PARC_SYNY3
ID PARC_SYNY3 Reviewed; 920 AA.
AC P73077; Q59945;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=DNA topoisomerase 4 subunit A;
DE EC=5.6.2.2;
DE AltName: Full=Topoisomerase IV subunit A;
GN Name=parC; OrderedLocusNames=sll1941;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-105.
RA Los D.A., Murata N.;
RL Submitted (OCT-1995) 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 (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2;
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA17102.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000022; BAA17102.1; ALT_INIT; Genomic_DNA.
DR EMBL; U38531; AAA80683.1; -; Genomic_DNA.
DR PIR; S75188; S75188.
DR AlphaFoldDB; P73077; -.
DR SMR; P73077; -.
DR STRING; 1148.1652178; -.
DR PaxDb; P73077; -.
DR EnsemblBacteria; BAA17102; BAA17102; BAA17102.
DR KEGG; syn:sll1941; -.
DR eggNOG; COG0188; Bacteria.
DR InParanoid; P73077; -.
DR OMA; LAGHGNF; -.
DR PhylomeDB; P73077; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
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 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 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; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..920
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145423"
FT REGION 499..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT SITE 45
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 81
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 83
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 124
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="R -> D (in Ref. 2; AAA80683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 920 AA; 101163 MW; B96BF7C8849B0CFE CRC64;
MARKSFPSGQ IIPTDLHEEM ERSYLEYAMS VIVGRALPDV RDGLKPVHRR ILYAMYELGL
TPDRPFRKCA RVVGDVLGKY HPHGDQSVYD ALVRMVQDFS SRYPLLAGHG NFGSVDNDPP
AAMRYTETRL APIAMGAMLE GISEAIVDFT GNFDNSQEEP TVVPAQLPLL LLNGCSGIAV
GMATSIPPHN LGEVVDGLIG LINKPDLSDQ ELFKLIPGPD FPTGGHILDS EGILQAYQTG
RGLIPVRGVS HIETIRGEKK RSHNRTAIVI TELPFQVNKA AWIEKIASLV NDGKLDGISD
LRDESDRTGM RVVIELKRDA EPNAILQKLY RMTPLQSNFG VIFLALVNNQ PVQMSLRQIL
QEFLQFREDT LLRQYENELG ENRRRLELLT GLLIGLENLD ALIEILRFAA DGTTAKIQLQ
ERLGISLQQG DAILGMPMRR ITGLEREKLQ QEHTDLAQRI EQLETLIGDR QERLKALKKE
LRGLKKKFAD ERRTKILQGM PAKIEPLPVN QDPLPEATIP PVESQSAPEE ELDSPGEPEQ
EQLVLENSSP PTADSAPEAK QDDLNLAVKP TPKTVKQEAQ PSPEVIATHS KLVSVAEKNP
LTLFTPQTPP AEAFLSINLQ GEIAWHPEEL TSANSFEPLD QQFSIQGRET LIVIGDHGKA
FPVAIADIPP LAVTRIPLLQ ILPKSAQRDA TTVTFQGFLP PPEQPQDLLL VSQQGRVKLL
AGQELQELGP RGLSLMKLKN GDLLQFAQLV TPVNPASAQN PGKNLVIATS NGRLLRFDPA
QVGLTCSSPS AQGQEAMRLR ATESLVGVLM ASPGDRVLLL TQAGYGKQLD LASVRLGNFG
ELGTTVMQFT SKADRLLTMV AANQGAQSPQ SSTYDFYSNQ QRLHSVQADQ FQPWGKDGFG
DRLVDLNEGE HLITQVAHLG
