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   27-MAR-2024, entry version 152.
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; Pseudomonadota; 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, PubMed:16023670, PubMed:21300644). MukB stimulates
CC       the relaxation activity of topoisomerase IV and also has a modest
CC       effect on 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; 511145-b3019; -.
DR   EnsemblBacteria; AAC76055; AAC76055; b3019.
DR   GeneID; 75203584; -.
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; MNVPDGH; -.
DR   OrthoDB; 9806486at2; -.
DR   PhylomeDB; P0AFI2; -.
DR   BioCyc; EcoCyc:EG10686-MONOMER; -.
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; 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.
DR   PROSITE; PS52040; TOPO_IIA; 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   DOMAIN          31..494
FT                   /note="Topo IIA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
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
//