ID A0A0D8IFJ9_9CLOT Unreviewed; 659 AA.
AC A0A0D8IFJ9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=gyrB2 {ECO:0000313|EMBL:AKL95351.1};
GN ORFNames=CACET_c19030 {ECO:0000313|EMBL:AKL95351.1}, TZ02_00360
GN {ECO:0000313|EMBL:KJF28839.1};
OS Clostridium aceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL95351.1, ECO:0000313|Proteomes:UP000035704};
RN [1] {ECO:0000313|EMBL:AKL95351.1, ECO:0000313|Proteomes:UP000035704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL95351.1,
RC ECO:0000313|Proteomes:UP000035704};
RA Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aceticum DSM 1496.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KJF28839.1, ECO:0000313|Proteomes:UP000032372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:KJF28839.1,
RC ECO:0000313|Proteomes:UP000032372};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Clostridium aceticum DSM 1496, a potential
RT butanol broducer through syngas fermentation.";
RL Submitted (FEB-2015) 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; CP009687; AKL95351.1; -; Genomic_DNA.
DR EMBL; JYHU01000001; KJF28839.1; -; Genomic_DNA.
DR RefSeq; WP_044822920.1; NZ_JYHU01000001.1.
DR AlphaFoldDB; A0A0D8IFJ9; -.
DR STRING; 84022.CACET_c19030; -.
DR KEGG; cace:CACET_c19030; -.
DR PATRIC; fig|84022.5.peg.74; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000032372; Unassembled WGS sequence.
DR Proteomes; UP000035704; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:AKL95351.1};
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:UP000035704};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 434..556
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 659 AA; 76005 MW; 6EFD023ACC596BF8 CRC64;
MTIKKQHNYG NDSLSTLQEK DKVRLRPGVI FGSDGIEGCC HTLVEIVANA RDEAQEGFGS
LIEVFRYKDR SIEVRDRGRG IPLEYNVKEE KYNWEIVFTI LYGGGKYNNN SGSNYQYSIG
LNGLGTAATQ FASEYMDVEV YRDGHRYQLH FEKGEVIGEL IKEKYDHQYT GTNIKWKPDL
EVFNDIDISL SFFKEVLKRQ AIVNKGITFK LYDEETDETF QYYYENGIID YVKEINGEKG
FTEPQYFELE TKGRDREDKE EYKLKIEVAF VFNNEHNLLE YYHNSSFLEY GGAPDKAVDS
GFSSQVHSFI KDKNKYTKNE KRVTFTDIKD SLILVTNTYS TITSYENQTK KAITNKFIQE
AITAFLKEKL EIYFTENQAD LEKIVDQILI NKRSREKAEL TRIDVRKKLS KGIDNFSNKV
KKFVDCRSKD ITKRELFIVE GDSALGSTKM GRDAEFQAII PVRGKILNCL KSDYDKIFKN
DIIVDLLKVL GCGVEIKSKH SDLSFFDIDK LNWSKIIICT DADVDGFQIR TLILTMLYVL
TPTLIEKGCV YIAESPLYEI TDSKDNTFFA YSEGEKNTII KKLKSNYKIQ RSKGLGENEP
DMMWQTTMNP ETRRLIKVTP TEAQATKEAF ALFLGDNLPG RKEYISKHGS KYLDQCDVV
//
