ID A0A0P1E4V6_9RHOB Unreviewed; 782 AA.
AC A0A0P1E4V6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:CUH43206.1};
GN ORFNames=RUM4293_02099 {ECO:0000313|EMBL:CUH43206.1};
OS Ruegeria atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=81569 {ECO:0000313|EMBL:CUH43206.1, ECO:0000313|Proteomes:UP000050786};
RN [1] {ECO:0000313|EMBL:CUH43206.1, ECO:0000313|Proteomes:UP000050786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4293 {ECO:0000313|EMBL:CUH43206.1,
RC ECO:0000313|Proteomes:UP000050786};
RG Swine Surveillance;
RL Submitted (SEP-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; CYPS01000036; CUH43206.1; -; Genomic_DNA.
DR RefSeq; WP_058273250.1; NZ_CYPS01000036.1.
DR AlphaFoldDB; A0A0P1E4V6; -.
DR Proteomes; UP000050786; 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 PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF1; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 3.
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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 21..495
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 782 AA; 87442 MW; 8B3B50BEA9CB3708 CRC64;
MNDTIDDPNM EAPDNGGEIA EPLRRAIGER YLTYALSTIM HRALPDARDG LKPVHRRILY
AMRELRLSAT GGFRKSAKIS GDVMGNYHPH GDAAIYDAMA RLAQDFNVRY PLVDGQGNFG
NIDGDNPAAS RYTEARMTIV AEALLEGLNE DAVDFRDNYD GTLSEPVVLP AQFPNLLANG
SSGIAVGMAT NIPPHNIAEL CDACLHLIKV PDARDDTLLN YVPGPDFPTG GIIVEPPENI
AQAYRTGRGS FRLRCKYEVE DLGRGQWQII VTEIPYQVQK SKLIEKIAEL IQTKKIPILA
DVRDESADDI RLILEPRSKN VDPEVLMGML YRSSDLEVRF SLNMNVLIDG VTPKVCSMKE
VLRAFLDHRQ EVLLRRSRHR MAKIDHRLEV LEGFIVAFLN LDRVIDIIRY DDDPKAALMR
EDWGIDHIRA TSEADYVSPK PGEGELSEVQ VDAILNMRLR SLRRLEEMEL VRERDALMLE
RANLEDLLAD PALQWAKIAE QLKATKKTFG KDYEGGARRT QFAEAGQVEE VPLEAMIDKE
PITVVCSQMG WIRAMTGHID LKRELKFKDG DGPRFIFHAE TTDRLLVFAS NGRFYTLSAA
NLPGGRGMGE PLRLMVDLPN EAQIIDILIH KPGRKLLVAS DAGNGFMVPE DDVLAQTRNG
KQVLNVKADE TAMICKPVSG DHVAVVSQNG KFLVFPVEEL PEMGRGKGVR LQKYNMARGR
QGTLELDGGL SDITTFNWEE GLRWSMGGDK TRHEADMSQW LAKRASVGKK APYGFPRDYK
FS
//
