ID A0A3Q8T837_9RICK Unreviewed; 741 AA.
AC A0A3Q8T837;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00936};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
GN Name=parC {ECO:0000256|HAMAP-Rule:MF_00936,
GN ECO:0000313|EMBL:AZL15892.1};
GN ORFNames=EF513_04955 {ECO:0000313|EMBL:AZL15892.1};
OS Rickettsiales endosymbiont of Stachyamoeba lipophora.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=2486578 {ECO:0000313|EMBL:AZL15892.1, ECO:0000313|Proteomes:UP000267655};
RN [1] {ECO:0000313|EMBL:AZL15892.1, ECO:0000313|Proteomes:UP000267655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RICK01 {ECO:0000313|EMBL:AZL15892.1,
RC ECO:0000313|Proteomes:UP000267655};
RA Munoz-Gomez S.A., Hess S., Burger G., Lang B.F., Susko E., Slamovits C.H.,
RA Roger A.J.;
RT "An updated phylogeny of the Alphaproteobacteria reveals that the parasitic
RT Rickettsiales and Holosporales have independent origins.";
RL Submitted (NOV-2018) 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. {ECO:0000256|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:0000256|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-Rule:MF_00936};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC Rule:MF_00936}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00936}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00936}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP033611; AZL15892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q8T837; -.
DR KEGG; ren:EF513_04955; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000267655; 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; 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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00936};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00936};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW Reference proteome {ECO:0000313|Proteomes:UP000267655};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 12..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 432..477
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 43
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 79
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 81
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 122
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 741 AA; 83773 MW; F528ADC5857AB93F CRC64;
MDPENKETIE NESFSNALSS RYLSYALSTI MSRSLPDVRD GLKPVHRRLL YAMHELKLDP
KSGFKKCARV VGDVIGKFHP HGDAAVYDTL VRLAQDFSLR YPLIEGQGNF GSIDGDNAAA
MRYTESKLTY TSTLLLADLE NETVGFRPNY DGSDQEPEVL PALFPNLLAN GSEGIAVGMA
TSIPPHNILE ICDALIALSH NAEISHEQLT NFIIGPDFPT GGLMYETRQS ITETYKTGKG
SFKIRARWEI ENLSHNMYQI IITEIPYQVN KSRLIEKLAD LLKDKRLALI GNIRDESTED
IRIIIEPKNK GVDAELLMES LYKLTELETR FNLNLNVLDP NLAPRVMSLK EVLSEFLKFR
REIITKRSQF RLRNINDRLE TLAGLLIAHL NIDHVIKIIR ESDEPKAELI KTFSITEKQA
EAILNIRLRS LRKLEEIEIK KEQDSLNSEK QELESILNDT KKLEKVLNKE IKELKTNFEK
NPALSNRRTE IIDQELKVVN INIDAFIEKE PITVIISQKG WLKSLKGHQS EISDNNFKDG
DNVKFILPTH NTEKIIVSSL KGKFFTLNAD KIPSGKGAGE PIRIILDLVP EDDILEIFEY
NPEHKILLAS SNNKGFITEM SNVIAQTKNG KQIADISGED KLIFVQIIKG DMVAVIGQNR
KLLIFPITQI PVMRKGQGVT LQKYKDGNIS DITIFNQQEG LKYGNKTLTD LTPYTGNRAS
VGRMAPLGMP RNNKFRNIRE G
//
