ID W0GPI3_9MOLU Unreviewed; 1039 AA.
AC W0GPI3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=P344_03385 {ECO:0000313|EMBL:AHI58020.1};
OS Spiroplasma mirum ATCC 29335.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=838561 {ECO:0000313|EMBL:AHI58020.1, ECO:0000313|Proteomes:UP000019260};
RN [1] {ECO:0000313|EMBL:AHI58020.1, ECO:0000313|Proteomes:UP000019260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMCA {ECO:0000313|EMBL:AHI58020.1,
RC ECO:0000313|Proteomes:UP000019260};
RA Landry C.A., Bastian F.O., Thune R.L.;
RT "Complete genome sequence of Spiroplasma mirum suckling mouse cataract
RT agent.";
RL Submitted (SEP-2013) 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; CP006720; AHI58020.1; -; Genomic_DNA.
DR RefSeq; WP_025317359.1; NZ_CP006720.1.
DR AlphaFoldDB; W0GPI3; -.
DR STRING; 838561.P344_03385; -.
DR KEGG; smia:P344_03385; -.
DR KEGG; smir:SMM_0573; -.
DR PATRIC; fig|838561.3.peg.658; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_0_0_14; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000019260; 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_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; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000019260};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 13..461
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 804..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 433..474
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 804..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 44
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 80
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 82
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 93
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 99
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 123
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 1039 AA; 116922 MW; 74D49C0FF8D9A49D CRC64;
MSNQKQTDNE LVYTLNDIMD DRFARYAKYI IQERALPDVR DGLKPVQRRI LFAMNELRLT
FNSSYKKSAR IVGEVIGKYH PHGDTSVYDA MVRLSQSWKV RYPLIDMHGN NGSIDGDHAA
AMRYTETRLS EIAGFLLQDL DKETVLFAPN FDDSETEPTI LPAMFPNLLI NGATGIAAGY
ATNIPPHNLQ EVINVTIHRI KNPDSKLNEL TKYIKGPDFP TGGIIQGKTG ILDAYRTGRG
KIIIRSKIEN EDNNIVITEI PYEVVKQDLV KKIDDIKYNE PGLNIKEVRD ETDRTGLRIV
VELSKQANYD TVRKYLLKNT NLQVSYNFNV VAIANKQPKL LGLKELIDYY IAHQKEVITN
RSKFELAKAQ KREEIVEGLI KAVSILDEII AIIRHSKDRT DAINNLCTKF KFTQVQAEAI
VQLRLYRLTS TDILQLQKEQ QELANLIKNL QVILAQEEKL LAVIVEQLEL IKNKFPSPRK
SVIENDIELI EIEKTETIIE KDVNIWVSRD GYLKSLDNSQ IAKITANEFN RKPLDLWVAN
FSANTLDKIL LITSKGNYVI IPVYKIKMSK IKDIGEHVNT ISELPGEEKI IASYLLDSFN
KPNVAIMIAT KNGMIKKVSV PDFEATRISK AIKAINLKAD DEVVASQLVK DEQYVSIFTK
NGFVVKYKQQ EIPSLGLRTS GVKSINLKED EVVGAGYGQK ENLIFITDQN MVKKIALKEL
PVSTRPIKGT RLFKLNKKLD QLIKWGFIIN KKETLNILHP NDKIEMFNVD KIALQELDAP
LETLGIENID EITIPKYYNL KELPTSETPP TNDNSNSVAK DPAVIKVIKK PNAAPTRKGA
AKSTKIKAKQ QKQKLSAKSK PQEAPVISSS AVQQPVEKIA ISKTGTTQSN SPTSQPSENS
EINTDVSKSL STNNKTSKES TKVMKPTQSP ELINKKSLAE KKNPTEVKNI KPEQQPNNAG
SSTPKVDIRQ AKTTVELLIE QKQQKVSSGG STPEMTTGEF QAQPNEKVDK NKFKHDLAVE
ETKELQININ DILKNNDDQ
//
