ID A0A0F5JXT6_9BURK Unreviewed; 770 AA.
AC A0A0F5JXT6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=WM40_17250 {ECO:0000313|EMBL:KKB62459.1};
OS Robbsia andropogonis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Robbsia.
OX NCBI_TaxID=28092 {ECO:0000313|EMBL:KKB62459.1, ECO:0000313|Proteomes:UP000033618};
RN [1] {ECO:0000313|EMBL:KKB62459.1, ECO:0000313|Proteomes:UP000033618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP2807 {ECO:0000313|EMBL:KKB62459.1,
RC ECO:0000313|Proteomes:UP000033618};
RA Lopes-Santos L., Castro D.B., Ottoboni L.M., Park D., Weirc B.S.,
RA Destefano S.A.;
RT "Draft Genome Sequence of Burkholderia andropogonis type strain ICMP2807,
RT isolated from Sorghum bicolor.";
RL Submitted (MAR-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:KKB62459.1}.
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DR EMBL; LAQU01000020; KKB62459.1; -; Genomic_DNA.
DR RefSeq; WP_046153529.1; NZ_LAQU01000020.1.
DR AlphaFoldDB; A0A0F5JXT6; -.
DR STRING; 28092.WM40_17250; -.
DR PATRIC; fig|28092.6.peg.4062; -.
DR Proteomes; UP000033618; 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 Reference proteome {ECO:0000313|Proteomes:UP000033618};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 16..488
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 741..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 453..483
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 127
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 83
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 85
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 126
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 770 AA; 84006 MW; AE150F094D78BBFB CRC64;
MEYDTIETPP PDGDALTLGV YAERAYLDYA VSVVKGRALP DVCDGQKPVQ RRILYAMSEM
GLASDAKPVK SARVVGDVLG KYHPHGDQSA YDALVRLAQG FSMRYPLIDG QGNFGSRDGD
GAAAMRYTEA RLTPIAKLLL DEIDMGTVDF MPNYDGSFQE PRLLPARLPF VLLNGASGIA
VGMATEIPSH NLRETAAAAV ALIRNPKMAL DELLALMPGP DFPGGGQIIS SPAEIAAAYE
TGRGSLKVRA RWKIEELARG QWNLVVTELP PNTSGQKVLE EIEDLTNPKI KLGKKALTPE
QLAGKQTILG LLDAVRDESG KDAAVRLVFE PKSSRIDQTE FINTLLAHTS MESNAAINLV
MIGGDGRPRQ KALPEILGEW VAFRQATMTR RTRHRLGKVN DRIHILEGRL IVFLNIDEVI
QTIRESDEPK PALIDRFKLT DRQAEDILEI RLRQLARLER LKIERELSEL SDEKKKLEEL
LGSDSAMRRL MIREIEADAK QYGDDRRTLI QQEKRASAEA RVVDEPVTVI VSARGWVRTQ
KGHGLDSAMF TFKAGDSLYG AFECRTTDNL IAWGNNGRVY STAVAGLPGG RGDGVPVTSL
VDLESGTRLL HYYAAAPERL LLLATSAGYG FLSKLGDLVS RNRSGKSFMT IEGEGDTQPV
PLMPTPVLDG ATEVACLASD GRLLVFGIDE MKTMAGGRGV TLMSLEDGQS LLQSVAFTPV
GLVLQGERGG KPVEAVLNND ALDPHRGKRA KRGKVPANRL KPTGLRPAIR
//
