PARC_SALTY
ID PARC_SALTY Reviewed; 752 AA.
AC P26973;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
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=STM3174;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1751451;
RA Luttinger A.L., Springer A.L., Schmid M.B.;
RT "A cluster of genes that affects nucleoid segregation in Salmonella
RT typhimurium.";
RL New Biol. 3:687-697(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF PRO-557.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=22916023; DOI=10.1371/journal.pgen.1002845;
RA Rovinskiy N., Agbleke A.A., Chesnokova O., Pang Z., Higgins N.P.;
RT "Rates of gyrase supercoiling and transcription elongation control
RT supercoil density in a bacterial chromosome.";
RL PLoS Genet. 8:E1002845-E1002845(2012).
CC -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It
CC relaxes supercoiled DNA (PubMed:22916023). Performs the decatenation
CC events required during the replication of a circular DNA molecule.
CC {ECO:0000269|PubMed:22916023}.
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; M68936; AAA27180.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22048.1; -; Genomic_DNA.
DR PIR; A45582; A45582.
DR RefSeq; NP_462089.1; NC_003197.2.
DR RefSeq; WP_001281908.1; NC_003197.2.
DR AlphaFoldDB; P26973; -.
DR SMR; P26973; -.
DR STRING; 99287.STM3174; -.
DR PaxDb; P26973; -.
DR PRIDE; P26973; -.
DR EnsemblBacteria; AAL22048; AAL22048; STM3174.
DR GeneID; 1254697; -.
DR KEGG; stm:STM3174; -.
DR PATRIC; fig|99287.12.peg.3365; -.
DR HOGENOM; CLU_002977_6_1_6; -.
DR OMA; PRSNRID; -.
DR PhylomeDB; P26973; -.
DR BioCyc; SENT99287:STM3174-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
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 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 Cell membrane; DNA-binding; Isomerase; Membrane; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..752
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145407"
FT REGION 472..492
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 557
FT /note="P->L: In parC281TS; a temperature-sensitive mutant,
FT no change in growth rate or negative supercoiling at
FT permissive temperature."
FT /evidence="ECO:0000269|PubMed:22916023"
FT CONFLICT 241..242
FT /note="MR -> IG (in Ref. 1; AAA27180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 84038 MW; F34FD7FFD20D6760 CRC64;
MSDMAERLAL HEFTENAYLN YSMYVIMDRA LPFIGDGLKP VQRRIVYAMS ELGLNATAKF
KKSARTVGDV LGKYHPHGDS ACYEAMVLMA QPFSYRYPLV DGQGNWGAPD DPKSFAAMRY
TESRLSKYAE LLLSELGQGT ADWVPNFDGT MQEPKMLPAR LPNILLNGTT GIAVGMATDI
PPHNLREVAK AAITLIEQPK TTLDQLLDIV QGPDYPTEAE IITPRAEIRK IYENGRGSVR
MRAVWTKEDG AVVISALPHQ VSGAKVLEQI AAQMRNKKLP MVDDLRDESD HENPTRLVIV
PRSNRVDMEQ VMNHLFATTD LEKSYRINLN MIGLDGRPAV KNLLEILTEW LAFRRDTVRR
RLNYRLEKVL KRLHILEGLL VAFLNIDEVI EIIRSEDEPK PALMSRFGIS ETQAEAILEL
KLRHLAKLEE MKIRGEQDEL EKERDQLQGI LASERKMNTL LKKELQADAD AYGDDRRSPL
REREEAKAMS EHDMLPSEPV TIVLSQMGWV RSAKGHDIDA PGLNYKAGDS FKAAVKGKSN
QPVVFIDTTG RSYAIDPITL PSARGQGEPL TGKLTLPPGA TVEHMLMEGD DQKLLMASDA
GYGFVCTFND LVARNRAGKT LITLPENAHV MPPLVIEDEH DMLLAITQAG RMLMFPVDSL
PQLSKGKGNK IINIPSAEAA KGDDGLAHLY VLPPQSTLTI HVGKRKIKLR PEELQKVVGE
RGRRGTLMRG LQRIDRIEID SPHRVSHGDS EE
