ID H5WWE7_9PSEU Unreviewed; 694 AA.
AC H5WWE7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=SacmaDRAFT_1148 {ECO:0000313|EMBL:EHR49431.1};
OS Saccharomonospora marina XMU15.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR49431.1, ECO:0000313|Proteomes:UP000004926};
RN [1] {ECO:0000313|EMBL:EHR49431.1, ECO:0000313|Proteomes:UP000004926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR49431.1,
RC ECO:0000313|Proteomes:UP000004926};
RX PubMed=22768369; DOI=10.4056/sigs.2655905;
RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT type strain (XMU15(T)).";
RL Stand. Genomic Sci. 6:265-275(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001439; EHR49431.1; -; Genomic_DNA.
DR AlphaFoldDB; H5WWE7; -.
DR STRING; 882083.SacmaDRAFT_1148; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_4_1_11; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000004926; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
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: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:EHR49431.1};
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:UP000004926};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 470..584
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 694 AA; 75631 MW; 7D0AA7A597940155 CRC64;
MTILGASDPV TASAETLYGA DDLTHLEGLE AVRKRPGMYI GSTDSRGVNH LFTEIVDNST
DEGVAGYASR VVVTLHADGS VEVEDDGRGI PTGVHGKSGL SGVELVLTRL HAGGKFGGSG
YKTSGGLHGV GASAVNALSL RFDVTVKQGG KVHEMSFARG VPGVFDGPGP KARFTRQSGL
RLVRKMKRGE STGTTIRYWH DARYFESGAT LDLETVRTKL RHTAFLVPGL TYVLRTATDA
TINEETFHFP NGLADMVEFL APAADKPVSG ILLMNGEGTY KENAADENGV MKSNVERKAE
VEVALRWGTG YERTVECFTN TIRNVHGGTH RKGFERALVR SVHDAISKTR GLLKPKEDPP
TLDDICEGMT AVIHVRIPEP QFTSQTKDEL STAGITKVIQ GIVEKNVKAW TEHRRSKSEA
KTVLQKIVDA SRVRIAQKQQ KDAARRKTAL EGAAMPPKLV DCRTTGVARS ELFLVEGDSA
LGSARMARVS EYQALLPLRG KILNVQKAGL GDALKNAEIA SIVQVLGAGT GRTFDTSTMR
YGRVILMADA DVDGSHIRTL LITLFARYMR PVIEEGRLYT AMPPLHKIVT KGRNQQTFYT
FTEREMETKV AQLEKAGKQV VKPVPRFKGL GEMDADELWE TTMNPATRAV RRITLDDVEA
AEAALELLMG EKVEPRRNWL VASAERVDQA AIDI
//
