ID C9K141_RHOER Unreviewed; 411 AA.
AC C9K141;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:BAI44529.1};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=1833 {ECO:0000313|EMBL:BAI44529.1};
RN [1] {ECO:0000313|EMBL:BAI44529.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 11397 {ECO:0000313|EMBL:BAI44529.1}, and DSM 44522
RC {ECO:0000313|EMBL:BAI44530.1};
RX PubMed=19716527; DOI=10.1016/j.jbiosc.2009.04.010;
RA Teramoto K., Kitagawa W., Sato H., Torimura M., Tamura T., Tao H.;
RT "Phylogenetic analysis of Rhodococcus erythropolis based on the variation
RT of ribosomal proteins as observed by matrix-assisted laser desorption
RT ionization-mass spectrometry without using genome information.";
RL J. Biosci. Bioeng. 108:348-353(2009).
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; AB355712; BAI44529.1; -; Genomic_DNA.
DR EMBL; AB355713; BAI44530.1; -; Genomic_DNA.
DR AlphaFoldDB; C9K141; -.
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 335..411
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 106..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAI44529.1"
FT NON_TER 411
FT /evidence="ECO:0000313|EMBL:BAI44529.1"
SQ SEQUENCE 411 AA; 45037 MW; 856F9A2B6668AF11 CRC64;
GGLHGVGISV VNALSTRLDV DIKVDGYRWQ QTYTDSKPGE LVQGDPTKET GTTVSFWADP
EIFETTRYNF ETVARRLQEM AFLNKGLTIT LTDERAEVID DEAAEVGEAP KSAAEEAEEA
AQAAPRKSKT RIYHYPGGLE DYVRHINKSK TPIHNSVVGF TAKGTGHELE VAMQWNSGYS
ESVHTFANTI NTHEGGTHEE GFRAALTATV NKYALEKKLL KDKDPKLTGD DIREGLAAII
SVKVGEPQFE GQTKTKLGNT EVKSFVQKAC NEHLAHWFEA NPADAKTIVN KAVSSAQARV
AARKARELVR RKSATDLGGL PGKLADCRSN DPEKSEIYIV EGDSAGGSAK SGRDSMYQAI
LPLRGKIINV EKARIDRVLK NTEVQSIITA FGTGIHDEFD IAKLRYHKIV L
//
