ID C3KDM2_PSEFS Unreviewed; 754 AA.
AC C3KDM2;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 102.
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:CAY46776.1};
GN OrderedLocusNames=PFLU_0501 {ECO:0000313|EMBL:CAY46776.1};
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY46776.1};
RN [1] {ECO:0000313|EMBL:CAY46776.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY46776.1};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
RN [2] {ECO:0000313|EMBL:CAI2794819.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAI2794819.1};
RA Fortmann-Grote C.;
RL Submitted (OCT-2023) 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}.
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DR EMBL; OV986001; CAI2794819.1; -; Genomic_DNA.
DR EMBL; AM181176; CAY46776.1; -; Genomic_DNA.
DR RefSeq; WP_012721898.1; NC_012660.1.
DR AlphaFoldDB; C3KDM2; -.
DR STRING; 294.SRM1_00555; -.
DR PATRIC; fig|216595.4.peg.740; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_4_1_6; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP001152918; Chromosome.
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; 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 15..467
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 127
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 46
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 82
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 84
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 126
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 754 AA; 83559 MW; F4B4BED5130A7ABB CRC64;
MSDILADSLD GVERRSLADF TENAYLNYSM YVIMDRALPH IGDGLKPVQR RIIYAMSELG
LDADSKHKKS ARTVGDVLGK FHPHGDSACY EAMVLMAQPF SYRYTLVDGQ GNWGAPDDPK
SFAAMRYTEA RLSRYSEVLL SELGQGTADW GPNFDGTLDE PLVLPARLPN ILLNGTTGIA
VGMATDVPPH NLREVATACV RLLDEPKATV EQLCEHIQGP DYPTEAEIIT PRADLLKMYE
TGKGSVRMRA VYHIEDGDII VTALPHQVSG AKVLEQIAAL MQAKPSKLPQ VADLRDESDH
ENPCRIVIIP TNSRVDHEVL MQHLFASTEL ESSYRVNVNI IGLDGKPQLK NLRNLLVEWL
EFRINTVRRR LQFRLDKVER RLHLLDGLLI AYLNLDEVIH IIRTAEHPKA ELIARFELSE
IQADYILDTR LRQLARLEEM KLRDEQDALL KEQAKLQALL GSEAKLKKLV RSELIKDAET
YGDDRRSPIV QRAEAKALTE TELLPNEKIT VVLSEKGWVR SAKGHDIDAT GLSYKAGDGF
KTAAAGRSNQ FAVFIDSTGR SYSVPAHTLP SARGQGEPLT GRLTPPPGAN FECVLLPDDD
ALYVIASDAG YGFVVKGEDL QAKNKAGKAL LSLPNNAKVI LPRPVDDRES NWLASVTTEG
RLLVFKISDL PQLGKGKGNK IIGIPGERVA SREEYVTDIA VIPEGSTLVL QAGKRTLSLR
PDDLEHYKGE RGRRGNKLPR GFQRVDALLV ETPV
//
