ID A0A2T6F8G3_9BURK Unreviewed; 772 AA.
AC A0A2T6F8G3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:PUA19277.1};
GN ORFNames=C7W93_05200 {ECO:0000313|EMBL:PUA19277.1};
OS Glaciimonas sp. PCH181.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Glaciimonas.
OX NCBI_TaxID=2133943 {ECO:0000313|EMBL:PUA19277.1, ECO:0000313|Proteomes:UP000244112};
RN [1] {ECO:0000313|EMBL:PUA19277.1, ECO:0000313|Proteomes:UP000244112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCH181 {ECO:0000313|EMBL:PUA19277.1,
RC ECO:0000313|Proteomes:UP000244112};
RA Kumar V., Thakur V., Kumar S., Singh D.;
RT "Genome analysis of a novel bacterium Glaciimonas sp. PCH181 isolated from
RT glacier stream of Indian trans-Himalaya.";
RL Submitted (MAR-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 -!- 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:PUA19277.1}.
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DR EMBL; PYFP01000001; PUA19277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6F8G3; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000244112; 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_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; 3.
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 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:UP000244112};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 21..493
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 52
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 88
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 90
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 131
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 772 AA; 83931 MW; B79EA64A5712A60F CRC64;
MTEQNDLFDL PPPDGEPNES LTLATFAERA YLDYAISVVK GRALPDVSDG QKPVQRRILF
AMNELGLNAN AKPRKSAAVV GDVLGKLHPH GDQSVYDALV RMAQDFSLRY PLIDGQGNFG
SRDGDGAAAM RYTEARLTPI ARLLLDEIDM GTVDFQPNYD GSTEEPKLLP GRLPFVLLNG
ASGIAVGLAT EIPSHNLTEV AKATVALIRN PNLTHAELME IIPGPDFPGG GQIISSAAAI
SDMYEIGRGS LKVRACWKIE ELARGQWQAV VTELPPNTSS QKVLEEIEEI TNPKIKLGKK
SLTPDQLALK QTILSVLDAV RDESGRDAPV RLVFEPKSKN LDQTEFTNML LAHTSLESSA
SINLVMIGGD GRPRQKGLGM ILREWIQFRF ATITRRSKFK LQKVEDRIHI LEGREAILLN
IDKVIKIIRE SDEPKPALMD AFKLSDRQAE DILEIRLRQL ARLETIKIQQ ELATLRDEKK
GLQDLLENPA SMKKLVIKEI EADQKQFGDA RRTLIEAAEK AVVETKVIDE AVTVIVSQKG
WVRTRGGHGQ DAAQFTFKAG DALYGAFECR TVDNLLVFGS NGRIYSVSVA ALPNARGDGI
PITTLIDLAN GSSILHYFAG AADITLLLAS SGGYGFTAKV GDMLSRVKAG KAYITLEDGD
QSLLPRPIGA NVSAIACLSE KGRLLVFGLD ECKMLTNGGR GVILMELENT EKLLAAQPIS
QRGVLVSGTG RGGKAQDVPL SANGLMPHIG KRARKGKLLE SKLKPLTLTP QG
//
