ID A0A2A7ML71_9CLOT Unreviewed; 649 AA.
AC A0A2A7ML71;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=CQ394_11335 {ECO:0000313|EMBL:PEG32253.1};
OS Clostridium neonatale.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG32253.1, ECO:0000313|Proteomes:UP000220840};
RN [1] {ECO:0000313|EMBL:PEG32253.1, ECO:0000313|Proteomes:UP000220840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG32253.1,
RC ECO:0000313|Proteomes:UP000220840};
RA Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT "Effective Description of Clostridium neonatale sp. nov. linked to
RT necrotizing enterocolitis in neonates and a clarification of species
RT assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT Rainey 2016.";
RL Submitted (OCT-2017) 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:PEG32253.1}.
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DR EMBL; PDCJ01000001; PEG32253.1; -; Genomic_DNA.
DR RefSeq; WP_058296399.1; NZ_PDCJ01000001.1.
DR AlphaFoldDB; A0A2A7ML71; -.
DR STRING; 137838.GCA_001458595_03756; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000220840; 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:PEG32253.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000220840}.
FT DOMAIN 437..551
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 649 AA; 73770 MW; FC6B116D13C90E5B CRC64;
MELKKMDSYD VTDLRSLEKL EPVRVRPGMY IGSTGNKGLH HCIWEIIDNS IDEISNGFGD
KVTITINEDK SITILDNGRG IPTGIHPTKK KSGVEMVFTE LHTGGKFDNK NYKTSGGLHG
VGAAVVNALS KFLEVEVYQN GKVYRQRFEY AYDKELKRDM PGTPVTDLEI VGKSIKTGTK
VTFKPDNEIF STTDFKFDII DERLQELAFQ NKGIRLELID KRKGHENSKE YYSENGLLDF
INYLNESKTP IHEKPIIFDG ERLVNNIQMY GEVCMQFTDS TTEYIASYVN NIPTTEAGTH
ETGFKTGMTR AFKEWAKKLG LVKEKDKEFE GDDLREGMTA IVRIKITNPV FEGQTKTKLG
NNEAYTMMND LVYTKFGEWI EDNKPLATTI INNALEAAKR RDKIKKINEA EKKKIGKGTA
PLAGKVAVCT LKDRNVNEFI VVEGDSAGGS AKQARDRRFQ TIMPSKGKIM NTEKQKLENV
LASEELKIFN TAIGTGTLDN YKEEDLKYDK IIIMSDADVD GYHIRTLWMT YIYRYMRPLI
TNGHLYLAQP PLYKVYKEGK GKSIVKYAYS DDQLEEVKKE VGKGALIQRY KGLGEMNPDQ
LWETTLNPET RTLLQVNIED AAKAEKMVSL LMGDIVEPRK NYMYKYGEF
//
