ID E1CA96_RHOGO Unreviewed; 418 AA.
AC E1CA96;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:BAJ22195.1};
OS Rhodococcus globerulus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=33008 {ECO:0000313|EMBL:BAJ22195.1};
RN [1] {ECO:0000313|EMBL:BAJ22195.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 15076 {ECO:0000313|EMBL:BAJ22195.1}, ATCC 21505
RC {ECO:0000313|EMBL:BAJ22198.1}, and ATCC 21506
RC {ECO:0000313|EMBL:BAJ22199.1};
RA Kasai H., Harayama S.;
RT "Construction of the gyrB database for identification and classification of
RT High GC Gram positive bacteria.";
RL Submitted (MAY-1998) 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; AB014247; BAJ22195.1; -; Genomic_DNA.
DR EMBL; AB014250; BAJ22198.1; -; Genomic_DNA.
DR EMBL; AB014251; BAJ22199.1; -; Genomic_DNA.
DR AlphaFoldDB; E1CA96; -.
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, ECO:0000313|EMBL:BAJ22195.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 342..418
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAJ22195.1"
FT NON_TER 418
FT /evidence="ECO:0000313|EMBL:BAJ22195.1"
SQ SEQUENCE 418 AA; 45760 MW; D140E33703B6E4D2 CRC64;
SDSYAVSGGL HGVGISVVNA LSTRLDVDIK VDGYRWQQTY TDSKPGELVQ GDPTKETGTT
VSFWADPEIF ETTRYNFETV ARRLQEMAFL NKGLTITLTD ERAEVIDDEA AEVAEAPKSA
AEEAEEAAQA APRKSKTRIY HYPGGLEDYV RHINKSKTPI HNSVVGFTAK GTGHELEVAM
QWNSGYSESV HTFANTINTH EGGTHEEGFR AALTATVNKY ALEKKLLKDK DPKLTGDDIR
EGLAAIISVK VGEPQFEGQT KTKLGNTEVK SFVQKACNEH LAHWFEANPA DAKTIVNKAV
SSAQARVAAR KARELVRRKS ATDLGGLPGK LADCRSNDPE KSEIYIVEGD SAGGSAKSGR
DSMYQAILPL RGKIINVEKA RIDRVLKNTE VQSIITAFGT GIHDEFDIAK LRYHKIVL
//
