ID K0NFD1_DESTT Unreviewed; 757 AA.
AC K0NFD1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=parC {ECO:0000313|EMBL:CCK79610.1};
GN OrderedLocusNames=TOL2_C14470 {ECO:0000313|EMBL:CCK79610.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79610.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK79610.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
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};
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DR EMBL; FO203503; CCK79610.1; -; Genomic_DNA.
DR RefSeq; WP_014956956.1; NC_018645.1.
DR AlphaFoldDB; K0NFD1; -.
DR STRING; 651182.TOL2_C14470; -.
DR KEGG; dto:TOL2_C14470; -.
DR PATRIC; fig|651182.5.peg.1738; -.
DR HOGENOM; CLU_002977_4_1_7; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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 HAMAP; MF_00936; ParC_type1; 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 InterPro; IPR005742; TopoIV_A_Gneg.
DR NCBIfam; TIGR01062; parC_Gneg; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF1; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 2.
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, ECO:0000313|EMBL:CCK79610.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 15..465
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
SQ SEQUENCE 757 AA; 85556 MW; 393DB75EDBE539AE CRC64;
MKDTLPSAID DYEKIPFQDF AEKAYLNYSM YVILDRALPH IGDGLKPVQR RIVYAMSQLG
LSSSAKFKKS ARTVGDVLGK FHPHGDTACY EAMVHLAQPF SLRYPLVDGQ GNWGDPNDPK
SFAAMRYTES RLSQYAQIFL QELDQGTVDW SPNFDGTLNE PKILPARLPN ILLNGSTGIA
VGMATSLLPH NLREVAKALI HLIDNENADL DQICKYIKGP DFPTDAEIIT PSEEIIESYR
TGAGRIKMRA VFHVEDSEII YTALPHHAST EKIYEQIAAQ MEAKKLPMIS DIRDESDHEE
PTRLVVIPRS KNLDLNALTD HLFATTDLEK SYSFNMNLIG IDGRPKVKNL LEILTEWLEF
RAETVRKKIN FRLEKILDRL HILEGLLTAF LNIDEVINII RNSDHPKKDL IKAFSLTQIQ
AAAILEIRLR QLARLEEIKI KSELKDLESQ RKELEKILGC EKTFKSYIKE EIKADAKNYG
DKRRSPLQKR KEAEKFSVTD LMDIEPVTII LSKNGWIRSA KGHEINPETV KFKSGDSLMD
CLRTRSDKPI IFLDNTGRSY MLFSHSLPSA RGNGEPLTGQ LSIAPNAHIK FMLSGASNDY
FLVASDNGYG FIIKFTDFLT NYKNGKAVIN LKENHELLNP ENIVDREKDS IAAFSSQGRL
LIFTLSQLPN LKKGQGNKII SISKKNLNST PPERLKILKI VPSESNIIIY SGKHFLKLTP
GNQKDYTGSR GQRGKKLPRG YQNVDRVEII PINPVDE
//
