ID A0A094PG71_9ACTN Unreviewed; 686 AA.
AC A0A094PG71;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=GM45_4940 {ECO:0000313|EMBL:KGA08604.1};
OS actinobacterium acAMD-5.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504319 {ECO:0000313|EMBL:KGA08604.1, ECO:0000313|Proteomes:UP000029322};
RN [1] {ECO:0000313|EMBL:KGA08604.1, ECO:0000313|Proteomes:UP000029322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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:KGA08604.1}.
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DR EMBL; JNSF01000008; KGA08604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094PG71; -.
DR STRING; 1504319.GM45_4940; -.
DR PATRIC; fig|1504319.4.peg.992; -.
DR eggNOG; COG0187; Bacteria.
DR Proteomes; UP000029322; 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: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; 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; 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:KGA08604.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 463..577
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 686 AA; 74971 MW; 5C6F5357C6A657BE CRC64;
MARAKTPKTG YDASDIQVLE GLDAVRKRPG MYIGSTDGRG MAHCLWELLD NAVDEAIAGY
SKNVEAILHP DGSFEVKDDG RGIPVDIETK SKLTGVELVM TKLHAGGKFG GSSYSTSGGL
HGVGASVVNA LSARMEVEVD RDGKIHRIDF RRGVPGTFAG KGADASFTKK GGLRIEGKAP
KGVTGTRVRF WPDMQIFTPG SEIDIQLLHD RARQTAFLVS GLNIKVTDLR NGKESVNYKF
SGGITEYVEH LATDDPVTRV IRLDGVGNFQ ETVPVMDANG HMTPKEVDRE MQVEIALRWG
VGYDSDLRSF VNVVSTPKGG THVQGFERAI VKTINEQLKQ QKIVKPSEDS VIKDDILEGL
VAVISVRVPE PQFEGQTKEI LGTPAAVRVV GNVVSKQLAI WLSEPPRGAK NEAKGVLEKI
ANAARARIAA RTHRDVQRKK TAVESSALPA KLVDCRSKDI ERNELFIVEG ESALGTAKLA
RDSEFQALLP IRGKILNVQK ASFADMLKNA ECASIIQVIG GGSAREFDLE SVRYGKIIIM
TDADVDGAHI RSLLLTLFHK YLRPLIEDGR VYAAMPPLHR IETVGNKEFK YTYSDQEMKA
AIAAIEKAGK RVKEPIQRYK GLGEMDAVQL RDTTMSTASR GLRRVTVQDA ARMAEMFELL
MGSDVAPRKD FIVAAARSLD RDRIDA
//
