ID C3XAH5_OXAFO Unreviewed; 772 AA.
AC C3XAH5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
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:EEO30201.1};
GN ORFNames=OFBG_01229 {ECO:0000313|EMBL:EEO30201.1};
OS Oxalobacter formigenes OXCC13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Oxalobacter.
OX NCBI_TaxID=556269 {ECO:0000313|EMBL:EEO30201.1, ECO:0000313|Proteomes:UP000005089};
RN [1] {ECO:0000313|EMBL:EEO30201.1, ECO:0000313|Proteomes:UP000005089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OXCC13 {ECO:0000313|EMBL:EEO30201.1,
RC ECO:0000313|Proteomes:UP000005089};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allison M.J., Lander E., Nusbaum C., Galagan J.,
RA Birren B.;
RT "The Genome Sequence of Oxalobacter formigenes OXCC13.";
RL Submitted (FEB-2009) 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; GG658170; EEO30201.1; -; Genomic_DNA.
DR RefSeq; WP_005881185.1; NZ_GG658170.1.
DR AlphaFoldDB; C3XAH5; -.
DR STRING; 847.BRW83_0898; -.
DR GeneID; 77134787; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_4_1_4; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000005089; 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; 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:UP000005089};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 21..493
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 458..485
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 52
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 88
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 90
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 131
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 772 AA; 85710 MW; 3C25AF02541D3B66 CRC64;
MTEQPTLFDQ LPPDDEHKES LMLASFAERA YLDYAISVVK GRALPDVCDG QKPVQRRILY
AMNELRLDSE AKPRKSAAVV GDVLGKLHPH GDQSVYDALV RMAQDFSMRY PLIDGHGNFG
SRDGDGAAAM RYTEARLTPI AELLLEEIDQ GTVEFQDNYD GSTQEPKLLP ARLPVTLLNG
ASGIAVGMAT EIPSHNLNEV ATAAVAMIRN PSISHAELME IIPGPDFPGG GQIITAPNTI
SEIYENGRGS VKVRARWKIE ELARGQWQAV VSELPPGTSA QKVLEEIEEI TNPKVRAGKK
ALSAEQVALR QQFLGILDTI RDEASRDAPV RIVLEPKSKR QNPDEFMQML LAHTSLECNA
PVNLVMIGID GRPRQKGLTD IISEWIDFRF ATVTRRTNWR LKRVDDRIHI LEGRETVLLN
IDAVIHIIRE SDEPKAALID AFQLSERQAD DILEIRLRQL ARLEKIRIEQ ELAELRKEKK
GLHDLLDNPS SMKRLIIREI EADRKKYGDA RRTLIEEAER ATAEQKIVDE PVTVIISQNG
WVRQRTGHGL NLSAITFKSG DNLFSSFECR STDFLLAFSS TGRIYTIPVH QLPGGRGDGM
PITTFAEIGI DETIVQYLVS SPDKSVLLSM DSGYGFAAKT SDMMSRVRNG KSFISLEDGE
TLLPPLVIPE ASKSIGVLSE KGRFLLFDAT ELRVLSSGGH GVILMGLDKG EKIRATLPVD
DNGCLVICMA KNDNRYEVRI SGNQIETYTG KRARKGKPVE TRFTPASLEN IK
//
