ID A0A246JK53_9BURK Unreviewed; 783 AA.
AC A0A246JK53;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:OWQ92965.1};
GN ORFNames=CDN99_00170 {ECO:0000313|EMBL:OWQ92965.1};
OS Roseateles aquatilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=431061 {ECO:0000313|EMBL:OWQ92965.1, ECO:0000313|Proteomes:UP000197468};
RN [1] {ECO:0000313|EMBL:OWQ92965.1, ECO:0000313|Proteomes:UP000197468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 48205 {ECO:0000313|EMBL:OWQ92965.1,
RC ECO:0000313|Proteomes:UP000197468};
RX PubMed=18175673; DOI=10.1099/ijs.0.65169-0;
RA Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT "Description of Roseateles aquatilis sp. nov. and Roseateles terrae sp.
RT nov., in the class Betaproteobacteria, and emended description of the genus
RT Roseateles.";
RL Int. J. Syst. Evol. Microbiol. 58:6-11(2008).
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:OWQ92965.1}.
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DR EMBL; NIOF01000001; OWQ92965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246JK53; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000197468; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000197468};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 27..503
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 468..495
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 142
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 58
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 98
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 100
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 141
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 783 AA; 85125 MW; A410B8AEB306A3A6 CRC64;
MNQETFDFET QGGAGGPGGQ SPSGDALTLA QYAQQAYLEY ALSVVKGRAL PAYSDGQKPV
QRRILFTMER MGLVFSGTSG AKAVKSARVV GDVLGKYHPH GDQAAYDALV RMAQDFSQRY
PLVDGQGNFG SRDGDGAAAM RYTEARLSPY ARLLLDELDM GTVDFQPNYD GSFEEPRELP
ARLPFVLLNG ASGIAVGMAT EVPSHNLREV AEAAVLLLKR PDASDDELFD KIKGPDYPGG
GQLISSADEI RAAYNSGRGS LKLRARWKIE DLARGQWQLV VTELPHGVST QKVLEEIEEL
TNPKVKTGKK TVTAEQLQLK GSVLAVLDKA RDESNKDAKV RLVFEPKSRA VEQQELINTL
LAHTSLETSA SMNLTMVGDD GRPMPKTLRK ILTEWIGFRL NTVTRRTQHR LDKVRDRIHI
LEGRHQILLH IDEVIALIRN SDEPKPALIE TFKLSERQAE DILEIRLRQL ARLEFIKIEQ
ELKQLREEAG KLEEILGNPS VLRRTVIKEI EADHKQYGDD RRTLILEDKR AVAEVRIVDE
PVTVVVSLKG WVRALKGHEV DPAALAFKSG DSLYGVFPCR SVDPLVVLGT NGRAYSVPVS
ALPGGRGDGQ PITTLIELES GSQIAHYFAG AATQRLVLAG TGGFGLVAEV GDLVGRQKAG
KSFLSLEGEE RPLPPAVVPA GAVAGVQVAC LTVGGRLLTF AIDELKHQPK GGRGLTLIDL
DAKDLLLSVA AFTTQLLVSG TARGGKPKDE MLKGVSLAAF AGKRAKKGKP ADVMQKPLRL
ITG
//
