ID A0A151B4D3_9CLOT Unreviewed; 650 AA.
AC A0A151B4D3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=parE {ECO:0000313|EMBL:KYH34768.1};
GN ORFNames=CLTEP_12330 {ECO:0000313|EMBL:KYH34768.1};
OS Clostridium tepidiprofundi DSM 19306.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121338 {ECO:0000313|EMBL:KYH34768.1, ECO:0000313|Proteomes:UP000075531};
RN [1] {ECO:0000313|EMBL:KYH34768.1, ECO:0000313|Proteomes:UP000075531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19306 {ECO:0000313|EMBL:KYH34768.1,
RC ECO:0000313|Proteomes:UP000075531};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium tepidiprofundi DSM 19306.";
RL Submitted (FEB-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYH34768.1}.
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DR EMBL; LTBA01000010; KYH34768.1; -; Genomic_DNA.
DR RefSeq; WP_066824081.1; NZ_LTBA01000010.1.
DR AlphaFoldDB; A0A151B4D3; -.
DR STRING; 1121338.CLTEP_12330; -.
DR PATRIC; fig|1121338.3.peg.1269; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000075531; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
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; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF12; DNA TOPOISOMERASE 4 SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 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.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KYH34768.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000075531}.
FT DOMAIN 438..552
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 650 AA; 73857 MW; 80E9CBBEB60DBC12 CRC64;
MEKDNQNHSY KVTDLMSLEK LEPVRVRPGM YIGSTGSKGL HHCIWEILDN SIDEITNGYG
DKVEIILNKD NSVTIIDNGR GIPTGIHPIK KISGVQMVYT ELHTGGKFNN KNYKTSGGLH
GVGAAVVNAL SEWLEVEIMQ NGNIYKQRFE YGYDKELKKD MPGTPCGDLK VIGKTNKTGT
KVTFKPDKRV FSAVDFKFDI IDERLQELAF QNKGVKLVLI DDRKEEKVIK EYHSERGLLD
FIDYLNESKT VLHKDAILFM GEREVKGINL SSEVCIQFTD TSTEYIASYV NNIPTTEAGT
HETGFKTGMT RAFKEWAKKL NLIKEKDKEF DGNDLREGMT AILKVKISNP IFEGQTKTKL
GNNEAYTMMN ELTYTKLCEW IEDNKEVATT IINNAIMAAK RREKIKKIND AERKKIGKGT
APLAGKIAVC TLKKPELLEF FVVEGDSAGG SAKQARDRRF QTIMPSKGKI LNTEKQKLEN
VIASEELKLF NTAIGTGILD NYDEKDLKYN KVIILSDADV DGYHIRTLWM TYIYRYMRPL
ITNGHLYLAQ PPLYKVYKKS KKGDKILYAY SDEELQSAKK EVGKGAQIQR FKGLGEMNPE
QLWETTLNPE TRTLYQVTIE DAAKAEKMIS LLMGDVVEPR RNYLYKYAEF
//
