ID K9PJ62_9CYAN Unreviewed; 846 AA.
AC K9PJ62;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=Cal7507_2776 {ECO:0000313|EMBL:AFY33193.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY33193.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY33193.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY33193.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-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; CP003943; AFY33193.1; -; Genomic_DNA.
DR RefSeq; WP_015129005.1; NC_019682.1.
DR AlphaFoldDB; K9PJ62; -.
DR STRING; 99598.Cal7507_2776; -.
DR KEGG; calo:Cal7507_2776; -.
DR PATRIC; fig|99598.3.peg.3141; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_3; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000010390; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AFY33193.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 16..475
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 489..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 93903 MW; 39C4198AE89188D1 CRC64;
MAKQLNLLST GEVITTALHT EMQRSYLEYA MSVIVGRALP DARDGLKPVH RRILYAMHEL
GLTPDRPYRK CARVVGDVLG KYHPHGDQSV YDALVRLVQD FSSRYPLLAG HGNFGSVDND
PPAAMRYTET RLAAIGHEGM LTEIGEETVE FIGNFDNSQQ EPTVLPAQLP FLLLNGCSGI
AVGMATNIPP HNLGELVDGL IALIDQPDLT DEKLFELIPG PDFPTGGEIV GDSGIREAYT
TGKGSIVLRG VATLEEIPAA RGSKRRTAII ITELPYQVNK AGWIEKVADL VNQSKLQGIS
DLRDESDREG MRVVIELKRD TNPQEVLQHL YHQTALQTNF GAILLALVDG QPRQLSLRQL
LQEFLHFREH TLNRRYGYEL GKAENRLHLV EGLLSALSNV DEVIEILRQS PDGSTAKITL
CSRLELSEVQ ADAILAMPLR RLTGLELQNL QQEFEQLTEQ ITLLRRLLSD RKELLKALKK
DLRSLKRKYN DSRRTKLAPS STETRKQEYS TGRLQKESDE DNSQSQISNL KSSEPPEETV
LEFTQRGYVR RSLPNAKKPK ADNGLPDHDF LIQTELTDTE KDLLILTSGG KVYPVKVGDI
PAATGRSPRR TPLITMLTNT AQVAQEAVVS RFLLPDNSPT TQMILLTKQG RIKRLSLEEF
TNLTRRGVTI VKLKDDDELL FTQLTNIGEH LIVASSGGRL LRFPANDQDL PAMGRTAMGL
QALRLRKYEQ MVGCVTVSKD DQLLLVTQEG YAKRIPASSL RGANRGDLGT QALKFTSKTD
NLAAMVIAMP SAGYANASAE VALVTNKERV VRIPVETVPL LNRDSKGESI LQLNRDEKIM
TVAPVR
//
