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Database: UniProt
Entry: A0A1F6N9U1_9BACT
LinkDB: A0A1F6N9U1_9BACT
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ID   A0A1F6N9U1_9BACT        Unreviewed;       582 AA.
AC   A0A1F6N9U1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=A3I29_03430 {ECO:0000313|EMBL:OGH80707.1};
OS   Candidatus Magasanikbacteria bacterium RIFCSPLOWO2_02_FULL_44_11.
OC   Bacteria; Candidatus Magasanikbacteria.
OX   NCBI_TaxID=1798689 {ECO:0000313|EMBL:OGH80707.1, ECO:0000313|Proteomes:UP000178726};
RN   [1] {ECO:0000313|EMBL:OGH80707.1, ECO:0000313|Proteomes:UP000178726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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   -!- 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:OGH80707.1}.
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DR   EMBL; MFQK01000034; OGH80707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6N9U1; -.
DR   STRING; 1798689.A3I29_03430; -.
DR   Proteomes; UP000178726; 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:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00081; Hint; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR030934; Intein_C.
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; IPR006171; TOPRIM_domain.
DR   NCBIfam; TIGR01443; intein_Cterm; 1.
DR   PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          312..335
FT                   /note="Intein C-terminal splicing"
FT                   /evidence="ECO:0000259|PROSITE:PS50818"
FT   DOMAIN          322..436
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   582 AA;  68250 MW;  54A0478CF2EA74C5 CRC64;
     MPLYRQTSRL GKRITIAGYE LVRDPKENRW IFTHLLADEY NLAQGTYSIN DGTHRHHVDY
     NKRNNNPKNI KRLTKEGHLQ IHRDHVDKTL RRPDVIAKML AAKKSPAYRS KMSAAMKKIA
     PLLRARAKKQ WSDPAYKDYM KEKFLTFYKT NEVYRKKNNA LLNEEQFKYW ADKTHRQKQA
     ERVTAFFEKH PERREALQAE ATEQWKNVDL RVWRAEKTKA QWDNSFRAKR KRAYDQVYLQ
     HSLKLLSDVY KTNGTIENYD MVRRSIKANK NYLKLSTIIQ RFFKNDQKEL LAAVQNYNHR
     IVSIKKLTKR IPVYDIEVPN THNFALANGV FVHNSAKQGR DREHQAILPL RGKVLNVERA
     RLDKILTNNE LKSLIIAMGT NIGEQFDITK LRYHRIVIMT DADVDGAHIR TLLLTFFYRY
     YVELLKNGHI YIAQPPLYSL KYGKEMFYAY NDEEKAKVLK DLENRKVAKA ETKKAAKNDK
     EIVEGEGENE SEADKAVEAE EKQAIMIGGT KVNIQRYKGL GEMNPDQLWD TTMDPKNRMM
     KLVTVDDAEA ANETFEILMG DEVEPRKKFI QTYAKSVQNL DI
//
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