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Database: UniProt
Entry: D5MNY8_RHOPL
LinkDB: D5MNY8_RHOPL
Original site: D5MNY8_RHOPL 
ID   D5MNY8_RHOPL            Unreviewed;       304 AA.
AC   D5MNY8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:BAJ07394.1};
OS   Rhodopseudomonas palustris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=1076 {ECO:0000313|EMBL:BAJ07394.1};
RN   [1] {ECO:0000313|EMBL:BAJ07394.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SGD3 {ECO:0000313|EMBL:BAJ07394.1}, and SGL12
RC   {ECO:0000313|EMBL:BAJ07396.1};
RA   Hamada T., Harayama S.;
RT   "Identification and Classification of Beta Proteobacteria.";
RL   Submitted (NOV-1998) 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   -!- 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; AB020245; BAJ07394.1; -; Genomic_DNA.
DR   EMBL; AB020247; BAJ07396.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5MNY8; -.
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   CDD; cd00822; TopoII_Trans_DNA_gyrase; 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, ECO:0000313|EMBL:BAJ07394.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          3..148
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAJ07394.1"
FT   NON_TER         304
FT                   /evidence="ECO:0000313|EMBL:BAJ07394.1"
SQ   SEQUENCE   304 AA;  33187 MW;  C594CDB0D2D1787A CRC64;
     DTDDGSGLHH MVYEVVDNAI DEALAGHATR VEVILNADGS VTVRDDGRGI PVDIHKGEGI
     SAAEVIMTQL HAGGKFDQNS YKVSGGLHGV GVSVVNALSS RLLLRVWRDG KEHFIEFAHG
     EAVAPLAVVG DAGGKRGTEV TFYASAETFT NVEYDFATLE HRLRELAFLN SGVNILLSDL
     RHGIEKREEM RYEGGVVEFV KYLDRNKKAI VPMPITILAE MNGITVECAL WWNDSYHENV
     LCFTNNIPQR DGGTHLAGFR GALTRQVNGY ADVIAKKEKI TLTGDDCREG LTAVLSVKVP
     DPKF
//
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