PARC_ECOLI
ID PARC_ECOLI Reviewed; 752 AA.
AC P0AFI2; O69154; P20082; Q2M9I1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00936, ECO:0000269|PubMed:12269820, ECO:0000269|PubMed:16023670, ECO:0000269|PubMed:21300644};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
GN Name=parC {ECO:0000255|HAMAP-Rule:MF_00936};
GN OrderedLocusNames=b3019, JW2987;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2170028; DOI=10.1016/0092-8674(90)90172-b;
RA Kato J., Nishimura Y., Imamura R., Niki H., Hiraga S., Suzuki H.;
RT "New topoisomerase essential for chromosome segregation in E. coli.";
RL Cell 63:393-404(1990).
RN [2]
RP ERRATUM OF PUBMED:2170028.
RA Kato J., Nishimura Y., Imamura R., Niki H., Hiraga S., Suzuki H.;
RL Cell 65:1289-1290(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 30-43; 97-113; 201-225 AND 552-564, FUNCTION MODIFIED
RP BY MUKB, AND INTERACTION WITH MUKB.
RX PubMed=20921377; DOI=10.1073/pnas.1008678107;
RA Li Y., Stewart N.K., Berger A.J., Vos S., Schoeffler A.J., Berger J.M.,
RA Chait B.T., Oakley M.G.;
RT "Escherichia coli condensin MukB stimulates topoisomerase IV activity by a
RT direct physical interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18832-18837(2010).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 724-752.
RX PubMed=1557036; DOI=10.1007/bf00280009;
RA Coleman J.;
RT "Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-
RT phosphate acyltransferase (plsC).";
RL Mol. Gen. Genet. 232:295-303(1992).
RN [7]
RP SEQUENCE REVISION, SUBUNIT, AND CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=8227000; DOI=10.1016/s0021-9258(20)80551-1;
RA Peng H., Marians K.J.;
RT "Escherichia coli topoisomerase IV. Purification, characterization, subunit
RT structure, and subunit interactions.";
RL J. Biol. Chem. 268:24481-24490(1993).
RN [8]
RP MUTAGENESIS OF SER-80 AND GLU-84, FUNCTION, ACTIVITY REGULATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=12269820; DOI=10.1021/bi026352v;
RA Hiasa H.;
RT "The Glu-84 of the ParC subunit plays critical roles in both topoisomerase
RT IV-quinolone and topoisomerase IV-DNA interactions.";
RL Biochemistry 41:11779-11785(2002).
RN [9]
RP FUNCTION.
RX PubMed=9334322; DOI=10.1101/gad.11.19.2580;
RA Zechiedrich E.L., Khodursky A.B., Cozzarelli N.R.;
RT "Topoisomerase IV, not gyrase, decatenates products of site-specific
RT recombination in Escherichia coli.";
RL Genes Dev. 11:2580-2592(1997).
RN [10]
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=21300644; DOI=10.1093/nar/gkr018;
RA Pitts S.L., Liou G.F., Mitchenall L.A., Burgin A.B., Maxwell A.,
RA Neuman K.C., Osheroff N.;
RT "Use of divalent metal ions in the DNA cleavage reaction of topoisomerase
RT IV.";
RL Nucleic Acids Res. 39:4808-4817(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-752, FUNCTION, CATALYTIC
RP ACTIVITY, INTERACTION WITH PARE, AND SUBUNIT.
RX PubMed=16023670; DOI=10.1016/j.jmb.2005.06.029;
RA Corbett K.D., Schoeffler A.J., Thomsen N.D., Berger J.M.;
RT "The structural basis for substrate specificity in DNA topoisomerase IV.";
RL J. Mol. Biol. 351:545-561(2005).
CC -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation; it
CC is the principal protein responsible for decatenating newly replicated
CC chromosomes (PubMed:9334322). It relaxes supercoiled DNA
CC (PubMed:12269820, PuMed:16023670, PubMed:21300644). MukB stimulates the
CC relaxation activity of topoisomerase IV and also has a modest effect on
CC decatenation (PubMed:20921377). {ECO:0000269|PubMed:12269820,
CC ECO:0000269|PubMed:16023670, ECO:0000269|PubMed:20921377,
CC ECO:0000269|PubMed:21300644, ECO:0000269|PubMed:9334322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00936,
CC ECO:0000269|PubMed:12269820, ECO:0000269|PubMed:16023670,
CC ECO:0000269|PubMed:21300644};
CC -!- ACTIVITY REGULATION: Inhibited by quinolones.
CC {ECO:0000269|PubMed:12269820}.
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. Interacts with MukB.
CC {ECO:0000255|HAMAP-Rule:MF_00936, ECO:0000269|PubMed:16023670,
CC ECO:0000269|PubMed:20921377, ECO:0000269|PubMed:21300644,
CC ECO:0000269|PubMed:8227000}.
CC -!- INTERACTION:
CC P0AFI2; P22523: mukB; NbExp=11; IntAct=EBI-878544, EBI-542943;
CC P0AFI2; P0A7K2: rplL; NbExp=3; IntAct=EBI-878544, EBI-543702;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00936}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24297.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M58408; AAA24297.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M63491; AAA24396.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69187.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76055.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77075.1; -; Genomic_DNA.
DR EMBL; L22025; AAC36840.1; -; Unassigned_DNA.
DR PIR; A65089; A65089.
DR RefSeq; NP_417491.1; NC_000913.3.
DR RefSeq; WP_001281881.1; NZ_LN832404.1.
DR PDB; 1ZVT; X-ray; 1.70 A; A/B=497-752.
DR PDB; 1ZVU; X-ray; 3.00 A; A=27-742.
DR PDB; 4MN4; X-ray; 2.30 A; A/B=497-752.
DR PDBsum; 1ZVT; -.
DR PDBsum; 1ZVU; -.
DR PDBsum; 4MN4; -.
DR AlphaFoldDB; P0AFI2; -.
DR SMR; P0AFI2; -.
DR BioGRID; 4262365; 18.
DR ComplexPortal; CPX-1104; Topoisomerase IV.
DR DIP; DIP-36030N; -.
DR IntAct; P0AFI2; 24.
DR MINT; P0AFI2; -.
DR STRING; 511145.b3019; -.
DR BindingDB; P0AFI2; -.
DR ChEMBL; CHEMBL1895; -.
DR DrugBank; DB11943; Delafloxacin.
DR DrugBank; DB12924; Ozenoxacin.
DR DrugBank; DB00817; Rosoxacin.
DR DrugCentral; P0AFI2; -.
DR jPOST; P0AFI2; -.
DR PaxDb; P0AFI2; -.
DR PRIDE; P0AFI2; -.
DR EnsemblBacteria; AAC76055; AAC76055; b3019.
DR EnsemblBacteria; BAE77075; BAE77075; BAE77075.
DR GeneID; 66673087; -.
DR GeneID; 947499; -.
DR KEGG; ecj:JW2987; -.
DR KEGG; eco:b3019; -.
DR PATRIC; fig|1411691.4.peg.3711; -.
DR EchoBASE; EB0680; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_6; -.
DR InParanoid; P0AFI2; -.
DR OMA; PRSNRID; -.
DR PhylomeDB; P0AFI2; -.
DR BioCyc; EcoCyc:EG10686-MON; -.
DR EvolutionaryTrace; P0AFI2; -.
DR PRO; PR:P0AFI2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IDA:EcoliWiki.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
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; IDA:EcoliWiki.
DR GO; GO:0006265; P:DNA topological change; IDA:EcoliWiki.
DR GO; GO:0030541; P:plasmid partitioning; IDA:EcoliWiki.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:EcoliWiki.
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; 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 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; DNA-binding;
KW Isomerase; Membrane; Reference proteome; Topoisomerase.
FT CHAIN 1..752
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145397"
FT REGION 472..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..752
FT /note="Sufficient for MukB binding"
FT REGION 718..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 39
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 75
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 77
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 119
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT MUTAGEN 80
FT /note="S->L: Confers resistance to quinolones. No effect on
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:12269820"
FT MUTAGEN 84
FT /note="E->K: Strongly reduced enzyme activity. Increases
FT stability of covalent reaction intermediate with DNA.
FT Confers resistance to quinolones."
FT /evidence="ECO:0000269|PubMed:12269820"
FT MUTAGEN 84
FT /note="E->P: Confers resistance to quinolones."
FT /evidence="ECO:0000269|PubMed:12269820"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1ZVU"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1ZVU"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:1ZVU"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 343..384
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 399..405
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 427..452
FT /evidence="ECO:0007829|PDB:1ZVU"
FT HELIX 454..472
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 508..516
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:4MN4"
FT STRAND 531..538
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:1ZVU"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:1ZVT"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1ZVT"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 593..598
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:1ZVT"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 642..647
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 650..656
FT /evidence="ECO:0007829|PDB:1ZVT"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:1ZVT"
FT HELIX 676..680
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 686..692
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 697..702
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 705..709
FT /evidence="ECO:0007829|PDB:1ZVT"
FT HELIX 711..715
FT /evidence="ECO:0007829|PDB:1ZVT"
FT STRAND 736..740
FT /evidence="ECO:0007829|PDB:1ZVT"
SQ SEQUENCE 752 AA; 83831 MW; 0D4907E96CEE7086 CRC64;
MSDMAERLAL HEFTENAYLN YSMYVIMDRA LPFIGDGLKP VQRRIVYAMS ELGLNASAKF
KKSARTVGDV LGKYHPHGDS ACYEAMVLMA QPFSYRYPLV DGQGNWGAPD DPKSFAAMRY
TESRLSKYSE LLLSELGQGT ADWVPNFDGT LQEPKMLPAR LPNILLNGTT GIAVGMATDI
PPHNLREVAQ AAIALIDQPK TTLDQLLDIV QGPDYPTEAE IITSRAEIRK IYENGRGSVR
MRAVWKKEDG AVVISALPHQ VSGARVLEQI AAQMRNKKLP MVDDLRDESD HENPTRLVIV
PRSNRVDMDQ VMNHLFATTD LEKSYRINLN MIGLDGRPAV KNLLEILSEW LVFRRDTVRR
RLNYRLEKVL KRLHILEGLL VAFLNIDEVI EIIRNEDEPK PALMSRFGLT ETQAEAILEL
KLRHLAKLEE MKIRGEQSEL EKERDQLQGI LASERKMNNL LKKELQADAQ AYGDDRRSPL
QEREEAKAMS EHDMLPSEPV TIVLSQMGWV RSAKGHDIDA PGLNYKAGDS FKAAVKGKSN
QPVVFVDSTG RSYAIDPITL PSARGQGEPL TGKLTLPPGA TVDHMLMESD DQKLLMASDA
GYGFVCTFND LVARNRAGKA LITLPENAHV MPPVVIEDAS DMLLAITQAG RMLMFPVSDL
PQLSKGKGNK IINIPSAEAA RGEDGLAQLY VLPPQSTLTI HVGKRKIKLR PEELQKVTGE
RGRRGTLMRG LQRIDRVEID SPRRASSGDS EE
