ID A0A2Z4QCK1_9CAUD Unreviewed; 605 AA.
AC A0A2Z4QCK1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
OS Escherichia phage SF.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Tevenvirinae; Mosigvirus; Mosigvirus sf.
OX NCBI_TaxID=2234080 {ECO:0000313|EMBL:AWY07992.1, ECO:0000313|Proteomes:UP000251525};
RN [1] {ECO:0000313|EMBL:AWY07992.1, ECO:0000313|Proteomes:UP000251525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mohd Tawfid M.H.A., Mohamad Zawawi N.A., Mat Arip Y.;
RT "Genome Assembly Of Bacteriophage Specific To Escherichia coli 0157:H7.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AWY07992.1, ECO:0000313|Proteomes:UP000251525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Juharul Zaman S.F., Mat Arip Y., Mohamad Zawawi N.A.;
RT "Isolation and characterization of bacteriophage from raw sewage specific
RT for Eschericia coli 0157:H7.";
RL Submitted (MAY-2018) 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; MH359124; AWY07992.1; -; Genomic_DNA.
DR Proteomes; UP000251525; 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:AWY07992.1}.
FT DOMAIN 47..191
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 605 AA; 68116 MW; 403D48C7E7E7ABCD CRC64;
MIKNEIKVLS DVEHIKKRSG MYIGSSAKEA HERFLFGKYQ QVEYVPGLVK LIDEIIDNSV
DEAIRTSFKF ANKIDVQIKN NQVSVEDNGR GIPQGLVTDQ TGEQIPGPVA AWTIPKAGGN
FGDDSERKTG GMNGVGSSLT NIFSTLFTGI TSDGENEITV NCSNGMENKS WSSKKSKGKG
TKVIFTPDFS SFEEHNLSQI YLDITLDRLQ TLAVVYPDIK FTFNGKKVDG NFKRFAKQFG
EDNIIQENDK VSIAFTTSPD GFRHLTYVNN IHTKNGGHHV ECVMDDICEH LLPGIKKKYK
GIEVTKARVK ECLTMLMFIR DMSNMRFDSQ TKERLTSTYG DIRNHIQLDT KKIAQALLKN
EALIMPIVEA ALARKLAAEK AAETKAAKKA TKAKVHKHIK ANQCGKDADT TLFLTEGDSA
IGYLIDVRDR ELHGGFPLRG KVMNSWGMSY ADMMKNKELF DICAITGLIL GEKAENTNYR
NIAIMTDADH DGLGSIYPAL LAFFSNWPEL FEQGRIRFVK TPVIIAQIGK TQKWFYTVTE
YEEAKDTLPK HSIRYIKGLG SLEKSEYREM IQNPVYDVVK LPENWKELFE MLLGDDSELR
KEWMS
//
