ID A0A1H9SYT3_9LACT Unreviewed; 814 AA.
AC A0A1H9SYT3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN04488559_1104 {ECO:0000313|EMBL:SER90105.1};
OS Isobaculum melis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Isobaculum.
OX NCBI_TaxID=142588 {ECO:0000313|EMBL:SER90105.1, ECO:0000313|Proteomes:UP000198948};
RN [1] {ECO:0000313|EMBL:SER90105.1, ECO:0000313|Proteomes:UP000198948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13760 {ECO:0000313|EMBL:SER90105.1,
RC ECO:0000313|Proteomes:UP000198948};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOHA01000010; SER90105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9SYT3; -.
DR STRING; 142588.SAMN04488559_1104; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000198948; 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; 4.
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:UP000198948};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 11..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 42
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 80
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 91
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 97
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 121
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 814 AA; 92002 MW; D299BE51BC17B33A CRC64;
MDPNRVDVQE LTLEEVMGDR FGRYSKYIIQ ERALPDIRDG LKPVQRRILY AMNMEGNTAE
KGFRKSAKTV GNVIGNYHPH GDTSVYEAMV RMSQDWKLRN VLVEMHGNNG SMDGDPPAAM
RYTEARLSKI ASEMLKDIDK ETVDFVLNFD DTEEEPTVLP AKFPNLLVNG ATGISAGYAT
DIPPHNLGEV IDATTHLLDH PDATFEDLMK FIKGPDFPTG GILQGLDGIK QAYATGKGKV
IVRSKTHIED LRGGKQQIIV TEVPYEVNKS VLVKKLDEVR LNKRIEGIAE VRDESDRTGL
QIAIELKKEA NAAGILNYLL KNTDLQVAYN FNMIAIDDKR PKLIGIVRFL SAYIDHQKQV
ITRRSIYNLK KAEARAHIVE GLIKALSILD KVIATIRESK DKKNAKENLM ESFDFTEKQA
EAIVSLQLYR LTNTDITALE AESAELKALI SSLKEILNSD AVMVDVIKSE LKEVKKQFKT
PRLTVIENEI EELKIETEVL VVQEDVMVSV TSDGYLKRSS LRSYGASKPE EIGAKEGDYP
IFIQQMNTMH HLLMFTNKGN YIYRPVHEIP DLKWKDMGEH ISQTIGLDMD ERIIKVIGLE
KYLPEANFVF VTKAGMVKRT LVTEYLPTRY ISKSAKAMKL KSDDDVLLNI WYVEQPENME
IFLSTYLAYG LRYDLSEVPV VGSKAAGVKA ISLKADDHVI SGIVVPKDEK ASVMILTQRG
SVKKMAIHDF DKQSRAKRGL MILRELKRNP HRVFYMDLVT GKHQLLVQTD KEKEFTINSA
DYSVSDRYSN GSFILDEQED GRPHQVLKSL EQLN
//
