ID C4TG79_9NOCA Unreviewed; 399 AA.
AC C4TG79;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, 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:BAH10761.1};
OS Nocardia niigatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=209249 {ECO:0000313|EMBL:BAH10761.1};
RN [1] {ECO:0000313|EMBL:BAH10761.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 0833 {ECO:0000313|EMBL:BAH10761.1};
RX PubMed=19833784; DOI=10.1099/jmm.0.011346-0;
RA Takeda K., Kang Y., Yazawa K., Gonoi T., Mikami Y.;
RT "Phylogenetic studies of Nocardia species based on gyrB gene analyses.";
RL J. Med. Microbiol. 59:165-171(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; AB450796; BAH10761.1; -; Genomic_DNA.
DR AlphaFoldDB; C4TG79; -.
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 323..399
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAH10761.1"
FT NON_TER 399
FT /evidence="ECO:0000313|EMBL:BAH10761.1"
SQ SEQUENCE 399 AA; 44158 MW; E81846B37487CE3B CRC64;
NALSTRLEAE VDYGGHHWTQ EYKDAKPGKL IQGEATKKTG TTIRFFPDPD IFETTTFSFE
TVARRLQEMA FLNKGLTITL TDQRIHEGDI TDEVVSETAE APKHLDENAP AAEPKVKTRT
YHYPGGLEDY VRHINRTKTP IHNSIVGFTG KGTGHEVEVA MQWNSGYSES VHTFANTINT
HEGGTHEEGF RAALTTVVNK YAKDKKLLKE KEGNLTGDDI REGLAAIVSV KIADPQFEGQ
TKTKLGNTEV KSFVQRTCNE HISHWFEANP ADAKTIVQKA VSSAQARVAA RKARELVRRK
SATDIGGLPG KLADCRSKDP SKSEIYIVEG DSAGGSAKSG RDSMYQAILP LRGKIINVEK
ARIDRVLKNT EVQSIITAFG TGIHDEFDIN KLRYHKIVL
//
