ID A0A387BV74_9MICO Unreviewed; 695 AA.
AC A0A387BV74;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=D7I44_16790 {ECO:0000313|EMBL:AYG05010.1};
OS Gryllotalpicola protaetiae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Gryllotalpicola.
OX NCBI_TaxID=2419771 {ECO:0000313|EMBL:AYG05010.1, ECO:0000313|Proteomes:UP000275069};
RN [1] {ECO:0000313|EMBL:AYG05010.1, ECO:0000313|Proteomes:UP000275069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2DFW10M-5 {ECO:0000313|EMBL:AYG05010.1,
RC ECO:0000313|Proteomes:UP000275069};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 2DFW10M-5.";
RL Submitted (SEP-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 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; CP032624; AYG05010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387BV74; -.
DR KEGG; gry:D7I44_16790; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000275069; 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 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:AYG05010.1};
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:UP000275069};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 468..582
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 695 AA; 76065 MW; BB6973D7EE57A7DF CRC64;
MGSADYSARH LSVLEGLEAV RKRPGMYIGS TDERGLMHCL WEIIDNSVDE ALAGFGGGID
VVLHPDDSVE VRDSARGIPV DIEPKTGLSG VEVVFTKLHA GGKFGGGSYS ASGGLHGVGA
SVVNALSERL DVEVDRDGKT WAMSFHRGEP GVFDDRGKAP TPDAPFTPFV ADSELRVVGR
VAKAKTGTRI RYWADRQIFG RDASFQPDGL VARARQTAFL VPGLRIVIDD QRSSDGEKTE
FHFDGGISQF ADYLAPDAGV TDTWRITGEG HFTETVPVLN ESGNMVPTEV KRTCEVDIAL
RWGTGYETVM KSFVNIIATP KGGSHQTGFE QGLMKFFRTQ FEQNARRLKI AATEKLEKDD
LLAGLTAVLT VRLPEPQFEG QTKEVLGTPA VRNIVANVLT KGLGERFTST KRDDKAQASV
LLDKLVAEMK SRISARAHKE TQRRKSALES STLPAKLVDC RSTNVAQTEL FIVEGDSALG
TARRGRDSEY QALLPIRGKI LNVQRASVSD MLSNAECAAI IQVIGAGSGR TFDLESARYG
KVIIMSDADV DGAHIRTLLL TLFFRYMRPM VEAGRVFAAV PPLHRVQTVG RGSRQSETIY
TYSEAELRAV LADLKKRNIG WKDPIQRYKG LGEMDADQLA STTMDRAHRM LRRVRVSDAE
QAAKVFEMLM GNEVAPRKEF IIAGSDSLSR DRIDA
//
