ID D0RNK2_9PROT Unreviewed; 646 AA.
AC D0RNK2;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=HIMB114_00003710 {ECO:0000313|EMBL:EMH79998.1};
OS alpha proteobacterium HIMB114.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=684719 {ECO:0000313|EMBL:EMH79998.1, ECO:0000313|Proteomes:UP000033990};
RN [1] {ECO:0000313|EMBL:EMH79998.1, ECO:0000313|Proteomes:UP000033990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB114 {ECO:0000313|EMBL:EMH79998.1,
RC ECO:0000313|Proteomes:UP000033990};
RA Rappe M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EMH79998.1, ECO:0000313|Proteomes:UP000033990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB114 {ECO:0000313|EMBL:EMH79998.1,
RC ECO:0000313|Proteomes:UP000033990};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (SEP-2012) 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}.
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:EMH79998.1}.
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DR EMBL; ADAC02000001; EMH79998.1; -; Genomic_DNA.
DR AlphaFoldDB; D0RNK2; -.
DR STRING; 684719.HIMB114_00003710; -.
DR eggNOG; COG0187; Bacteria.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000033990; Unassembled WGS sequence.
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 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:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE 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 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:EMH79998.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000033990};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 427..541
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 646 AA; 72217 MW; FCD74B100B363AC5 CRC64;
MAISKTYSAK DIEVLEGLAP VRKRPGMYIG GTDETAYHHL ANEILDNSID EAVAGYAKEI
VIKLVNKNTI IISDDGRGIP IDKHPKKKKT ALEVVMTTLH SGGKFNDSVY KSSAGLHGVG
LSVVNALSSK LNIQVTKSSK IYSQDYSKGK ILNKLKTKGK NKIKNGTQIT FSPDPEIFGK
DVNFKPEKIY ELAKNKAYLQ KGIKISWECN KDLLNRKSSV PSKETLLFSK GLEDFLKNEI
NQNNVLHEKV SFQSGNLEDK KGKIEFALQF NKEKIKYNKA FCNTVYNMNG GTHDAGFRSG
IAKSIRKYAK NKNNKIVSKA TQDDIFDQAA YIISVYISNP EFEGQTKHKL SSNFVQKYCD
SFASSAFDEW LNRNSKAAKN ILNVLEEKIR EKNIYDLNQN VERQSAFRKI RLPGKLSDCT
SDKTEGTELF IVEGDSAGGS AKQARDRTTQ AILPLRGKIL NVKSSNAAKI LANSEINNLL
QALGCGRGKN YSKKDLRYEK IIIMTDADVD GDHISTLLLT FFISEMPQLI LDGHLYLAVP
PLYKLNISGK STYAIDESEK NKLLKDNKKA KIEISRFKGL GEMMPAQLKE TTMNIETRKL
IKVVLPVQKP KMKKTNKLVS DLMGKNAELR LKFISENANK SLSLDI
//
