYLFET LEKRLRELAF LNSGVRIILI DERPAERLEV ELFYEGGVKE
FVKYLDRSKS PVMEAPIYIT GDRDEIGVEV AMWWNDSYHE TVLPFTNNIP QRDGGTHVAG
FRGALTRTIN NYAQSSGIAK KEKVSFTGDD AREGLTCVLS VKVPDPKFSS QTKDKLVSSE
VRPVVESLVN EKLAEWFEEN PNQAKQIVGK IIEAALAREA ARKARELTRR KTAMDVNYLA
GKLKDCSEKD PSKTEVFLVE GDSAGGSAQT GRDRMTQAIL PLRGKILNVE RARFDRMLGS
QEIGNLVMAL GTGIGRDE
//
