ID A0A2S7JV97_9BURK Unreviewed; 783 AA.
AC A0A2S7JV97;
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:PQA84141.1};
GN ORFNames=C5F52_06805 {ECO:0000313|EMBL:PQA84141.1};
OS Limnohabitans sp. TS-CS-82.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=2094193 {ECO:0000313|EMBL:PQA84141.1, ECO:0000313|Proteomes:UP000238850};
RN [1] {ECO:0000313|EMBL:PQA84141.1, ECO:0000313|Proteomes:UP000238850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TS-CS-82 {ECO:0000313|EMBL:PQA84141.1,
RC ECO:0000313|Proteomes:UP000238850};
RA Shabarova T., Salcher M.;
RT "Limnohabitans TS-CS-82.";
RL Submitted (FEB-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:PQA84141.1}.
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DR EMBL; PTQX01000002; PQA84141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7JV97; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000238850; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 18..497
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 462..492
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 136
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 49
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 92
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 94
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 135
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 783 AA; 85088 MW; C76DE3761F4F4CB0 CRC64;
MTDLLTPELP TADNDGDIAL GHYAQRAYLE YALSVVKGRA LPDVCDGQKP VQRRILYSMS
RMGLGFSGPN NNTGAKPVKC ARVVGDVLGR YHPHGDSAAY EALVRMAQDF AQRYPLIDGQ
GNFGSRDGDG AAAMRYTEAR LAKITTLLLD EIDEGTVDFQ PNYDGSTEEP KQLPARLPFA
LLNGASGIAV GMATEIPSHN LREVADACVA LIKTPKMSDA ELLQILPAPD YPGGGQIISS
ASDIADAYRT GRGSLKVRAR WTIEELARGQ WQLVVNELPP GVSSQRVLEE IEELTNPKVK
TGKKALSADQ TQLKATVLAV LDVVRDESSK DAAVRLVFEP KTRTIEQQEL ITTLLAHTSL
ETSSSINLTM VGIDGRPVPK SLRDMLTEWI EFRSITILRR SQHRLNKVLD RIHILEGRQL
VLLNIDEVIA IIRQSDEPKQ ALMERFRLSE RQAEDILEIR LRQLARLEAI KIEQELKELR
DEQAKLEDIV GNPSALRRLM VKEIEADAKT FADPRRTLIQ EEKKAVAEVK VVDEPVTVVV
SEKGWVRART GHGHEASAFA FKAGDGLYGT FECRTVDTFI AFGSNGRIYS VPVSALPGAR
GDGQPVTTLV DLESGTQLLH YVAGPAGATY LLSSSGGYGF MANIEHMISR NKGGKAFITV
GEGETVCRPS PASGGSGAQP VAPATHVACA STGGRFLTFE LSELKAMEKG GRGLMLIDLE
TKDTLAGAAA YTRSVRIEGI GRGGKVREET LEIRSLNNAK AARAKKGKVA DLGFKPNAVV
RVE
//
