ID W0DBK6_9AQUI Unreviewed; 756 AA.
AC W0DBK6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=THERU_01910 {ECO:0000313|EMBL:AHE95626.1};
OS Thermocrinis ruber.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX NCBI_TaxID=75906 {ECO:0000313|Proteomes:UP000018914};
RN [1] {ECO:0000313|EMBL:AHE95626.1, ECO:0000313|Proteomes:UP000018914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23557 {ECO:0000313|EMBL:AHE95626.1,
RC ECO:0000313|Proteomes:UP000018914};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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DR EMBL; CP007028; AHE95626.1; -; Genomic_DNA.
DR RefSeq; WP_025305593.1; NZ_CP007028.1.
DR AlphaFoldDB; W0DBK6; -.
DR STRING; 75906.THERU_01910; -.
DR KEGG; trd:THERU_01910; -.
DR PATRIC; fig|75906.3.peg.374; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_4_1_0; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000018914; Chromosome.
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; 3.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 6..459
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 431..472
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 756 AA; 85309 MW; A48979F5321CD69B CRC64;
MEILEVPIEE EVKQSYIDYA MSVIVGRAIP DVRDGLKPVQ RRILYAMHDM GLTPDKGFVK
SARIVGAVLG HFHPHGDQAV YETLVRMAQD FVMNYPLIIG QGNFGSIDGD PPAAMRYTEA
KLSKYAVLML EDIDKDTVDF VPNFDGSTLE PTVLPSKFPN LLCNGASGIA VGLATSIPPH
NLKEVCTALI ELAKNPDIDT KEIMRYIKGP DFPTGGVVEN YDELIEFYEK GRGQVRIRAK
AHVEKLSGGR EQIVITEIPY QVNKAELIKR MAELVREGKL KEISDIRDES DKEGLRIVVE
LKRDADGSKV LEKLYKYTQL RKNFPINFVV LINGEPKQVG IKTLLYEFFR HRLEVIHRRS
KYYLKKAEER LHIVKGLLIA LAHLDQVIQD IKSSKDTQEA KEKLIKKYSL TEAQANAVLD
LRLQRLTSLE RQKLEEEEKE LLEKIEYYTR LVESEEEKIK VFIEEMSNLS ESFPAVRRTF
VEGVGGEQRT GSITVVVFSD GKVMPLTEIE EGEVVNILDV PFDDGLFMVS NRGRVYWVAG
LQALQGSKVS FKEPEERLVG AFVRSQAADR LLLATSEGYV KKIPLVDFEY KAQGTNIIKL
TEDQGDVVKV LQSPEEGDLL IFTKMGKILR FPVAEISPAT IGSKGVVGIK LDRGDKVVGM
RVIRGEKFLL IITEKGTVQK MVSEYVPRKS RGSKGLSILT RERLVDILPL GEGQFLDLML
ITQEGSVFYD RVREEELPLN KAQKRWDGKI VKVVIK
//
