ID   A0A485FYM2_PSEAI        Unreviewed;       707 AA.
AC   A0A485FYM2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   29-MAY-2024, entry version 18.
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; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287 {ECO:0000313|EMBL:VFT26456.1, ECO:0000313|Proteomes:UP000344659};
RN   [1] {ECO:0000313|EMBL:VFT26456.1, ECO:0000313|Proteomes:UP000344659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13621 {ECO:0000313|EMBL:VFT26456.1,
RC   ECO:0000313|Proteomes:UP000344659};
RG   Pathogen Informatics;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It
CC       relaxes supercoiled DNA. Performs the decatenation events required
CC       during the replication of a circular DNA molecule. {ECO:0000256|HAMAP-
CC       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|ARBA:ARBA00000185,
CC         ECO:0000256|HAMAP-Rule:MF_00936};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC       Rule:MF_00936}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00936}.
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DR   EMBL; CAADJP010000009; VFT26456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A485FYM2; -.
DR   Proteomes; UP000344659; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:TreeGrafter.
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; 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   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; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   InterPro; IPR005742; TopoIV_A_Gneg.
DR   NCBIfam; TIGR01062; parC_Gneg; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   PANTHER; PTHR43493:SF1; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 2.
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   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00936};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00936};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00936}.
FT   DOMAIN          1..418
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   ACT_SITE        80
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            35
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            37
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            79
FT                   /note="Transition state stabilizer"
FT                   /evidence="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
//