ID A0A1Q7UPZ9_9CHLR Unreviewed; 830 AA.
AC A0A1Q7UPZ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=AUG82_06905 {ECO:0000313|EMBL:OLE03564.1};
OS Ktedonobacter sp. 13_1_20CM_4_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE03564.1, ECO:0000313|Proteomes:UP000186213};
RN [1] {ECO:0000313|EMBL:OLE03564.1, ECO:0000313|Proteomes:UP000186213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(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 GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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:OLE03564.1}.
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DR EMBL; MNIY01000131; OLE03564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7UPZ9; -.
DR STRING; 1805225.AUG82_06905; -.
DR Proteomes; UP000186213; 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:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 4.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 19..479
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
SQ SEQUENCE 830 AA; 91305 MW; 2984784C8DF5B3A7 CRC64;
MARITDNSTT VETGIIREED FSVIMAQAFA TYGLSVVTDR ALPDARDGLK PVQRRILAGM
RAARYLSTRP TVKSAEVVGL ILGNYHPHGD TSVYDAAVRM AQPFTLRYPL IEGQGNMGSE
DGDAPAAYRY TEMRLSPLAE ALMADMESDT VPQHPSYKQD PKVLEPDYLP GRIPPIVNPS
SGIAVGLSTN IPPHNLVEVL RACIALLDQP NMDVEQLMRY IQGPDFCQGG RIIGVDGIKD
YFATGKGRII ARAEVRLEDT PRSRSLIVTQ IPPIGRDKVK ASIVKAINAR KLEGLLPDVR
DESDTEKGMR IVLELRKDAD AAQALSQLFA ETDLQIALSF QMVFLFGEPM QAARQPKQVG
MIDLLNYWNT HQMDVLTRRT QFELRKAEER LHIVEGLIVG AANADKIVKI FQQAEDRAAA
RQVIEKTYKL TLIQSEVIAS MTLAQVTRLD ASKYAREKVE LQTRIGELQH LLSDRKAMLL
LLKKEMQQLI KQFGDERRTT IDVEGQVHEP IKEVASLHER EPLAIAFTRA GTLKALPADT
FVPRGKNGAA IYTPVRGDEQ LRQVVAATSQ DYVLCVSSSG RVFQIAAHRI PTGNRSAKGE
PVRKLLGLAQ GEEIVTVLPV ENYDEDRYLV TFSRMGKVKK SPLSDYKTAD VDGLQDMKLA
DGDAVAVALL SRGQGEYFVT TNTAQTLRFK DDALRAQGRV GQGVAAIALG PDAQVVSASY
LDSEISTDSG NFLSLLVVTE SGLGKKVPLS QYPPKGRATA GIVTTELVDR DRVLLTMIID
EKDHLLLTWK NEDGEQVTAI KAVELKAFTR AKKGVPLVKG HMLGVVALDK
//