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Database: UniProt
Entry: A0A2S6G0L0_9CLOT
LinkDB: A0A2S6G0L0_9CLOT
Original site: A0A2S6G0L0_9CLOT 
ID   A0A2S6G0L0_9CLOT        Unreviewed;       976 AA.
AC   A0A2S6G0L0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=BD821_101120 {ECO:0000313|EMBL:PPK49459.1};
OS   Clostridium algidicarnis DSM 15099.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121295 {ECO:0000313|EMBL:PPK49459.1, ECO:0000313|Proteomes:UP000239863};
RN   [1] {ECO:0000313|EMBL:PPK49459.1, ECO:0000313|Proteomes:UP000239863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15099 {ECO:0000313|EMBL:PPK49459.1,
RC   ECO:0000313|Proteomes:UP000239863};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (FEB-2018) 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}.
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:PPK49459.1}.
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DR   EMBL; PTIS01000001; PPK49459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6G0L0; -.
DR   STRING; 37659.GCA_000703125_02838; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000239863; 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; 2.
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; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 2.
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, ECO:0000313|EMBL:PPK49459.1};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          16..476
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          448..489
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   976 AA;  111340 MW;  A8C4DB6B10C36B81 CRC64;
     MAKKFIVPKD NNIIEVPLEE AMPENYLPYA VEVAKDRALP DVRDGLKPVH RRILYGAYLL
     KAFPDKAYFK SARIVGDILG KFHPHGDTSV YDAMTILAQD FSTRYKLIDG HGNWGSMDGD
     GAAAMRYTEA RLTPLALQMI RDIDKDVVDM ALNYSDTEFE PTVLPSRYPN LLVNGAFGIA
     VGLATNIPPH NLKEVIDASI KLMEDENITT KELMEYIKGP DLPTGGIILG KESLLAAYET
     GEGKVTSRAK TSIETLENGR FGIIITEFPY RKNKSKILQA ISDMTGDKKH AKYLESIVDI
     RDESDRTGVR SVVELKKTVE YEDAEKVLKY LFKKTDLQCN INFNMVALAN GKPETLGLKS
     ILKHYVNHQK EVVIRRTKRE LNIAEKRFHI VEGFIKAVGA MDEIISIIRA SKSKKDASNN
     LIERFEFSKE QTEAILELML YRLTGLEIKV FEKEYKELSK VIKSLKNILE NEKELLKVIK
     SELLEIRNTY GDERRTKIVE DDSEGKIDLE ELLVVEDIMV TLSKDGFIKR VPMKSYNRIN
     SDISDIEYRE GDAGRFLFQS NTKDTILVFT NKGQMYQIRG NDLPERKWKD NGVRLDSLIR
     SFNLDEETIV DVYSIENFSS SLDFMFLTSK GNIKKTSLDK FQTNYSRYSA LKLKKEDYLI
     DVKLVKKDRE EGFINIITKK GLNFDLEEPK LEESDRNVLG QQLFLLCKED EIIKAEYCKE
     MKYSEMIIGV NPQGNLKSFK KNSASTYKKV LTNSKEFIII FTDRGFAYKI PGFMIGNIED
     STINIEDLVD TFLKGKEKVL NILSSKDFNE EIWMYFFTKR GMIKKTNIKE LKGEYIETQV
     YKYKYEDDTL VTVEFGKDQN QEILLVTEKA MGIKFTSNSI KEMGKVASGV TGISLKEEDK
     VVFGTLTENS DDSNSNLCYN KEIAFTTNIK SINLLSSSGR KEGVKLENIK LQNRAGRGNN
     IMAISTGEYI KDIKLK
//
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