ID Q8GI96_RHOFA Unreviewed; 421 AA.
AC Q8GI96;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 89.
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:BAC54054.1};
OS Rhodococcus fascians.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1828 {ECO:0000313|EMBL:BAC54054.1};
RN [1] {ECO:0000313|EMBL:BAC54054.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM10002 {ECO:0000313|EMBL:BAC54054.1};
RA Kasai H., Watanabe K., Harayama S.;
RT "Phylogenetic structure of suborder Corynebacterineae deduced from the gyrB
RT sequences.";
RL Submitted (DEC-2001) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB075563; BAC54054.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GI96; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
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 345..421
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 112..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAC54054.1"
FT NON_TER 421
FT /evidence="ECO:0000313|EMBL:BAC54054.1"
SQ SEQUENCE 421 AA; 46268 MW; 6970C6F9636649F4 CRC64;
SDSYAVSGGL HGVGISVVNA LSTKVELQIA RDGHRYKQTY DYAKPGPLET VGDTTETGTT
VRFWADGKIF ETLDYSFETV HRRLQEMAFL NKGLTINFTD ERVAATDATE EELGETAEAP
KTAEEEQADA ANAKPAKVRK RTYHYPDGLV DFVKHINRTK TAIHNSVVGF TGKGEGHEVE
IAMQWNAGYS ESVHTFANTI NTHEGGTHEE GFRTALTSTV NKYAIEKKLV KEKDVKLTGD
DIREGLAAVI SVRVGEPQFE GQTKTKLGNT EIRSFVQKAC NEHLSHWFES NPADAKTIIN
KAVSSAQARM AARKARELVR RKSATDIGGL PGKLADCRSN DPSKSEIYIV EGDSAGGSAK
SGRDSMFQAI LPLRGKIINV EKARIDRVLK NNEVQSIITA FGTGIHDEFD IAKLRYHKIV
L
//
