ID X5A2E5_9BACL Unreviewed; 813 AA.
AC X5A2E5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=PSAB_15460 {ECO:0000313|EMBL:AHV97999.1};
OS Paenibacillus sabinae T27.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV97999.1, ECO:0000313|Proteomes:UP000019772};
RN [1] {ECO:0000313|EMBL:AHV97999.1, ECO:0000313|Proteomes:UP000019772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T27 {ECO:0000313|EMBL:AHV97999.1,
RC ECO:0000313|Proteomes:UP000019772};
RX PubMed=24651173;
RA Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA Chen X., Cheng Q., Chen S., Li J.;
RT "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT Genes.";
RL PLoS Genet. 10:E1004231-E1004231(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004078; AHV97999.1; -; Genomic_DNA.
DR RefSeq; WP_025335497.1; NZ_CP004078.1.
DR AlphaFoldDB; X5A2E5; -.
DR STRING; 1268072.PSAB_15460; -.
DR KEGG; psab:PSAB_15460; -.
DR PATRIC; fig|1268072.3.peg.3195; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000019772; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 InterPro; IPR005741; TopoIV_A_Gpos.
DR NCBIfam; TIGR01063; gyrA; 1.
DR NCBIfam; TIGR01061; parC_Gpos; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF9; DNA TOPOISOMERASE 4 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 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AHV97999.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 11..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 429..456
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 813 AA; 90717 MW; 5634E3F90EDB5F25 CRC64;
MSSLSEQFLP AFLEEVVGDR FGRYSKYIIQ DRAIPDVRDG LKPVQRRILY AMYDSGNTPD
KPYRKSAKTV GDVMGNYHPH GDSSIYEGMV RMAQPWKMGH VLVDGHGNWG SMDDDPAAAM
RYTEARLSPI AMEMMRDIEK RTVLFKDNFD NTAKEPVVVP SRYPNLLVNG TSGISAGFAT
EIPPHNLRET IDACIAVMQK PEIELEEIMT FMKGPDFPTG GLIMGGDGIM DAYRSGKGRI
YLRSKTEFEN LRGGKQQIVI TEIPFQVVKS RLVTAMENIR LEKKVEGIAE VRDESGREGL
RIVVELKKEA DAQGILAYLL KKTDLQITYN FNMVAIVNKA PQQLGLKSIL EAYIAHQREV
VTHRTQFDLE RAEDRAHVLE GLVKALNILD EVIAAIKASK NRQDAQNNLV WMFGFSERQA
DSILTLQLYR LTNLEIRTLE KELEETQRKI LTLRGILESD KKLVGVIRKE LLEIRDKYGI
DRRSAIQGEV EELKVSLEAL VNAEDVLVAL SADGYIKRTS MLSFTRSGGE RNASGVKEGD
YITRILDVNT RDSLLVFTGK GQYFLLPVHQ IPEFKWKDPG TAIVNVIGLS KGDGIAGIIP
VSNFEEPGRS LIFVTRKGQV KRTELKEYVT SRSGAIAACK VGAEDEVLTV MLSEGDQDLV
LVTREGMSIR FRENEVNPMG RVAAGVKGIQ LKEGDEVVAC FRVTDDEGEI LVLSDIGYGK
RSLLLDYVPQ SRGGKGVPTF EFKEGKRVRP NGSRIAGAFY CRETLELTAI TREGEILSFS
SEAAPIDERR STGKLLVPVV KKDEIVSVQI SVK
//