ID   F2R7Y8_STRVP            Unreviewed;       819 AA.
AC   F2R7Y8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   OrderedLocusNames=SVEN_5511 {ECO:0000313|EMBL:CCA58797.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA58797.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA58797.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
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; FR845719; CCA58797.1; -; Genomic_DNA.
DR   RefSeq; WP_015036693.1; NZ_JABVZO010000033.1.
DR   AlphaFoldDB; F2R7Y8; -.
DR   STRING; 953739.SVEN_5511; -.
DR   GeneID; 69867578; -.
DR   KEGG; sve:SVEN_5511; -.
DR   PATRIC; fig|953739.5.peg.658; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_11; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
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; 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:CCA58797.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          22..477
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          783..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  88255 MW;  F6EB2B0399E95E60 CRC64;
     MARRSTKTPP PDDAFEERIL DIDVVDEMQG SFLEYAYSVI YSRALPDARD GMKPVQRRIV
     YQMGEMGLRP DRGFVKCARV VGEVMGKLHP HGDASIYDAM VRMAQPFSMR LPLVDGHGNF
     GSLGNDDPPA AMRYTESRMA PAALLMTESI DEDTVDFAPN YDGQEQEPVA LPAAYPNLLV
     NGASGIAVGM ATNMPPHNLG EVIAAARHLI RHPHADLETL MRFVPGPDLP TGGRIVGLSG
     IKDAYESGRG SFKIRATTSV ETVTARRKGI VVTELPFTVG PEKVISKIKD LVGSKKLQGI
     ADVKDLTDRN HGLRLVIEIK NGFVPEAVLE QLYKLTPMEE SFGINNVALV DGQPLTLGLK
     ELLEVYLDHR FEVVRRRSEF RRTKKRDRLH LVEGLLVALL DIDEVIRLIR ESENSAQAKE
     RLMERFSLSE IQTQYILDTP LRRLTKFDRI ELETEQNRLN GEIDELTGIL ESDAELRKLV
     SAELAAVAKK FATDRRTVLL ESAGAPVAAV SLEVADDPCR VLLSSTGLLA RTATAELPPV
     DPDAARAKHD VILSSVAATQ RGDIGAVTSG GRLLRIAVID LPQLPDTASA PNLAGGAPLS
     EFLSLEADET VVCLTTLDEA SPGLALGTLQ GVVKRVVPDY PANKDELEVI TLKDGDRIVG
     ATELRTGDED LVFITSDAQL LRYPAAQVRP QGRPAGGMAG VKLSAGADVI SFTAVDPAAD
     AVVFTVAGST GTLDGSAATS AKLTPFDQYP RKGRATGGVR CQRFLKGEDV LLLAWAGTTP
     ARAAQKSGAP VNLPEVDPRR DGSGTPLPKP VDVVASAPS
//