ID   I0I422_CALAS            Unreviewed;      1004 AA.
AC   I0I422;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-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=gyrA {ECO:0000313|EMBL:BAM00010.1};
GN   OrderedLocusNames=CLDAP_19700 {ECO:0000313|EMBL:BAM00010.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAM00010.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAM00010.1, ECO:0000313|Proteomes:UP000007880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC   {ECO:0000313|Proteomes:UP000007880};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-2012) 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; AP012337; BAM00010.1; -; Genomic_DNA.
DR   RefSeq; WP_014433245.1; NC_017079.1.
DR   AlphaFoldDB; I0I422; -.
DR   STRING; 926550.CLDAP_19700; -.
DR   KEGG; cap:CLDAP_19700; -.
DR   PATRIC; fig|926550.5.peg.2180; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_0; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000007880; 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   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; 5.
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   Reference proteome {ECO:0000313|Proteomes:UP000007880};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          28..496
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          835..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          461..488
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        835..850
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..921
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1004 AA;  110345 MW;  7D165E612D1ED0BD CRC64;
     MTDTNGVSTN AVSNNGAPDA FIGAVRIADI TQEMQTAYLD YAMSVIVARA LPDVRDGLKP
     VHRRILYAMW HDLSLTHDKP HKKSARIVGE VLGKYHPHGD AAVYDAMVRM AQPFSLRYPL
     IDGQGNFGSI DGDNAAAMRY TEARLARIAD LMLEDLEKDT VDWHDNFDNT LREPDILPAA
     LPNLLINGSS GIAVGMATNI PPHNLGEVVD ALAYMIDHYD HVDAITTEAL MRFIKGPDFP
     TGGILYRYRE ENKGEEEADA IAQGYSVGKS RLILQAKAHF EEISRGRTRI VITELPYQTN
     KTALLERIAD LVRDGKIEGI GDLRDESDRT GMRIVVELTR GADPKAVLAD LFRYTPLQQT
     FGMQLLALVD GQPRLLSLKR MLQLFIQHRQ EIIRRRSEFD LKKAKERAHI VEGLLRALDI
     LDEVIQTIRR SQTVETARNN LMHNFKFTEL QAQAILDMQL RRLAALERKK LQEEYKELKQ
     RIAYLEDLLA NPQKVLGVIK EELLAIKQEF GDARRTQIVD RTKGTLTTTD LLPDQRVWVS
     LSKNGDLRRQ AVSKPSASIV RQVGKDSQVA LLTASTRDYL CVFSKDGRCS RIGVHEIPEE
     GSKKVADLTG FTGRDAITAA LALPRERNGD EAGFIFLVTE QGIVKRVRTE DVQSNTGSEF
     TVIKVEEGDR LLWVFRTQGE QEVILVSAQG QSIRFSEEEV RSMGLPAGGV GGMKLKPNDR
     IVYAGAVDPT GELLTVTRAG FAKRSPLADY SAQGRNGGGI VTHKVTDKTG EVAAALVLPT
     KSESDWLVFV TARGVAKPML AVEVPAMGRG VQGKALVELS SQDAIVAVWR IESVKGEKSE
     EQRAESEASR TPIARTRSTT ERSTAERSTT KRSATDGETV PLASPHPAGS GVKSGGSVNK
     TTGDKKSTST ADKKKPADVD QQPSEARTPS PPTLKERKKK AAPPLQTPEV QTPEEAAPLA
     FEFIEQVPEV QPGKGGKSGR GKSKLSAVVS VPEAQIKTKK KPKA
//