ID R5K9Z2_9CLOT Unreviewed; 676 AA.
AC R5K9Z2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=BN743_01127 {ECO:0000313|EMBL:CCY57842.1};
OS Clostridium sp. CAG:632.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262830 {ECO:0000313|EMBL:CCY57842.1, ECO:0000313|Proteomes:UP000018242};
RN [1] {ECO:0000313|EMBL:CCY57842.1, ECO:0000313|Proteomes:UP000018242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:632 {ECO:0000313|Proteomes:UP000018242};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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}.
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:CCY57842.1}.
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DR EMBL; CAYL010000025; CCY57842.1; -; Genomic_DNA.
DR AlphaFoldDB; R5K9Z2; -.
DR STRING; 1262830.BN743_01127; -.
DR Proteomes; UP000018242; 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 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; 6.
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:UP000018242};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 1..292
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 649..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..291
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 653..669
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 76261 MW; B18E5935EFAC80EB CRC64;
MATNIPPHNL REVIDAVVKI IDNRIMEDRD TDIEEIIQII KGPDFPTGAQ ILGTSEIDAA
YRTGRGKVKV RAISNIEPMA NGKQRIVITE LPYMVNKARL IQKIAELVKD KKIEGITALR
DESSREGMRV VIELKKDANA NIIMKKLYKH TQLQDTFGVI MLALVNNEPK VLNLLEMLTY
YLKHQEDVVT RRTKYELNKA EERAHILEGL LIALDNIERV IEIIRGSKNV TEAKEKLMQE
FGLSDAQSQA IVDMRLRALT GLERDKIENE YRELIERIAE LKAILADEKK LLGVIREELL
IISTKYGDDR RTAIGPDEDD ITDEELIKRE NTVIAMTKLG YIKRMTVDNF RAQNRGGKGI
KGMQTIEDDF IEELIMTTTH HFIMFFTNLG RVYRLKAYEI PESGRTARGT AIVNLLQMLP
GEHITAVIPI REFKPGRYLL MATKKGMIKK TPITDYQNIR KNGLAAITLR DEDELIEVKS
TNNKKEVILV SKQGMCIRFL ETDVRSTGRT SIGVKGMNLN AGDEVIGMQL DTQGEDLLIV
SENGMGKRTS MDEFTPQNRG GKGVKCYKIN DKTGNVIGVK AVNEDNEIML ISTEGIVIRL
QCSDISRLSR VTSGVKLINM DTENNIHVAS VAKVRDKDPE ADIKALESQM EEELDVGAVE
EIEDDVPDTT DDNEKN
//
