ID C4TG58_9NOCA Unreviewed; 399 AA.
AC C4TG58;
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:BAH10740.1};
OS Nocardia beijingensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=95162 {ECO:0000313|EMBL:BAH10740.1};
RN [1] {ECO:0000313|EMBL:BAH10740.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 10174 {ECO:0000313|EMBL:BAH10740.1};
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; AB450772; BAH10740.1; -; Genomic_DNA.
DR AlphaFoldDB; C4TG58; -.
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:BAH10740.1"
FT NON_TER 399
FT /evidence="ECO:0000313|EMBL:BAH10740.1"
SQ SEQUENCE 399 AA; 44130 MW; 237CC69F0FF6BE46 CRC64;
NALSTRLQAE VDTGGYHWTQ EYKDAKPGKL IQGEPTKRTG TTIRFWPDPE IFETTTFNFE
TVARRLQEMA FLNKGLTIVL TDERVSDTEI TDEVVSETAE APKHAEDAAA PAEHKVKSRT
YHYPGGLEDF VRHINRTKQP IHNSVVAFTG KGTGHELEVA MQWNSGYSES VHTFANTINT
HEGGTHEEGF RAALTTVVNK YAKDKKLIKE KDGNLTGDDI REGLAAIVSV KVGEPQFEGQ
TKTKLGNTEV KSFVQRTCNE HLTHWFEANP ADAKTIVNKA VSSAQARVAA RKARELVRRK
SATDLGGLPG KLADCRSKDP SKSEIYIVEG DSAGGSAKSG RDSMYQAILP LRGKIINVEK
ARIDKVLKNN EVQSIITAFG TGIHDEFDIS KLRYHKIVL
//
