ID A0A0A6D0P0_9SPHN Unreviewed; 749 AA.
AC A0A0A6D0P0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=NI18_12160 {ECO:0000313|EMBL:KHA64017.1};
OS Sphingomonas sp. Ant20.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=104605 {ECO:0000313|EMBL:KHA64017.1, ECO:0000313|Proteomes:UP000033201};
RN [1] {ECO:0000313|EMBL:KHA64017.1, ECO:0000313|Proteomes:UP000033201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ant20 {ECO:0000313|EMBL:KHA64017.1,
RC ECO:0000313|Proteomes:UP000033201};
RA Ronca S., Frossard A., Guerrero L.D., Makhalanyane T.P., Aislabie J.M.,
RA Cowan D.A.;
RT "Draft Genome Sequence of Spingomonas sp. strain Ant20, isolated from oil-
RT polluted soil near Scott Base, Antarctica.";
RL Submitted (OCT-2014) 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:KHA64017.1}.
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DR EMBL; JRVI01000085; KHA64017.1; -; Genomic_DNA.
DR RefSeq; WP_037530076.1; NZ_JRVI01000085.1.
DR AlphaFoldDB; A0A0A6D0P0; -.
DR Proteomes; UP000033201; 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; 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:UP000033201};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 15..467
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 729..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 46
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 82
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 125
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 749 AA; 83272 MW; 3746EF2E2D879D44 CRC64;
MVTDFKDPFD SIVDAPFDSA LSERYLVYAL STITARSLPD VRDGMKPVHR RLLWAMRLLK
LDPSQGYKKC ARVVGDVIGK YHPHGDQSVY DAMVRLAQTF SLRYPLVDGQ GNFGNIDGDN
AAAYRYTEAR LTQVAVDLMD GLDEDAANLR PTYNGEDEEP ELFPGMFPNL LANGASGIAV
GMATSIPPHN AAELIEAAIL LVDQPDADND AILAHVTGPD FPTGGLVVDP PAVIRESYAT
GRGGFRVRAR WEIEREKGGM WTLIVSEIPY GVQKGKLIEQ IADLINAKRL PILADVRDES
DAEIRIVLEP RSRTVDPQVL MDGLFRLTDL ETRVSLNLNV LDKDRTPRVM SLREALAAWV
EHQFVVLTRR TQHRLEKIAD RIELLDGYLI AYLNLDRVIE IIRTEDEPKK VMIAEFNLTD
RQAEAILNMR LRSLRRLEEF EIKTERDKLD KEQATLTALL ADPKLQKKRM KADLRKIRDR
YGAETLLGKR RTTIEEAAPT RDIPLEAMIE REPITVILSQ RGWIRAMRGH NDLASPEALK
FKEGDGPAFA FHAQTTDKLL LAAENGRFFT LAADKLPGGR GFGEPVRAMI DLDGSVGIVA
LLPAARQAKL MVAATDGRAF IATAADVIAE TRKGKTVMTP RIGEKVKLVR PVDPADDYVA
AIGDNRKLLV FPINELVEMN RGQGVQLQRY RDGGLADAIT FVFANGLSWA MGGETKRTRT
EADLGPWRTA RGAAGRMPPT GFPRDNRFG
//
