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Database: UniProt
Entry: X5A2E5_9BACL
LinkDB: X5A2E5_9BACL
Original site: X5A2E5_9BACL 
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};
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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
//
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