ID A0A0G1F537_9BACT Unreviewed; 818 AA.
AC A0A0G1F537;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=UV98_C0008G0007 {ECO:0000313|EMBL:KKT17445.1};
OS Parcubacteria group bacterium GW2011_GWB1_43_6.
OC Bacteria.
OX NCBI_TaxID=1618872 {ECO:0000313|EMBL:KKT17445.1, ECO:0000313|Proteomes:UP000034919};
RN [1] {ECO:0000313|EMBL:KKT17445.1, ECO:0000313|Proteomes:UP000034919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT17445.1}.
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DR EMBL; LCGO01000008; KKT17445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1F537; -.
DR PATRIC; fig|1618872.3.peg.182; -.
DR Proteomes; UP000034919; 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; 2.
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 NCBIfam; TIGR01063; gyrA; 1.
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; 6.
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 41..471
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 90955 MW; 91C8EF41E9E67560 CRC64;
MPQKKPIINK PIKPEKPKQA ASKKGEPRPE SGREIGYVKP REIVAEMQES YIDYAMSVIV
ARALPDVRDG LKPVHRRILY AMYEDGLTHG AKFRKSATVV GSVLGRLIQG QGNWGSIDGD
SAAAMRYTEC KMSKIGEEML RDIDKNTVEF TDNYDASRKE PMVLPSPVPQ LLLNGSLGIA
VGMATNIPPH NLTEVVEASI YLLDHPKADT EDLFKFVQGP DFPTGGNIYN AKEILEAYSL
GKGAIVTRGK AEVLENEKTG RSQIIITEIP YQVVKSTLIE QLALLVQEKK IDGIKDIRDE
SDREGLRIVI DMQKDAYPQK ILNRLYKFSD LQKTFHLNML ALVDGIQPRV LSLAEVLSYY
LQHRQDVVTR RLNFDLMKAK ERAHILEGLH KCLANIDLVI KIIKSSASRE DAMKNLMARF
RLTEIQANAI LETKLAALAK LERQKIADEL KELMALIKEL ALTLKDPEKI KEVVKKELKE
AKEVFGDPRK TKLHVQKIGE IAEEDLIPQE ETIITLTQGG YVKRINPSQY KNQKRGGKGM
MGMKTLGDDV VEHFLTAMTH DSLLFFTDSG KVFRTQAYEI PEGQRVAKGR GLLNFLELSS
EEKILSLNSL GKEDKDAGVK YLAMVTKNGI IKKTAIEDFD NVRRSGLIAI SLKKGDSLKS
VRKTTGENEL VIVTKLGQSI HFKEKDVRSM GRTASGIRGI RLGKGDEVIA MDVVSTDKQN
LLLVVSENGY GKRTDLKEYK IQGRGGSGIK TAQVTSKTGA LVYSMILKGD EEDLIVISKK
GQVIRTPVNA IAKISRATQG VRVMRLDPGD KVASAACL
//
