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Database: UniProt
Entry: A0A1G5EZ75_9CLOT
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ID   A0A1G5EZ75_9CLOT        Unreviewed;       659 AA.
AC   A0A1G5EZ75;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=SAMN03080606_01274 {ECO:0000313|EMBL:SCY32141.1};
OS   Alkaliphilus peptidifermentans DSM 18978.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=1120976 {ECO:0000313|EMBL:SCY32141.1, ECO:0000313|Proteomes:UP000198636};
RN   [1] {ECO:0000313|EMBL:SCY32141.1, ECO:0000313|Proteomes:UP000198636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18978 {ECO:0000313|EMBL:SCY32141.1,
RC   ECO:0000313|Proteomes:UP000198636};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FMUS01000006; SCY32141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5EZ75; -.
DR   STRING; 1120976.SAMN03080606_01274; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000198636; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd01030; TOPRIM_TopoIIA_like; 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; 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:UP000198636};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          434..556
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   659 AA;  76116 MW;  EAACC07F8F28404D CRC64;
     MTLKTQHTYD NDSLSTLEEK DKVRLRPGVI FGSDGVEGCR HTLVEIVANA RDEAQEGYGD
     LIEVVRYKDK SIEVRDRGRG IPLEYNTKEQ KYNWEIVFTI LYGGGKYNNN SGSNYQYSIG
     LNGLGTAATQ FAAEYMDVEV YRDGHKYQLH FEKGENIGGL KKQEFNYTHT GSIIKWKPDL
     DVFNDINIPL SFFKETLKRQ AIVNKGITFK LYDEETEETF EYLYENGIVD YVKEINGEIG
     FTECQYFEFE TKGRDREDKE LYKLKIEVAF AFNNENTLLE YYHNSSFLEH GGSPDKAVDS
     AFSSQIHSFI KDKNKYTKNE KRVTFTDIKD SLILVTNTYS TITSYENQTK KAITNKFIQE
     AMTTFLKEKL EVYFIENKAD LEKIIDQVLI NKRSREKAEL TRIDVKKKLS KGIDNFSNKV
     KKFVDCRTKD ISRRELFIVE GDSALGSTKM GRDADFQAII PVRGKILNCL KSDYEKIFKN
     DIIVDILKVL GCGVEIKNKH NDLSFFDIEK LNWNKIIICT DADVDGFQIR TLILTMLYVL
     TPTLIEKGYV YIAESPLYEI ADSKDNVYFA YSDGEKNKIL KKLKANYKIQ RSKGLGENEP
     EMMWQTTMNP ESRRLIKVTP AEAQATKEAF ELFLGDNLMG RKEFISEHGY KYIEESDVI
//
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