ID A6N6C8_9BACT Unreviewed; 418 AA.
AC A6N6C8;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:ABR20221.1};
GN Synonyms=gyrb {ECO:0000313|EMBL:ABQ66047.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:ABR20221.1};
RN [1] {ECO:0000313|EMBL:ABQ66047.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17957354; DOI=10.1007/s00203-007-0298-6;
RA Yin H., Cao L., Qiu G., Wang D., Kellogg L., Zhou J., Liu X., Dai Z.,
RA Ding J., Liu X.;
RT "Molecular diversity of 16S rRNA and gyrB genes in copper mines.";
RL Arch. Microbiol. 189:101-110(2008).
RN [2] {ECO:0000313|EMBL:ABR20221.1}
RP NUCLEOTIDE SEQUENCE.
RA Yin H., Cao L., Xie M., Chen Q., Qiu G., Zhou J., Wu L., Wang D., Liu X.;
RT "Bacterial diversity based on 16S rRNA and gyrB genes at Yinshan mine,
RT China.";
RL Syst. Appl. Microbiol. 31:302-311(2008).
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};
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DR EMBL; EF409884; ABQ66047.1; -; Genomic_DNA.
DR EMBL; EF613070; ABR20221.1; -; Genomic_DNA.
DR AlphaFoldDB; A6N6C8; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
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; 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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 326..418
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABR20221.1"
FT NON_TER 418
FT /evidence="ECO:0000313|EMBL:ABR20221.1"
SQ SEQUENCE 418 AA; 46452 MW; 3B250B5D04640589 CRC64;
EVIMTVLHAG GKFDSNSYKI SGGLHGVGVS VVNALSTWLK LTIYRDGKRH FMEFREGDAV
APLAVVGDSP KRGTEIHFLP SPLTFGTIEF HYDILARRLR ELSFLNNGVS ILLKDLRHGQ
EENFSFNGGV RGFVEYLNRT RTVLHPTVFH SVGEKEGITV EVAMQWNESY QENVLCFTNN
IPQRDGGTHL TALRAAMTRT LNHFIEENEL ARKAKVETTG DDMREGLTCV LSVKVPDPKF
SSQTKEKLVS SEVRPAVEEV VSDQMRSFLL EKPAEARIIV GKIIEAARAR EAARKARELT
RRKGALDGLG LPGKLADCQE KDPAQCEIYL VEGDSAGGSA KQGRDRRFQA ILPLKGKILN
VERARFDKLV SSQEIVTLIT ALGTGIGKDE YSPEKVRYHR IIIMTDADVD GSHIRTLL
//
