ID A0A0R1VY66_9LACO Unreviewed; 825 AA.
AC A0A0R1VY66;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=FC15_GL001244 {ECO:0000313|EMBL:KRM10640.1};
OS Lapidilactobacillus concavus DSM 17758.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lapidilactobacillus.
OX NCBI_TaxID=1423735 {ECO:0000313|EMBL:KRM10640.1, ECO:0000313|Proteomes:UP000051315};
RN [1] {ECO:0000313|EMBL:KRM10640.1, ECO:0000313|Proteomes:UP000051315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17758 {ECO:0000313|EMBL:KRM10640.1,
RC ECO:0000313|Proteomes:UP000051315};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM10640.1}.
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DR EMBL; AZFX01000036; KRM10640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1VY66; -.
DR STRING; 1423735.FC15_GL001244; -.
DR PATRIC; fig|1423735.3.peg.1290; -.
DR Proteomes; UP000051315; 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};
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 Reference proteome {ECO:0000313|Proteomes:UP000051315};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 14..467
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 125
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 45
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 81
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 83
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 94
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 100
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 124
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 825 AA; 92698 MW; 13F303B62127473B CRC64;
MKLMAEDTQK IEELSLETVM GERFSRYSKY IIQERALPDI RDGLKPVQRR ILFAMNQDGN
TYDHAFRKSA KSVGNIMGNF HPHGDSSIYE SMVRMSQDWK LRQPLIEMHG NNGSMDGDPP
AAMRYTEARL SHISTELLRD IDKDTVNMVL NFDDTTEEPT VLPAHFPNLL VNGSSGISAG
YATEIPPHNL GEVIDTVIYL MDHPDATLDE LMKFVPGPDF PTGGILQGID GIKQAYQTGR
GRVVLRSKTA IEELRSQREQ IVITELPYEV NKALLVKKID ELRLMKKVDG ISEVRDETDR
TGLRVVIELK RNADAQGISN YLFKNTDLQI SYNFNMVAIA DLRPQQIGLK QALTAYLAHQ
RDVMTRRTKF DLAKAQKRQH IVEGLIRALS ILDEVIRIIR GSKNKGDAKQ NLMSEYQFSE
IQAEAIVSLQ LYRLTNTDVT ALEAEHHELS DKIAEFQNIL NDAKTLDRVI IKDLKRIKRD
FPGERLTTVE REVESLDIDT SVMVTAEDVQ VMVSHDGYLK RSSLRSFQAT DASDNGLKDE
DYPVFMATVN TLDHLFIFTT KGNLIYRPIH EIDESKWKDM GQHLSQDVGL ASDESVLAAY
VFKDLKQVGQ FVLVTSDGYI KQVAFESLLP GRTYRTRPQQ AIKLKDEASQ VIGMRYLLPD
EATFADTYLF TKNALGIHFS LSEVPVVGAK AAGVKAANLK DDDELVAAIF TTVAEESTDN
AVGILTQRGA FKKMPLSEIP LGNRARRGLL MLRILKRQPH EIVAASLLTP GEQALEVTTD
QNQKVTVTID DVPLNDRYSN GSFILDPEQS GLPIRMTKLE NDAEA
//
