ID A0A1M5J3T4_9BURK Unreviewed; 773 AA.
AC A0A1M5J3T4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ORFNames=SAMN05428948_0039 {ECO:0000313|EMBL:SHG35288.1};
OS Massilia sp. CF038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1881045 {ECO:0000313|EMBL:SHG35288.1, ECO:0000313|Proteomes:UP000184361};
RN [1] {ECO:0000313|EMBL:SHG35288.1, ECO:0000313|Proteomes:UP000184361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF038 {ECO:0000313|EMBL:SHG35288.1,
RC ECO:0000313|Proteomes:UP000184361};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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_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; FQWU01000001; SHG35288.1; -; Genomic_DNA.
DR RefSeq; WP_073212090.1; NZ_FQWU01000001.1.
DR AlphaFoldDB; A0A1M5J3T4; -.
DR STRING; 1881045.SAMN05428948_0039; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000184361; 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:UP000184361};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 22..494
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 459..489
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 133
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 53
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 91
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 132
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 773 AA; 84055 MW; FEADF8C812281DFB CRC64;
MTNQTDLFAE PPPPPPEDGD TLTLSTFAER AYLDYAVSVV KGRALPDVSD GQKPVQRRIL
FQMNELGLGA TAKPRKSAAV VGDVMGKLHP HGDQSIYDAL VRMAQDFSLR YPLVDGQGNF
GSRDGDGAAA MRYTEARLTP IARVLMEEID EGTVDFQPNY DGAHNEPKAL PARLPMVLLN
GASGIAVGLA TEIPSHNLTE VAQAAVAMIR NPKITHAELM AFMPGPDFPG GGQIITPQSQ
IADMYTSGRG SMKVRARWKI EELARGQWQA VVYELPPGCS SQKVLEEIEE LTNPKIKLGK
KSLSPEQLAM KQNILGSLDK VRDESGREAP VRLVFEPKSK NQDQNEFMLM LLAHTSLESS
NSINLVMIGG DGRPRQKGLT EILQEWIEFR FVTVRRRTEF RLGKVNARIH ILEGRMTVLL
NIDKVIHIIR NSDDPKAALI AEFDLTDIQA EDILEIRLRQ LARLEAIKIE KELGELRKEK
ETLQDLLDNP SSMKRLIIRE IESDAKTFGD ARRTIIEEAA RATAEQKVID EPVTVIVSEK
GWVRARTGIG HDVTQFTFKA GDSLHNAFEC RTVDTLLAFG DNGKVYSVPV SALPGARGDG
VPMTTLVDLS GGVRLLHFFA GSAATNLMLA SSAGYGFAAK AGDMVSRLKG GKSFITLDEG
AVPLTPRVIA TGASAIACLS EKGRLLVFGM DELKTLTNGG RGVTLMELEA KEKLAAVQPI
TQKGVTVVGT WAGGKPREVD LSASGLAVHF GKRARKGKAL EAKVKALALK AIV
//
