ID A0A0A6UJN9_ACTUT Unreviewed; 685 AA.
AC A0A0A6UJN9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=MB27_28200 {ECO:0000313|EMBL:KHD74539.1};
OS Actinoplanes utahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1869 {ECO:0000313|EMBL:KHD74539.1, ECO:0000313|Proteomes:UP000054537};
RN [1] {ECO:0000313|EMBL:KHD74539.1, ECO:0000313|Proteomes:UP000054537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 12052 {ECO:0000313|EMBL:KHD74539.1,
RC ECO:0000313|Proteomes:UP000054537};
RA Velasco-Bucheli B., del Cerro C., Hormigo D., Garcia J.L., Acebal C.,
RA Arroyo M., de la Mata I.;
RT "Draft genome sequence of Actinoplanes utahensis NRRL 12052.";
RL Submitted (OCT-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:KHD74539.1}.
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DR EMBL; JRTT01000042; KHD74539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6UJN9; -.
DR STRING; 1869.MB27_28200; -.
DR eggNOG; COG0187; Bacteria.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000054537; 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, ECO:0000313|EMBL:KHD74539.1};
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:UP000054537};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 461..575
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 685 AA; 75280 MW; A1C9D312B91CC903 CRC64;
MTAQPETLYG ADDLTHLEGL DAVRKRPGMY IGSTDSRGIN HLANEIIDNC TDEGVAGHAT
RIAVTLHSDG SVQVDDDGRG IPVDVHAKSG LSGVELVLTR LHAGGKFGGS GYKTSGGLHG
VGASAVNALS HRFDVTVKRD GKVHEISFQR GVPGVFDGPG PEAAFTRQAG LRVVRRMKRG
ELSGTSIRYW YDARYFETGA RLDVDNVRTK LRNTAFLVPG VQYSLFDATA EEPATETFHY
PNGLADMVEF LTPAADKPVS GMLLVTGEGT YKENAADANG VMQSNVVRTA QIEVAFRWGT
GYERTVECFT NTIRNMHGGT HRKGFERALV RALTEAIRNA RGLLKPKEEP PVLDDFLEGM
TAVIHVRVPE PQFTSQTKDE LSTAGVARVM QSLVEAYLKE WIDGRRTKTE ARTVLQKVVD
AARVRLTQKQ QKDAARRKTA LEGASMPAKL VDCRAIGIDR SELFIVEGDS ALGTARMARS
SEYQALLPIR GKILNVQKAS LQQVLDNAEC SAIVQVLGAG SGRTFDIGQM RYGRVMIMAD
ADVDGSHIRT LLITLFAKYM RPVIENGRLF AAMPPLHKVV IKGRNSETLY TYTQQEMEST
VSRLERGGRQ VQKPVPRFKG LGEMDADELW DTTMNPAERT VRRITIEDAE RAEATLELLM
GERVEPRKNW LIEAAGRIDQ ETIDA
//
