ID A0A158M767_9BORD Unreviewed; 771 AA.
AC A0A158M767;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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:KAK95983.1};
GN ORFNames=L497_2406 {ECO:0000313|EMBL:KAK95983.1};
OS Bordetella holmesii CDC-H585-BH.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK95983.1, ECO:0000313|Proteomes:UP000026682};
RN [1] {ECO:0000313|EMBL:KAK95983.1, ECO:0000313|Proteomes:UP000026682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK95983.1,
RC ECO:0000313|Proteomes:UP000026682};
RA Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P.,
RA Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J.,
RA Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L.M., Sanka R., Kim M.,
RA Losada L.;
RT "Genome sequence of Bordetella holmseii.";
RL Submitted (MAR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK95983.1}.
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DR EMBL; JFZZ01000045; KAK95983.1; -; Genomic_DNA.
DR RefSeq; WP_005015965.1; NZ_JFZZ01000045.1.
DR AlphaFoldDB; A0A158M767; -.
DR STRING; 35814.BBB42_15060; -.
DR GeneID; 56623732; -.
DR PATRIC; fig|1331206.3.peg.1233; -.
DR Proteomes; UP000026682; 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; 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..493
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
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 771 AA; 84589 MW; 365F6C97B04D32F9 CRC64;
MTDSNQAGLF DAPSGGDDAA ITLGLYAEQA YLDYAVSVVR GRALPDVGDG QKPVQRRILY
AMQAMGLQSG SKPVKSARVV GDVLGKYHPH GDQAAYDAMV RMAQDFSLRY PLIDGQGNFG
SRDGDNAAAM RYTEARLTPI ARLLLDELDE GTVDFVPNYD GSQQEPQMLP ARLPVMLLNG
ASGIAVGMAT EIPSHNLREV AQACVALIRN PKLPDAEILQ IIPGPDFAGG GQIITPATDI
AQIYANGRGS LKARARWQFE EMARGQWQLV VHELPPGTSC QKVLEEIEEL TNPKVKTGKK
ALTPEQQQSK AMMLALLDAV RDESGKDAAV RLVFEPKTSR VDRDEFVNTL LAQTSMESNV
PINLVCIGTD SRPRQKGLRD ILEEWVAFRT DTVLRRTRYR LDKVLDRIHV LEGRMVVYLN
VDEVIQTIRE SDEPRQALMT RFNLTERQAE DILEMRLRQL ARLEGFKIEQ ELADKREEQV
RLQDLLENPS SLKRTLIKEI ESDAKQFGDE RRTLIESAER AVLETKVVDE PVTVIVSCNG
WLRARQGHGH DAGQFSFKQG DDLYGAFECR TTDTLIAVGD NGRVYSVAVS ALPSARGDGQ
PVTTMIDLEA GTRIMHTIAA ATDSRWLLAT RSGYGFATKL SDMSSRQRGG KQFVTLDKGD
ALLRPVPLFE GARQLALLSS KGKLLVFGLD ELKSLSGGGR GTILMGLEAN DPLDQAVPIG
AGGLRAAGIY RNKATEDILV GATLAPYLGK RARKGRALDV RPKQPLLSPV L
//
