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Database: UniProt
Entry: A0A1R1LJV9_9MICC
LinkDB: A0A1R1LJV9_9MICC
Original site: A0A1R1LJV9_9MICC 
ID   A0A1R1LJV9_9MICC        Unreviewed;       703 AA.
AC   A0A1R1LJV9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=BKD30_02420 {ECO:0000313|EMBL:OMH27812.1};
OS   Tersicoccus phoenicis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Tersicoccus.
OX   NCBI_TaxID=554083 {ECO:0000313|EMBL:OMH27812.1, ECO:0000313|Proteomes:UP000187085};
RN   [1] {ECO:0000313|EMBL:OMH27812.1, ECO:0000313|Proteomes:UP000187085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1p05MA {ECO:0000313|EMBL:OMH27812.1,
RC   ECO:0000313|Proteomes:UP000187085};
RA   Nakajima Y., Yoshizawa S., Nakamura K., Ogura Y., Hayashi T., Kogure K.;
RT   "Draft genome of Tersicoccus phoenicis 1P05MA.";
RL   Submitted (DEC-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}.
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:OMH27812.1}.
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DR   EMBL; MRDE01000015; OMH27812.1; -; Genomic_DNA.
DR   RefSeq; WP_076701508.1; NZ_MRDE01000015.1.
DR   AlphaFoldDB; A0A1R1LJV9; -.
DR   STRING; 554083.BKD30_02420; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000187085; 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:OMH27812.1};
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:UP000187085};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          476..590
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          141..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  77058 MW;  6630BA0382DA7654 CRC64;
     MTAQRSEYTA RHLSVLEGLE AVRKRPGMYI GSTDSRGLMH CLWEIIDNSV DEALAGYGQS
     ITVILHADSS VEIHDEGRGV PVDIEPRTGL TGVEVVFTKL HAGGKFGGGS YTASGGLHGV
     GASVVNALSA RLDVQVDRGG KTHQMSFRRG EPGRFADRGP RPTADAVFTP FEEASTLDVV
     GKAKRGVTGT RIRYWADRQI FTPDARFNYD ELVTRARQTS FLVPGLRITI RDERGLPGTP
     GEHEMAEEVF QHDGGIAEFA DYLAVDASVT DTWRIHGSGS FTETVPVLDG SGHSRLTEVT
     RDCEVDVALR WGIGYETTIR SFVNIIATPK GGTHQSGFEQ ALLKTFRKTV EANARRLKAG
     NDKIERDDVF AGLTAVLTVR LAEPQFEGQT KEVLGTPAVR GIVSRVVEEA LTAKLTSTAR
     GEKTQANALL EKIVNEMKSR VSARQHKETQ RRKNALETST MPAKLADCRI NDVERSELFI
     VEGDSALGTA KLARSSDYQA LLPIRGKILN VQKASIGDML SNAECAALIQ VVGAGSGRTF
     DLTAARYGKV ILMTDADVDG AHIRTLLLTL FFRYMRPMVE DGRVYAAVPP LHRVEIVNPG
     GKANETVYTY SDAELHRVLT GLEKSGRRYK EPIQRYKGLG EMDADQLAET TMDPRHRTLR
     RVRYREAATA ETVFELLMGS EVAPRKDFIV AGAAMLDRDR IDA
//
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