ID Q5KZ51_GEOKA Unreviewed; 814 AA.
AC Q5KZ51;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
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 OrderedLocusNames=GK1750 {ECO:0000313|EMBL:BAD76035.1};
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD76035.1, ECO:0000313|Proteomes:UP000001172};
RN [1] {ECO:0000313|EMBL:BAD76035.1, ECO:0000313|Proteomes:UP000001172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD76035.1,
RC ECO:0000313|Proteomes:UP000001172};
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76035.1; -; Genomic_DNA.
DR RefSeq; WP_011231242.1; NC_006510.1.
DR AlphaFoldDB; Q5KZ51; -.
DR STRING; 235909.GK1750; -.
DR KEGG; gka:GK1750; -.
DR PATRIC; fig|235909.7.peg.1870; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR Proteomes; UP000001172; 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_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; TIGR01063; gyrA; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000001172};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 8..461
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 426..453
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 39
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 75
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 77
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 88
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 118
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 814 AA; 90613 MW; 843446D669075B9A CRC64;
MAERLLEMPL EDVLGDRFGR YSKYIIQDRA LPDARDGLKP VQRRILYAMY IDGNTADKPF
RKAAKTVGNV IGNFHPHGDS SVYEAMVRMS QEWKLRNVLV EMHGNNGSID GDPPAAMRYT
EARLSAIAAE LLRDIDKETV PFVPNFDDTT DEPTVLPAMF PNLLVNGSTG ISAGYATDIP
PHALGEVIDA VLMRIDRPDC TVDELMTVLP GPDFPTGGII QGKDGIRKAY ETGRGKIIIR
AKAAIEQGKG GKKHIVITEL PYEVNKANLV KKIDELRLDK KLDGIADVRD ETDRNGLSIV
IELKKDADAE AILNYLYKNT DLQVPYSFNM VAIHERRPKL MSLPELLDAY IAHRKEVVTN
RSHFELKKAN ERKHIVDGLI RALSILDEVI ATIRASSDKR DAKERLMAHY GFTEAQAEAI
VTLQLYRLTN TDITALRQEA EELDQAIAEL TGILADEKKL LGVIKKELKT MKKQYADERR
TVIEEEIEEL KVKVEALIPA EDVIVTVTKE GYVKRTSYRS YSASNGQDMG MKETDRLLAQ
LEMNTTDVLL LFTRRGYYLY CPVHTLPDIR WKEVGQHISH LIPLERDDEL VAAVPVSSFN
TGEQLVFVTK QGLVKRTELA QYQVQRYTRP LVAVNVKEDD DVIAVYATDG CGHLWLATHD
GHALLFAEEE ISLVGVRAAG VKGIQLKEGD FVAAACPVRL EEGSSFVVVT QRGAVKKVAM
SEFEPSSRAK RGVVIVREVK SNPHRVVGAV FVSSDEEMVG LRTEKGVVET IEAASLRLSD
RYSTGSFVVD TDEAGPVVDV WKEPAKLLGK GEEG
//
