ID A0A1N6WVM2_9ACTN Unreviewed; 685 AA.
AC A0A1N6WVM2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=SAMN05444858_105125 {ECO:0000313|EMBL:SIQ94149.1};
OS Micromonospora avicenniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1198245 {ECO:0000313|EMBL:SIQ94149.1, ECO:0000313|Proteomes:UP000186004};
RN [1] {ECO:0000313|EMBL:SIQ94149.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45758 {ECO:0000313|EMBL:SIQ94149.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; FTNF01000005; SIQ94149.1; -; Genomic_DNA.
DR RefSeq; WP_076470082.1; NZ_FTNF01000005.1.
DR AlphaFoldDB; A0A1N6WVM2; -.
DR STRING; 1198245.SAMN05444858_105125; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000186004; 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; 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};
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:UP000186004};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 461..575
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 685 AA; 74928 MW; E3E38B1E9C8D44E4 CRC64;
MTAEPETLYG ADDLTHLEGL DAVRKRPGMY IGSTDSRGVG HLVNEILDNS TDEGVAGHAS
RVEVTLHADG SVQVDDDGRG IPTDVHARSG LSGVELVLTR LHAGGKFGGS GYKTSGGLHG
VGASAVNALS RRFDVTVRRG GKIHSMSFRH GVPGIFDGDG PDASFTAGPG LQVVGAMKRN
QRTGTSIRWW HDARYFETGA ALDVEAVRMK LRNTAFLVPG VSYLLRDLTG EEPVEETFHF
PNGLTDMVDF LAPAGDRPVS GTLLVNGEGT YRENAADANG VMQSNVQRRA EVEIALRWGT
GYERTVECFS NTIRNAHGGT HRKGFERALV RTLADAARNT RGLLKAKEDA PTLDDVLEGM
TAVVHVRIPE PQFTSQTKDE LSTAGITKVV QQLVEQHLKS WLEDRRTRAE ARTVLQKIVD
AARVRLTQKR QKDAARRKTA LEGASMPAKL VDCRATGIDR SELFIVEGDS ALGTSRMARS
SEYQALLPIR GKILNVQKAN LQQVLDNAEC AAIVQVLGAG SGRTFDLSAL RYGRVLIMAD
ADVDGAHIRT LLITLFARYM RPLIEAGRLY AAMPPLHKIT TKGRNPQTIY TYTQAEMETT
VRRLEKAGKQ IVTPIPRFKG LGEMDADELW ETTMNPATRA VRRITLDDVD AAERILDLLM
GEKVEPRRNW LIDSADRVDR EAIDA
//
