ID A0A0R0LHJ7_9PROT Unreviewed; 778 AA.
AC A0A0R0LHJ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:KRH78714.1};
GN ORFNames=FERRO_17080 {ECO:0000313|EMBL:KRH78714.1};
OS Ferrovum sp. JA12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=1356299 {ECO:0000313|EMBL:KRH78714.1, ECO:0000313|Proteomes:UP000050960};
RN [1] {ECO:0000313|EMBL:KRH78714.1, ECO:0000313|Proteomes:UP000050960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA12 {ECO:0000313|EMBL:KRH78714.1,
RC ECO:0000313|Proteomes:UP000050960};
RA Poehlein A., Ullrich S.R., Tischler J.S., Schloemann M., Muehling M.,
RA Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain JA12.";
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}.
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:KRH78714.1}.
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DR EMBL; LJWX01000002; KRH78714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0LHJ7; -.
DR STRING; 1356299.FERRO_17080; -.
DR PATRIC; fig|1356299.4.peg.1717; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000050960; 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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 31..503
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 468..502
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 142
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 62
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 98
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 100
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 141
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 778 AA; 87096 MW; 131171A03B3EA753 CRC64;
MVKKTHIELD QVSGDLFSHN NPVPQEPEEQ LELSHFIERS YLEYAMSVVM GRAIPDVSDG
QKPVQRRILF AMHELGLYRP NRHVKSARVV GDVIGKYHPH GDSAAYEALV RQAQDFTLRY
PLIDGQGNFG SRDGDGAAAM RYTECRLTPI AELLLSEIDK DTVDFTPNYD GSFKEPKLLP
ARLPFVLLNG SSGIGVGMAT EIPSHNMREV AKAVISLIQK PDTTISQIVR AIKGPDLPGG
GQIISSHSDI LSAYETGRGS LKIRARWSIE ELARGQWRIV VNELPYGVST KDILEDIEKI
SNPKVRDGKK TLTPDQANLK ALILGALDLI RDESDKNSPV RIVIEPKSSR QNPQELMNFL
LVNTRLESSI SINMVMLGVD NKPKQKNIKD ILNEWITFRL NTIVRRTQHR LNEVLRRIHI
LEGRELILLH IDEVIKVIRE SEEPKIELIK HYSLSETQAE DILEIRLRQL AKLEYIKIEK
ELTELRSEKS NLSYLLDNEE ARRELLIHEV NTDAELYGDK RRTLIEFVEE ELIAPTVLDE
AVTVTLSKNG WIKSRQGHAL DASQFSYKSG DHAHCVIESR TIHSLILLDS KGRVYTIKVS
DIPSGRGDGV PVSTLVDLQN GARVIGLMSA LPDVRYLVSS SSGTGFMVKP LDLISRVKAG
KAFMSIEEND YPLFPRLIDK DATHVASLSE KGRLLIFPMS ELKELPKGKG IILMGLDHDE
KLLSSIATNL SRLVILGTNR AGKEVQAQLS GAELKSYIHG RARKGSQIDY KMTVTGFA
//
