ID A0A1B3PI17_9BURK Unreviewed; 785 AA.
AC A0A1B3PI17;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:AOG22397.1};
GN ORFNames=BSY15_2765 {ECO:0000313|EMBL:AOG22397.1};
OS Acidovorax sp. RAC01.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1842533 {ECO:0000313|EMBL:AOG22397.1, ECO:0000313|Proteomes:UP000094760};
RN [1] {ECO:0000313|Proteomes:UP000094760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC01 {ECO:0000313|Proteomes:UP000094760};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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}.
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DR EMBL; CP016447; AOG22397.1; -; Genomic_DNA.
DR RefSeq; WP_069105268.1; NZ_CP016447.1.
DR AlphaFoldDB; A0A1B3PI17; -.
DR STRING; 1842533.BSY15_2765; -.
DR KEGG; acra:BSY15_2765; -.
DR PATRIC; fig|1842533.3.peg.2872; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000094760; Chromosome.
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:UP000094760};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 20..499
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 762..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 464..494
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 138
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 51
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 96
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 137
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 785 AA; 84809 MW; 731889AA159A5C3B CRC64;
MSDQPTLDFT TAGDDGGDSL GLAGYAQRAY LEYALSVVKG RALPDVCDGL KPVQRRILYS
MDRMGLGYSG PTRNTAAKPV KSARVVGDVL GRFHPHGDQS AYDALVRMAQ DFAQRYPLID
GQGNFGSRDG DGAAAMRYTE ARLSRITSLL LDEIDEGTVD FMPNYDGSTQ EPRQLPARLP
FALLNGASGI AVGLATEIPS HNLREIADAC IALIKTPSLS PEDLLAIVPG PDYPGGGQII
SSPGDIADAY RTGRGSLKVR ARWKIEDMAR GQWQLVVTEL PPGVSTQRVL EEIEEITNPK
VKAGKKALSQ DQTQLKASML AVLDVVRDES SKDAPVRLVF EPKTGKTPQQ ELITALLAHT
SLETSAPINL TMVGLDGKPV QKSLRQMLEE WIAFRQTTIT RRSQHRLDKV LDRIHILEGR
QTVLLNIDEV IAIIRAAEEP KAALIARFNL SDRQAEDILE IRLRQLARLE AIKIEQELKE
LRESQGKLED ILNNPGSLRR TMVKEIEADA KTFADPRRTL IQAEKKAVAE VKVVDEPVTV
VVSQKGWVRA RNGHGHEAAS FAFKAGDGLY RTFECRTVDT LLVFGSNGRV YSVPVAALPG
GRGDGQPVTT LIELESGTQL LHYFAGPAQA QLLLASSAGY GFVAAVESMV SRQKGGKAFV
TLGDGETLCA PSHAAGTTGS QPLAPATHVA CASTGGRILT FEISELKTLA NGGRGLMLID
LEPKDTLAGA AAYTRSIRID GIGRGGKERD ETLEIRSLNN ARAPRGRKGK AADLGFKPAT
VTRVE
//
