ID D5MP48_9SPHN Unreviewed; 321 AA.
AC D5MP48;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:BAJ07454.1};
OS Porphyrobacter sp. MBIC3897.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=82667 {ECO:0000313|EMBL:BAJ07454.1};
RN [1] {ECO:0000313|EMBL:BAJ07454.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MBIC3897 {ECO:0000313|EMBL:BAJ07454.1};
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; AB020305; BAJ07454.1; -; Genomic_DNA.
DR AlphaFoldDB; D5MP48; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR000565; Topo_IIA_B.
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; PR01159; DNAGYRASEB.
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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAJ07454.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 3..162
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAJ07454.1"
FT NON_TER 321
FT /evidence="ECO:0000313|EMBL:BAJ07454.1"
SQ SEQUENCE 321 AA; 35515 MW; FAA2E7AB93EEC172 CRC64;
DTDDGSGLHH MVFEVSDNAI DEALAGHCDL VLIELNPDGS VSVEDNGRGI PTGMHSEEGV
SAAEVIMTQL HAGGKFENTS DDNAYKVSGG LHGVGVSVVN ALSEWLELTI WREGKEHWMR
FEHGDAVAPL EVKGDAPRSD RNADANGFKK GTRVTFKASH DTFKNVTEFD FEKLEHRYRE
LAFLNSGVRI KLRDKRHEDV VEHDLYYEGG IAAFVKYLDR NKQALIPEPI AVSAEKDGIG
IDVALEWNDS YYENVLAFTN NIPQRDGGTH LSAFRAALTR TLNNYAERSG MLKKEKVSLS
GEDMREGLTA IVSVKLPDPK F
//
