PARC_CAUVC
ID PARC_CAUVC Reviewed; 759 AA.
AC O54478;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=CC_1566;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=9426128; DOI=10.1046/j.1365-2958.1997.6242005.x;
RA Ward D.V., Newton A.;
RT "Requirement of topoisomerase IV parC and parE genes for cell cycle
RT progression and developmental regulation in Caulobacter crescentus.";
RL Mol. Microbiol. 26:897-910(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RA Ward D.V., Newton A.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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.
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; U94696; AAC38043.1; -; Genomic_DNA.
DR EMBL; U86302; AAF14339.1; -; Genomic_DNA.
DR EMBL; AE005673; AAK23545.1; -; Genomic_DNA.
DR PIR; E87443; E87443.
DR RefSeq; NP_420377.1; NC_002696.2.
DR RefSeq; WP_010919440.1; NC_002696.2.
DR AlphaFoldDB; O54478; -.
DR SMR; O54478; -.
DR STRING; 190650.CC_1566; -.
DR PRIDE; O54478; -.
DR EnsemblBacteria; AAK23545; AAK23545; CC_1566.
DR KEGG; ccr:CC_1566; -.
DR PATRIC; fig|190650.5.peg.1594; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_4_1_5; -.
DR OMA; PRSNRID; -.
DR BioCyc; CAULO:CC1566-MON; -.
DR Proteomes; UP000001816; 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; 2.
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; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..759
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145396"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 52
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 88
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 90
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 131
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT CONFLICT 498
FT /note="R -> A (in Ref. 1; AAC38043 and 2; AAF14339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 83521 MW; 65DDA34154A347D4 CRC64;
MNKPVLPPPG GPDDGDRILD EPLTEALSRR YLAYALSTIG SRALPDVRDG LKPVHRRVLY
AMSNMRLNPD AAARKCAKVV GEVMGNFHPH GDASIYDALV RLAQEFSQRI PLVEGQGNFG
NIDGDSAAAM RYTECKMTEA AMLLLDGIDE DAVDFRPTYD GQDEEPVVLP SGFPNLLANG
SSGIAVGMAT SIPPHNAAEL IDACQLLLAN PDATTADLLE KVPGPDFPTG GVIVESRASL
LETYETGRGG VRMRAKWEKE DTGRGTYQIV VTEIPYQVKK SDLVEQLADL IDSKKAALLG
DVRDESAEDI RLVLEPKSKN VEPEVLMESL FKLSALESRF PVNINVLDAR GTPGVMGIKQ
ALMAFLAHRR EVLTRRARHR LAKIEARLHI LDGLLIAYLN LDEVIRIVRY EDKPKEKLIE
TFGLTDIQAD AILNTRLRQL AKLEEMEIRR EHAELVEERD GILAMLASEA KQWKLVGVGL
SEVRAALLKI KHPLDKPRPT GVTGRSVFGE APQVDADAAI EAMIVREPIT IILSERGWIR
AAKGKIDDPS ELKFKEGDKL GFLVPAETTD KLLIFSSDGR FFTLGCDKLP SARGHGEPVR
MMIELDDKVK IIDVFPFKAG RKRILASKGG YGFLMPEEEA LANRKAGKQV LNVGNEGAAF
CLEAVGDQLA VIGDNGKILI FPLEELPEMP RGKGVKLQAY REGGLRDGLS FNAETGAYWI
DTAGRRRDWA EWKEWVGRRA GAGKLVPKGF ATNKRFRPK
