ID A0A1S2C6S3_9BACI Unreviewed; 808 AA. AC A0A1S2C6S3; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-JUN-2017, entry version 3. DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00937}; DE EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_00937}; DE AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00937}; GN Name=parC {ECO:0000256|HAMAP-Rule:MF_00937}; GN ORFNames=BCV52_16060 {ECO:0000313|EMBL:OHY76221.1}; OS Bacillus aryabhattai. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=412384 {ECO:0000313|EMBL:OHY76221.1, ECO:0000313|Proteomes:UP000180110}; RN [1] {ECO:0000313|EMBL:OHY76221.1, ECO:0000313|Proteomes:UP000180110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB211 {ECO:0000313|EMBL:OHY76221.1, RC ECO:0000313|Proteomes:UP000180110}; RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Topoisomerase IV is essential for chromosome CC segregation. It relaxes supercoiled DNA. Performs the decatenation CC events required during the replication of a circular DNA molecule. CC {ECO:0000256|HAMAP-Rule:MF_00937}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_00937, CC ECO:0000256|SAAS:SAAS00377109}. CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000256|HAMAP-Rule:MF_00937}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00937}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00937}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. ParC type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00937}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OHY76221.1}. 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; MCAN01000003; OHY76221.1; -; Genomic_DNA. DR RefSeq; WP_071274130.1; NZ_MCAN01000003.1. DR Proteomes; UP000180110; Unassembled WGS sequence. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.268.10; -; 1. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 1. DR HAMAP; MF_00937; ParC_type2; 1. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR006691; GyrA/parC_pinwhl. DR InterPro; IPR013760; Topo_IIA-like_dom. DR InterPro; IPR002205; Topo_IIA_A/C. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR013757; Topo_IIA_A_a. DR InterPro; IPR005741; TopoIV_A_Gpos. DR Pfam; PF03989; DNA_gyraseA_C; 5. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01061; parC_Gpos; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00937}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000180110}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00937, KW ECO:0000256|SAAS:SAAS00454525}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00937, KW ECO:0000256|SAAS:SAAS00454466}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00937}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00937, KW ECO:0000256|SAAS:SAAS00075980}. FT DOMAIN 10 463 TOP4c. {ECO:0000259|SMART:SM00434}. FT COILED 435 462 {ECO:0000256|SAM:Coils}. FT ACT_SITE 121 121 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00937}. FT SITE 41 41 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00937}. FT SITE 77 77 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00937}. FT SITE 79 79 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00937}. FT SITE 90 90 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00937}. FT SITE 96 96 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00937}. FT SITE 120 120 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00937}. SQ SEQUENCE 808 AA; 91410 MW; BA6167C30398702A CRC64; MTQTERFLDL PLEDVLGDRF GRYSKYIIQE RALPDARDGL KPVQRRILYA MHVDGNTAEK GFRKSAKTVG NVIGNYHPHG DSSVYDAMVR MSQEWKVRNV LIEMHGNNGS IDGDPPAAMR YTEARLSSIA AELLRDIDKQ TVEFVSNFDD TSSEPTVLPA MFPNLLVNGS TGISAGYATE LPPHHLGEVI DATIMRIDKP TCTIEELMTA IQGPDFPTGG IIQGVDGIKK AYETGKGKII IRGKTEVESI RGGKQQIVIT EIPFEVNKAN LVKKMDELRL DKKVEGIAEV RDETDRTGLR IVVELKKDAN AQGVLHFLYK NTDLQVPYNF NMVAIAKKRP KLMSLPNILD AYIDHQKEVV TNRSKYELQK AREREHIVAG LIKALSILDE VIATIRASKD KRDAKNNLIA KYEFTEPQAE AIVSLQLYRL TNTDITALQA EAEELGAKIN ELEEILHSEK KLFNVIKKEL RRVKKQYSTE RRSKIEAEIE EIKINLEVMV PSEEVMVTVT KDGYVKRTSL RSYAASNGQD FGMKDTDRIL AKYEINTTET LLIFTNKGNY LYMPVHELPD IRWKDMGQHI MNIVPIDKEE QIVRAIPVKE FKENQYLLFF TKNGMVKKSE LLQYKAQRYS KALVAVNLKG DDEVVDVYQT DGKKQVFIAT RSGYGLRFRE EEINIVGTRA SGVKGINLKD EDYVVSGVVF DEDEALSTEL FIATQRGAVK KTKITEFEES ARAKRGLVMV RELKSNPHQI AKVKVISKEH YMIVESSKGQ IEQVDPSTMR ASDRYSNGSF VLDQSEAGNL VDMWLEEK //