ID A0A0Q6KW86_9SPHN Unreviewed; 748 AA.
AC A0A0Q6KW86;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=ASG67_06865 {ECO:0000313|EMBL:KQU55829.1};
OS Sphingomonas sp. Leaf339.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU55829.1, ECO:0000313|Proteomes:UP000051371};
RN [1] {ECO:0000313|EMBL:KQU55829.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU55829.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU55829.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU55829.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQU55829.1}.
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DR EMBL; LMRS01000012; KQU55829.1; -; Genomic_DNA.
DR RefSeq; WP_056528282.1; NZ_LMRS01000012.1.
DR AlphaFoldDB; A0A0Q6KW86; -.
DR STRING; 1736343.ASG67_06865; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000051371; 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 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:UP000051371};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 17..466
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 128
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 48
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 84
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 86
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 127
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 748 AA; 83149 MW; 18D504600B7B2012 CRC64;
MATDLTGPDT PIGIFDAPFD TALSERYLVY ALSTITARSL PDVRDGLKPV HRRLLWAMRL
LRLDPASGYK KCARVVGDVI GKYHPHGDQS VYDAMVRLAQ DFALRYPLVD GQGNFGNIDG
DNAAAYRYTE ARLTQVAVDL MDGLDENAVN LRPTYNGEEE EPELFPGMFP NLLANGAAGI
AVGMATSIPP HNAAELLDAA MALVDDPMAN VLDHVTGPDF PTGGLVVDPA AVIAESYATG
RGSFRVRARW TLEKEKGGGW QAVISEIPYG VQKGKLIEQI AALINDRKLP ILADIRDESD
AEVRIVLEPR ARTVDVQVMM DGLFRLTDLE TRVPLNLNVL DKERTPRVMS LRDALYAWIE
HQFVVLERRT THRLAKIADR IELLDGYLVA YLNLDRVIEI IRTEDEPKRV MIAEFSLTDR
QAEAILNMRL RSLRKLEEFE IRKERDGLDK ERVDLESLLA DPAKRKRRMK RDLKRIRERY
GPETLLGKRR TTIEEAAPTR DIPLEAMIER EPITVILSQR GWIRAMRGHV DLTASDTLKF
KEGDGPAFAF HAQTTDKLLL AAENGRFFTL AADKLPGGRG FGEPVRAMID LDGSIRVVGF
LPASRQTRLL LVASDGRGFI VPVADTIAET RKGKAVMTPR TGATLKVMRA VLSTDDYVAA
IGDNRKMLVF PIAELVEMTR GQGLQLQRFR DGGLSDAITF RFVDGLSWAM GGESGRTRTE
TDLSAWRAAR GAAGRMPPTG FPRDNRFG
//
