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Database: UniProt
Entry: I1X1K2_9BRAD
LinkDB: I1X1K2_9BRAD
Original site: I1X1K2_9BRAD 
ID   I1X1K2_9BRAD            Unreviewed;       260 AA.
AC   I1X1K2;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
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:AFI73566.1};
OS   Bradyrhizobium sp. cp16.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1178969 {ECO:0000313|EMBL:AFI73566.1};
RN   [1] {ECO:0000313|EMBL:AFI73566.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cp16 {ECO:0000313|EMBL:AFI73566.1};
RX   PubMed=22539163; DOI=10.1099/mic.0.059238-0;
RA   Koppell J.H., Parker M.A.;
RT   "Phylogenetic clustering of Bradyrhizobium symbionts on legumes indigenous
RT   to North America.";
RL   Microbiology 158:2050-2059(2012).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708}.
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DR   EMBL; JQ693230; AFI73566.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1X1K2; -.
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; cd16928; HATPase_GyrB-like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
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; IPR013506; Topo_IIA_bsu_dom2.
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; PF02518; HATPase_c; 1.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
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.
PE   3: Inferred from homology;
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          1..133
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFI73566.1"
FT   NON_TER         260
FT                   /evidence="ECO:0000313|EMBL:AFI73566.1"
SQ   SEQUENCE   260 AA;  28260 MW;  EE8A72E8CB3478D6 CRC64;
     VDNAIDEALA GHASRVLVTL NADNSVTVYD DGRGIPVGIH KGEGVSAAEV IMTQLHAGGK
     FDQNSYKVSG GLHGVGVSVV NALSSKLGLR IWRDDKEHYI EFAHGDAVAP LKVVGDAPGK
     RGTEVTFLAS PETFKNIEYD FATLEHRLRE LAFLNSGVHI VLSDMRHAVE KREEMHYSGG
     VEEFVKYLDR NKKAIVPAPI MVRAEANGIG VEAALWWNDS YHENVLCFTN NIPQRDGGTH
     LAGFRGALTR QVNGYAEANA
//
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