ID A0A1G8Q582_9BACI Unreviewed; 812 AA.
AC A0A1G8Q582;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00937};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00937};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00937};
GN Name=parC {ECO:0000256|HAMAP-Rule:MF_00937};
GN ORFNames=SAMN04490247_0392 {ECO:0000313|EMBL:SDI99625.1};
OS Salimicrobium halophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=86666 {ECO:0000313|EMBL:SDI99625.1, ECO:0000313|Proteomes:UP000199225};
RN [1] {ECO:0000313|EMBL:SDI99625.1, ECO:0000313|Proteomes:UP000199225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4771 {ECO:0000313|EMBL:SDI99625.1,
RC ECO:0000313|Proteomes:UP000199225};
RA de Groot N.N.;
RL Submitted (OCT-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_00937}.
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_00937};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC Rule:MF_00937}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00937};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00937}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00937}.
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DR EMBL; FNEV01000001; SDI99625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8Q582; -.
DR STRING; 86666.SAMN04490247_0392; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000199225; 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_00937; ParC_type2; 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; IPR005741; TopoIV_A_Gpos.
DR NCBIfam; TIGR01061; parC_Gpos; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF9; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 5.
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|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00937}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00937};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00937};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00937};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 10..463
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 428..483
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 41
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 77
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 79
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 90
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 96
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 120
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 812 AA; 91971 MW; D5F811473F2B891C CRC64;
MAETERLLDL PLEEVLGDRF GRYSKYIIQE RALPDARDGL KPVQRRILYA MQQEKNTADK
PYRKSAKTVG TVIGNYHPHG DSSVYEAMVR LSQSWKVRYP LVEMHGNNGS IDGDPPAAMR
YTEARLAGIS TELLRDIQKN TVEHIPNFDD TIEEPTVLPA KFPNLLVNGS TGISAGYATE
IPPHRLEEVI DAVIMRIDSP EASVDKLMTK LPGPDFPTGG IIQGKEGLKE AYENGKGKII
VRGKAEIERI KGGKEQIVID EVPYDVNKAT MVKRMDELRI DKKVEGIAEV RDETDRTGLR
IVIELKKEAN SEGILNYLYK HTDLQVSYSF NMVAISDRSP KLMSLPMILD SYITHQKEVV
TNQANYDLEK AKNRAHIVEG LIKAISILDE VISTIRASKD KSDAKEKLKN AYSFSEAQAE
AIVTLQLYRL TNTDITSLEQ EAEELQQTIK TLEEILADEN KLLKEIKSDL RKIKKEYKDE
RRTVIEEKVE ELKVDLEVTV ASEDVLASVT KDGYVKRTSL RSYTASQEED LPLKEGDHLQ
RLIEINTTDT LLLFTNLGKY LYIPVHKLPD IRWKDLGQHV ANLVPIEVGE KIIEAVPVRH
FDTEDYLVFV TKNGMVKRTM LKEYQAQRHS KPLVAINTKK DDEVVSVQRS GGGKDIMIAS
DKGYCLRFEE NEVNPVGPRA AGVKGIHLKD GEAVVSGQVF DPEEANIVFV VSQRGAVKRM
DLNEFEKGSR ANRGIIVFRE LKKNPHQLVR LLILPKKSVV DIFTERDMLQ VEPFQYRTKD
RYSNGTFVVD TEQNGEVVGA RRKVEYEKPT WE
//
