ID A1EGN0_9BACT Unreviewed; 421 AA.
AC A1EGN0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, 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:ABL67970.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:ABL67970.1};
RN [1] {ECO:0000313|EMBL:ABL67970.1}
RP NUCLEOTIDE SEQUENCE.
RA Wan M., Zhang F., Yin H., Yang Y., Qiu G.;
RT "GyrB sequences of Acidithiobacillus ferrooxidans and clones in acid mine
RT drainage.";
RL Submitted (NOV-2006) 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; EF124814; ABL67970.1; -; Genomic_DNA.
DR AlphaFoldDB; A1EGN0; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 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 329..421
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL67970.1"
FT NON_TER 421
FT /evidence="ECO:0000313|EMBL:ABL67970.1"
SQ SEQUENCE 421 AA; 46197 MW; 1537FCCA490EFBAF CRC64;
EVIMTVLHAG GKFEQNAYKV SGGLHGVGVS VVNALSEWLE LRIWRSGQEH KMRFHDGEPQ
APLALVGPAN GKRGTEVTFL PSPRTFTKTE FDYATLEHRL RELAFLNSGV TIRLSDQRGV
EKKESKLHYE GGLEAFVRYL DRAKNGLIPA PLLITGERDG ITVEAALSWN DSYHESMLCF
TNNIPQRDGG THLAGFRAAL TRVVIKYAED SGIAKKEKVQ ISGDDCREGL TCVLSVKVPD
PKFSSQTKDK LVSSEVRPVV ESVAADQIGR WFEEHPGEAK TVVGKVVEAA AAREAARKAR
ELTRRKGAFD SASLPGKLAD CQERDPAKCE LFIVEGDSAG GSAKQARNRN NQAVLPLRGK
ILNVERARFD KMLSSDAIAT LITALGTSVG PEEFNPEKLR YHKIIIMTDA DVDGSHIRTL
L
//
