ID A0A3P3VIZ8_9GAMM Unreviewed; 750 AA.
AC A0A3P3VIZ8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:RRJ82334.1};
GN ORFNames=D0544_10635 {ECO:0000313|EMBL:RRJ82334.1};
OS Aestuariirhabdus litorea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Aestuariirhabdaceae; Aestuariirhabdus.
OX NCBI_TaxID=2528527 {ECO:0000313|EMBL:RRJ82334.1, ECO:0000313|Proteomes:UP000280792};
RN [1] {ECO:0000313|EMBL:RRJ82334.1, ECO:0000313|Proteomes:UP000280792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GTF-13 {ECO:0000313|EMBL:RRJ82334.1,
RC ECO:0000313|Proteomes:UP000280792};
RA Khan S.A.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRJ82334.1, ECO:0000313|Proteomes:UP000280792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GTF-13 {ECO:0000313|EMBL:RRJ82334.1,
RC ECO:0000313|Proteomes:UP000280792};
RA Shieh W.Y.;
RT "Simiduia agarivorans gen. nov., sp. nov., a marine, agarolytic bacterium
RT isolated from shallow coastal water from Keelung, Taiwan.";
RL Submitted (DEC-2018) 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:RRJ82334.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QWEZ01000002; RRJ82334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3VIZ8; -.
DR Proteomes; UP000280792; 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:UP000280792};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 15..465
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 432..460
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 127
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 46
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 82
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 84
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 126
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 750 AA; 83707 MW; 75262FBEB1D0CC06 CRC64;
MTDQIIIGDD GVERQSLRDY TRNAYLNYSM YVILDRALPH VGDGLKPVQR RIVYAMSELG
LKNSAKYKKS ARTIGDVLGK FHPHGDSACY EAMVLMAQPF SYRYTLVEGQ GNWGSPDDPK
SFAAMRYTEA KLSTYSEVLL GELGQGTVDW VPNFDGTLDE PATLPARLPN VLLNGGTGIA
VGMATDIPPH NLREVAAACV RLLEEPKATL EQLCEHIKGP DFPTEAELIT PRAELLKMYQ
SGRGSLRMRA VYQRENGDLV ITALPHQVSG AKVLEQIADQ MQKKKLPMVA DLRDESDHEN
PTRLVIVPRS NRIDTEQLMN HLFATTDLER TYRVNLNLIG IDGRPQVKAL DQLLREWLSY
RTETVRRRLQ YRLDKVNKRL HLLDGLLIAF LNLDEVIHII RTEDEPKPVL MERFGLTEVQ
ADYILDTRLR QLARLEEMKI RTEQSELEQE REKLEKILGS EARLKTLIKK EIIADAESYG
DERRSPIVER GEARALDETE LMAAEPVTVV LSKKGWIRSA KGHDVDPAAL SYKSGDEYQL
SVKGRSNQPT VVIDSTGRSY SVTTHSLPSA RGQGEPLTGR LNVPSGASFE GMLIGEERQT
LLMASDAGYG FVTTLGELQS KNRSGKAALS LPKGARVLPP VAITDLSQEL VAAVTNEGRL
LLFPVADLPQ LARGKGNKII NIASARVASR EEFVIDLTVL SPTQTLVLYA GKRHLNLRPS
DLEHYRGERG RRGNKLPRGF QKVDRIEAEG
//