PARC_RICTY
ID PARC_RICTY Reviewed; 737 AA.
AC Q68XU1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
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};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
GN Name=parC {ECO:0000255|HAMAP-Rule:MF_00936}; OrderedLocusNames=RT0065;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00936};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP-
CC Rule:MF_00936}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00936};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00936}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00936}.
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DR EMBL; AE017197; AAU03551.1; -; Genomic_DNA.
DR RefSeq; WP_011190538.1; NC_006142.1.
DR AlphaFoldDB; Q68XU1; -.
DR SMR; Q68XU1; -.
DR STRING; 257363.RT0065; -.
DR EnsemblBacteria; AAU03551; AAU03551; RT0065.
DR KEGG; rty:RT0065; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_4_1_5; -.
DR OMA; PRSNRID; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000604; 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; 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; 3.
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; DNA-binding; Isomerase; Membrane; Topoisomerase.
FT CHAIN 1..737
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000273115"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 40
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 76
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 78
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"
SQ SEQUENCE 737 AA; 83414 MW; CF736359974EBB90 CRC64;
MKEAKIENID FGNALSERYL AYALSTIMSR SLPDVRDGLK PVHRRLLYAM LQLRLEPNSG
YKKCARVVGD VIGKYHPHGD VAVYDTLVRL AQHFSLRYPL IDGQGNFGSI DGDNAAAMRY
TESRMTEICM LLMKDIDKDT VDFRSTYDDS DLEPVIMPAS FPNLLANGSE GIAVGMATNI
PPHNLHELCD ALLYLIDNPQ AGVNDIMNFI KGPDFPTGGI IIDQTKVINA AYTTGRGSFR
VRSRWEKEEL SYGTYQIVVT EIPYQVQKSK LIEQIAILLK DKKIPLISSI RDESTDIIRL
VIEPRDRSCD PQIVMESLFK LTNLESRIQL NMNVIGSNNV PRVMNIVEIL QEFLVHRQNI
ITRRSTYLLN KIKQRLEILK VLKIVYLNLD EIIEIIRRED EPKTIIMERF KISEIQVEVI
LNTRLRALQK LEEHAIIDEH SNLQKQQAIL EKILKNHKEL WKIVKKEIKS VQTQFGLNTI
IGARRTSFEE VDLTNQVIDI TAFITKEPIT IICSKMGWIR LLKGHNTDLS TIKYKEGDAE
KFIIEAYTTD KILIISSKGR FFTLLADNIS KGKGTAVSIK LLVDIGNNDI TNILVYKPYQ
LLLLASSIGK GFLVNSNEVI AQTKAGKQIM NIPEGYACIT CLPVNGNSIA CINESRRLLI
FNINEIPEMK KGQGVVLQRF KNAKLLDIKI FNKEDGLSWN DGKKIQLEKN IVAFLGKRGS
AGTLPPIGFP KNNRFSS