ID   A0A485FYM2_PSEAI        Unreviewed;       707 AA.
AC   A0A485FYM2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   31-JUL-2019, entry version 3.
DE   RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
DE            EC=5.6.2.3 {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   -!- 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}.
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DR   EMBL; CAADJP010000009; VFT26456.1; -; Genomic_DNA.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (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
//