ID A0A1Q8Q2P8_9BACI Unreviewed; 807 AA.
AC A0A1Q8Q2P8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00937};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00937};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00937};
GN Name=parC {ECO:0000256|HAMAP-Rule:MF_00937};
GN ORFNames=BTO30_13940 {ECO:0000313|EMBL:OLN21581.1};
OS Domibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN21581.1, ECO:0000313|Proteomes:UP000185568};
RN [1] {ECO:0000313|EMBL:OLN21581.1, ECO:0000313|Proteomes:UP000185568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XD80 {ECO:0000313|EMBL:OLN21581.1,
RC ECO:0000313|Proteomes:UP000185568};
RA Verma A., Krishnamurthi S.;
RT "Domibacillus antri genome sequencing.";
RL Submitted (DEC-2016) 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_00937}.
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_00937};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC Rule:MF_00937}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00937};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00937}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00937}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLN21581.1}.
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DR EMBL; MSDU01000038; OLN21581.1; -; Genomic_DNA.
DR RefSeq; WP_075399327.1; NZ_MSDU01000038.1.
DR AlphaFoldDB; A0A1Q8Q2P8; -.
DR STRING; 1714264.BTO30_13940; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000185568; Unassembled WGS sequence.
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_00937; ParC_type2; 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; IPR005741; TopoIV_A_Gpos.
DR NCBIfam; TIGR01061; parC_Gpos; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF9; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 5.
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|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00937}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00937};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00937};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00937};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 9..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 427..489
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 40
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 76
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 78
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 89
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 95
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 119
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 807 AA; 90621 MW; 2DF835B2A50CE3D9 CRC64;
MEKEHIQDLP LEDVIGDRFG RYSKYIIQER ALPDARDGLK PVQRRILFSM HTEGNTHQKP
FRKAAKTVGN VIGNYHPHGD SSVYDAMVRL SQDWKMRTPL IEMHGNNGSV DGDPPAAMRY
TETRLSAIAG ELLTDIEKRT VDFIPNFDET TNEPVVLPAR FPNLLVNGST GISAGYATEI
PPHRLDEVID AVIMRMEQPD CTVEQLMTVI KGPDFPTGGI IQGVDGIEKA YKTGKGKIII
RGRAEIESVR GGRQRIVITE IPYEINKASL VKKMDELRVD RKLDGIAEVR DETDRTGLRV
VVDLKKDADA ELILQYLYKV TDLQVSYNFN MVAIYNKRPV LMGLNRLLDA YIEHRKEVVT
NRSEYDLEKA KVRHHIVAGL IKALSILDEV IACIRASKDK QDAKNRLIAE FSFTEAQAEA
IVTLQLYRLT NTDITALERE SEELEKTIQL LESVLASDKK LASVIKRELK ELKKTYATER
RTKIEAEIEE IKIDREAMIP SEDVIVSVTR EGYIKRTGIR SYTASGGLPA MKESDGLLFK
KEMNTTDVLL VFTNKGSYLY LPVHELPDIR WKDAGQHAAG LVNGIKDETI VAAFSIRDFT
KPKYILAVTK AGMVKRTELS QFKVQRYSRP LMAMNVKKDD EVRAVALTDG AFDVLLVTHF
GFGLRFSEEE IPVVGPRAAG VKGISLKEGD YTTAAIVSSE GDSAQFVAVT NRGAVKRSGF
DQFEKSTRAK RGVVMLRELK ANPHRITGAA LIDEHHTYFL RMNKGEDIQI DVQSLKKVDR
YSNGSFVVDE KEQGTVQRLL VTELPAD
//
