ID A0A0U3JQF3_9BURK Unreviewed; 771 AA.
AC A0A0U3JQF3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:ALU88909.1};
GN ORFNames=Hrubri_1704 {ECO:0000313|EMBL:ALU88909.1};
OS Herbaspirillum rubrisubalbicans M1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1078773 {ECO:0000313|EMBL:ALU88909.1, ECO:0000313|Proteomes:UP000069903};
RN [1] {ECO:0000313|EMBL:ALU88909.1, ECO:0000313|Proteomes:UP000069903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ALU88909.1,
RC ECO:0000313|Proteomes:UP000069903};
RA Balsanelli E., Cardoso R.L.A., Cruz L.M., Faoro H., Chubatsu L.S.,
RA Muller-Santos M., Baura V.A., Huergo L.F., Wassem R., Broughton W.,
RA Monteiro R.A., Souza E.M., Pedrosa F.O.;
RT "Herbaspirillum rubrisubalbicans M1 complete genome.";
RL Submitted (DEC-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}.
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DR EMBL; CP013737; ALU88909.1; -; Genomic_DNA.
DR RefSeq; WP_058895061.1; NZ_CP013737.1.
DR AlphaFoldDB; A0A0U3JQF3; -.
DR STRING; 1078773.Hrubri_1704; -.
DR KEGG; hrb:Hrubri_1704; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000069903; 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_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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 20..492
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 457..487
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 131
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 51
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 87
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 89
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 130
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 771 AA; 83987 MW; 21A4FB956E364095 CRC64;
MTDQPTLFDQ VPTAPDGESL TLSTFAERAY LDYAISVVKG RALPDVADGQ KPVQRRILYA
MNELSLNSAA KPRKSAAVVG DVLGKLHPHG DQSVYDALVR MAQDFSLRYP LIDGHGNFGS
RDGDGAAAMR YTEARLTPIS KLLLDEIDMG TVEFQPNYDG STEEPRLLPA RLPFLLLNGA
SGIAVGMATE IPSHNLTEVA KAAVAMIRNP KITHAELMEL IPGPDFPGGG QIITPKSTIA
EMYQSGRGSL KVRARWKIED LARGQWQAVI TELPPGVSSQ RVLEEIEELT NPKLKLGKKS
LTPEQQTQKT TILGLLDAVR DESGREAPVR LVFEPKSKNQ DQTEFMNTLL AQTSLETSAS
LNLVMIGGDG RPRQKNLSDI LTEWISFRFE TVTRRTQFRM QKVNDRIHIL EGREAVLLNI
DKVIKIIRES DEPKPALIDA FKLSERQAED ILEIRLRQLA RLEAIKIQQE LAELRNEKTT
LQDLLDNPAS MKKLVIKEIE GDAKTYGDAR RTIIEEAERA TFEQKVIDEP VTVIISQKGW
VRARTGHGHD ATQFTFKAGD SLYGAFECRT VDNLLAFGSN GRVYTIAVNA LPNARGDGVP
VTTLIELASG SSIQHYFAGP ADTTLLLASD AAAGFIAKAS DMFGRVKGGK SFFTLDEGAL
PLAPTPVAAD ASAVACVSAN GRLLVFGLDE MKTLSSGGRG VNLMELEKNE KLVAAQAISQ
KGVVVYGTGN VGKAKEIPLS GEKLLAHVGK RARKGRVLES RIKAAGLRSQ G
//
