ID A0A0N0JM36_9PROT Unreviewed; 772 AA.
AC A0A0N0JM36;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ORFNames=D621_04925 {ECO:0000313|EMBL:KPF59196.1};
OS beta proteobacterium AAP51.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523421 {ECO:0000313|EMBL:KPF59196.1, ECO:0000313|Proteomes:UP000037990};
RN [1] {ECO:0000313|EMBL:KPF59196.1, ECO:0000313|Proteomes:UP000037990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP51 {ECO:0000313|EMBL:KPF59196.1,
RC ECO:0000313|Proteomes:UP000037990};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF59196.1}.
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DR EMBL; LJHT01000014; KPF59196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0JM36; -.
DR PATRIC; fig|1523421.3.peg.1017; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000037990; 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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 16..492
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 457..487
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 131
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 47
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 87
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 89
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 130
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 772 AA; 83923 MW; 3C0659D9803DED4A CRC64;
MPDDLFSQPA DPADTLALAD YAERAYLEYA LSVVKGRALP DVCDGNKPVQ RRILYSMFRM
GLAYTGSGGA KPVKSARVVG DVLGRYHPHG DTAAYDALVR MAQNFSQRYP LIDGQGNFGS
RDGDGAAAMR YTEARLAPIA RLLLDEIDEG TIDFQPNYDG STEEPKQLPA RLPFVLLNGA
SGIAVGLATE VPSHNLREVA AASIALLKDE KLSDDELFAL LPAPDFPGGG QIISSTADIR
EAYTTGRGSL KVRARWVIED LARGQWQLVV TELPPQTSTQ KVLEEIEEIT NPKVKAGKKA
LAPEQVQLKA ALLSVLDTVR DESSKDAPVR LVFEPKSRTV EQAELITTLL AHTSLESSVP
MNLTMVGLDG RPVQKGLRKI LMEWIEFRQR TVERRTRHRL GKVLDRIHIL EGRQAVLLNI
DEVIRIIRNS DEPKPALIER FRLSDRQAED ILEIRLRQLA RLESIKIEQE LKELREQQGK
LEDILASPTA LKRTVIKEIE ADAKAHGDER RTLVQAEKKA VAEVKVVDEP VTVVVSTKGW
VRALKGHEVE TATLAFKPGD GLYATFPVRT VDVLLVFGSN GRVYSVAVSL LPGGRGDGVP
ITTLIDLEAG SQIVHYFAGA AVTTLLLANS GGYGLLAQVG DMVGRNRGGK AFLTLEATDK
LLPPVPVATQ PVPHKQVACL AADGRLLVYG LDELKLQPGG GRGLTLMDVD GAAPLLSVAT
VADALKVLGT GRGQKPREEV LKWSALAEHH GKRARKGRVV AGFQKVLQVV AA
//
