ID A0A485FYM2_PSEAI Unreviewed; 707 AA. AC A0A485FYM2; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 13-NOV-2019, entry version 5. DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00936}; DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00936}; DE AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00936}; GN Name=parC {ECO:0000256|HAMAP-Rule:MF_00936, GN ECO:0000313|EMBL:VFT26456.1}; GN ORFNames=NCTC13621_03576 {ECO:0000313|EMBL:VFT26456.1}; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287 {ECO:0000313|EMBL:VFT26456.1}; RN [1] {ECO:0000313|EMBL:VFT26456.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC13621 {ECO:0000313|EMBL:VFT26456.1}; RG Pathogen Informatics; RL Submitted (MAR-2019) 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_00936}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent breakage, passage and rejoining of double- CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00936, ECO:0000256|SAAS:SAAS01218217}; CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000256|HAMAP-Rule:MF_00936}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00936}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00936}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. ParC type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00936}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00936}. 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; CAADJP010000009; VFT26456.1; -; Genomic_DNA. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR CDD; cd00187; TOP4c; 1. DR Gene3D; 1.10.268.10; -; 1. DR Gene3D; 2.120.10.90; -; 1. DR Gene3D; 3.90.199.10; -; 1. DR HAMAP; MF_00936; ParC_type1; 1. DR InterPro; IPR006691; GyrA/parC_rep. DR InterPro; IPR035516; Gyrase/topoIV_suA_C. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR002205; Topo_IIA_A/C. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR013757; Topo_IIA_A_a_sf. DR InterPro; IPR005742; TopoIV_A_Gneg. DR Pfam; PF03989; DNA_gyraseA_C; 2. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF101904; SSF101904; 1. DR SUPFAM; SSF56719; SSF56719; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00936, KW ECO:0000256|SAAS:SAAS01062879}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00936, KW ECO:0000256|SAAS:SAAS00972514, ECO:0000313|EMBL:VFT26456.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00936}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00936, KW ECO:0000256|SAAS:SAAS00974554}. FT DOMAIN 1 418 TOP4c. {ECO:0000259|SMART:SM00434}. FT ACT_SITE 80 80 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00936}. FT SITE 35 35 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00936}. FT SITE 37 37 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00936}. FT SITE 79 79 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00936}. SQ SEQUENCE 707 AA; 78068 MW; B010F941E40238F0 CRC64; MQRRIVYAMS ELGLDADSKH KKSARTVGDV LGKFHPHGDS ACYEAMVLMA QPFSYRYPLV DGQGNWGAPD DPKSFAAMRY TEARLSRYSE VLLSELGQGT VDWVPNFDGT LDEPAVLPAR LPNLLLNGTT GIAVGMATDV PPHNLREVAS ACVRLLDQPG ATVAELCEHV PGPDFPTEAE IITPRADLQK VYETGRGSVR MRAVYRVEDG DIVIHALPHQ VSGSKVLEQI AGQMQAKKLP MVADLRDESD HENPTRIVII PRSNRVDVEE LMTHLFATTD LETSYRVNLN IIGLDGKPQV KDLRQLLSEW LQFRIGTVRR RLQFRLDKVE RRLHLLDGLL IAFLNLDEVI HIIRTEDQPK AVLMERFELS EVQADYILDT RLRQLARLEE MKIRGEQEEL LKEQKRLQTL LGSEAKLKKL VREELIKDAE TYGDDRRSPI VARAEARALS ETELMPTEPV TVVLSEKGWV RCAKGHDIDA AGLSYKAGDG FKAAAPGRSN QYAVFIDSTG RSYSLPAHSL PSARGQGEPL SGRLTPPPGA SFECVLLPDD DALFVIASDA GYGFVVKGED LQAKNKAGKA LLSLPNGSAV VAPRPVRDVE QDWLAAVTTE GRLLLFKVSD LPQLGKGKGN KIIGIPGERV ASREEYLTDL AVLPAGATLV LQAGKRTLSL KGDDLEHYKG ERGRRGNKLP RGFQRVDSLL VDIPPQD //