ID A0A1C4Z7N2_MICVI Unreviewed; 748 AA.
AC A0A1C4Z7N2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=GA0074695_5174 {ECO:0000313|EMBL:SCF28671.1};
OS Micromonospora viridifaciens.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1881 {ECO:0000313|EMBL:SCF28671.1, ECO:0000313|Proteomes:UP000198242};
RN [1] {ECO:0000313|EMBL:SCF28671.1, ECO:0000313|Proteomes:UP000198242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43909 {ECO:0000313|EMBL:SCF28671.1,
RC ECO:0000313|Proteomes:UP000198242};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; LT607411; SCF28671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4Z7N2; -.
DR Proteomes; UP000198242; Chromosome i.
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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 524..638
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 81459 MW; 171B65C1620E75E7 CRC64;
MQVRLLASGN GASTGPGAAQ PDAAPHPVPQ LCRGSGLGSL RRAAHSDRAG ERHHTAETWE
YDQLTAQPET LYGADDLTHL EGLDAVRKRP GMYIGSTDSR GVGHLVNEIL DNSTDEGVGG
HATKIDVILH ADGSVQVDDD GRGIPTDVHA KSGISGVELV LTRLHAGGKF GGSGYKTSGG
LHGVGASAVN ALSRRFDVTV RRGGKIHSMS FRHGVPGIFD GDGPDAPFTP GPGLQIVGAM
KRRQPTGTSI RWWHDPRYFE TGARLDTEAV RLKLRNTAFL VPGVAYRLRD ETGEEVVEEN
FHFPNGLTDM VEYLAPAGDR AVSGTLLVTG EGTYRENAAD ANGVMQSNVQ RRAEVEVAFR
WGTGYERTVE CFTNTIRNAH GGTHRKGFER ALARTLAEAA RNTRGLLKPK EDAPTLDDVL
EGMTAVVHVR IPEPQFTSQT KDELSTAGIT KVIQGLVEQH LKSWLEDRKT KAEARTVLQK
IVDAARVRLT QKQQKDAARR KTALEGASMP AKLVDCRATG VDRSELFIVE GDSALGTSRM
ARSSEYQALL PIRGKILNVQ KANLQQVLDN AECAAIVQVL GAGSGRTFDL SALRYGRVLI
MADADVDGAH IRTLLITLFA RYMRPLIEAG RLYAAMPPLH KITTKGRNPQ TIYTYTQAEM
EATVRKLEKA GKQIVTPIPR FKGLGEMDAD ELWETTMNPA TRAVRRITLD DVEAAEQILE
LLMGEKVEPR RNWLIDSADR VDREAIDA
//
