ID Q7Y5D4_BPR69 Unreviewed; 606 AA.
AC Q7Y5D4;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=60plus39 {ECO:0000313|EMBL:AAP75906.1};
OS Escherichia phage RB69 (Bacteriophage RB69).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Tevenvirinae; Mosigvirus; Mosigvirus RB69.
OX NCBI_TaxID=12353 {ECO:0000313|EMBL:AAP75906.1, ECO:0000313|Proteomes:UP000000876};
OH NCBI_TaxID=562; Escherichia coli.
RN [1] {ECO:0000313|EMBL:AAP75906.1, ECO:0000313|Proteomes:UP000000876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11114936; DOI=10.1128/JB.183.1.358-366.2001;
RA Tetart F., Desplats C., Kutateladze M., Monod C., Ackermann H.W.,
RA Krisch H.M.;
RT "Phylogeny of the major head and tail genes of the wide-ranging T4-type
RT bacteriophages.";
RL J. Bacteriol. 183:358-366(2001).
RN [2] {ECO:0000313|EMBL:AAP75906.1, ECO:0000313|Proteomes:UP000000876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Petrov V., Nolan J., Chin D., Letarov A., Krisch H.M., Karam J.D.;
RT "Enterobacteria phage RB69 complete genome.";
RL Submitted (MAY-2003) 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 family.
CC {ECO:0000256|ARBA:ARBA00011080}.
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DR EMBL; AY303349; AAP75906.1; -; Genomic_DNA.
DR RefSeq; NP_861694.1; NC_004928.1.
DR GeneID; 1494120; -.
DR KEGG; vg:1494120; -.
DR OrthoDB; 931at10239; -.
DR Proteomes; UP000000876; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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; 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; 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 PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 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.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AAP75906.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000876}.
FT DOMAIN 48..192
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 606 AA; 68117 MW; 9565BA4EC5881E95 CRC64;
MIKNEIRVLS DVEPLLRNRM VCILVLSAKE AHEPFLVGNY SPVEMFLGLV KLIDEIIDNS
VDEAIRTSFK FANKIDVQIK NNQVSVEDNG RGIPQGLVTD QTGEQIPGPV AAWTIPKAGG
NFGDDSERKT GGMNGVGSSL TNIFSTLFTG ITSDGENEIT VNCSNGMENK SWSSKKSKGK
GTKVIFTPDF TSFEEHNLSQ IYLDITLDRL QTLAVVYPDI KFTFNGKKVD GNFKRFAKQF
GEDNIIQEND KVSIAFTTSP DGFRHLTYVN NIHTKNGGHH VECVMDDICE HLLPGIKKKY
KGIEVTKARV KECLTMLMFI RDMSNMRFDS QTKERLTSTY GDIRNHIQLD AKKIAQALLK
NEALIMPIVE AALARKLAAE KAAETKAAKK ATKAKVHKHI KANQCGKDAD TTLFLTEGDS
AIGYLIDVRD RELHGGFPLR GKVMNSWGMS YADMMKNKEL FDICAITGLI LGEKAENTNY
RNIAIMTDAD HDGLGSIYPA LLAFFSNWPE LFEQGRIRFV KTPVIIAQIG KTQKWFYTVA
EYEEAKDTLP KHSIRYIKGL GSLEKSEYRK MIQNPVYDVV KLPENWKELF EMLMGDDSEL
RKEWMS
//
