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Database: UniProt
Entry: A0A1H3W8K4_9FIRM
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Original site: A0A1H3W8K4_9FIRM 
ID   A0A1H3W8K4_9FIRM        Unreviewed;       641 AA.
AC   A0A1H3W8K4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-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=SAMN02910384_00266 {ECO:0000313|EMBL:SDZ83406.1};
OS   Pseudobutyrivibrio sp. ACV-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=1520801 {ECO:0000313|EMBL:SDZ83406.1, ECO:0000313|Proteomes:UP000199179};
RN   [1] {ECO:0000313|Proteomes:UP000199179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACV-2 {ECO:0000313|Proteomes:UP000199179};
RA   Varghese N., Submissions S.;
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; FNQZ01000001; SDZ83406.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3W8K4; -.
DR   STRING; 1520801.SAMN02910384_00266; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000199179; 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: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; cd16928; HATPase_GyrB-like; 1.
DR   CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR   CDD; cd03366; TOPRIM_TopoIIA_GyrB; 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   InterPro; IPR034160; TOPRIM_GyrB.
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          422..540
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   641 AA;  71715 MW;  2ED7F00441F5F9EA CRC64;
     MANKVTYDAS SIAVLEGLEA VRKRPGMYIG STSRKGLNHL IYEIVDNSVD EHLAGECDTI
     YVTLEKDGSC TVEDNGRGIP VGMHAKGVPA ARLVFSTLHA GGKFDDSVYK TSGGLHGVGS
     SVVNALSEYM VVDISREGYV HHDRYERGVP TEELVDGLLP KISKTNKHGT KINFLPDPEI
     FEKTYFKEDE VKSRLHETAY LNPGLTINYA DLRGEEPEYK TYHEPEGIKG FVKEINKSAE
     TLHDVVYFSG KSDDVELEVA FQYCNEFKEN ILGFCNNIYN SEGGTHITGF KTVLTTVINN
     YARELGILKD KDANFTGADV RNGITAIVSI KHPDPRFEGQ TKTKLDNPDA SKATQKVCQD
     EFVLYFDRNL DTLKAIISCA EKSAKIRKSE EKAKTNLLTK QKFSFDQNGK LANCESRDSS
     KCEIFIVEGD SAGGSAKKAR NRMYQAIMPI RGKILNVEKA SMDKVLANAE IKTLINAFGC
     GFSEGYGNDF DIAKLRYDKI VIMADADVDG AHISTLLLTF FYRFMPELIR EGHVYIAMPP
     LYKAIPTKGE EEYLYDDVAL DKYRKKMNGK TFTLQRYKGL GEMDAEQLWE TTLDPERRKL
     KLVEIEDALM ASEVTELLMG SDVAPRKEFI YKHAKEAEID A
//
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