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Database: UniProt
Entry: A0A061SUI6_9RHOB
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Original site: A0A061SUI6_9RHOB 
ID   A0A061SUI6_9RHOB        Unreviewed;       767 AA.
AC   A0A061SUI6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=PM02_04080 {ECO:0000313|EMBL:KAJ04622.1};
OS   Sulfitobacter mediterraneus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ04622.1, ECO:0000313|Proteomes:UP000027337};
RN   [1] {ECO:0000313|EMBL:KAJ04622.1, ECO:0000313|Proteomes:UP000027337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ04622.1,
RC   ECO:0000313|Proteomes:UP000027337};
RX   PubMed=24855294;
RA   Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT   "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT   Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT   Mallorca Island (Mediterranean Sea).";
RL   Genome Announc. 2:e00350-14(2014).
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:KAJ04622.1}.
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DR   EMBL; JEMU01000002; KAJ04622.1; -; Genomic_DNA.
DR   RefSeq; WP_037905560.1; NZ_JEMU01000002.1.
DR   AlphaFoldDB; A0A061SUI6; -.
DR   STRING; 83219.PM02_04080; -.
DR   eggNOG; COG0188; Bacteria.
DR   Proteomes; UP000027337; 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   Reference proteome {ECO:0000313|Proteomes:UP000027337};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00936}.
FT   DOMAIN          17..491
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          738..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            48
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            86
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            127
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ   SEQUENCE   767 AA;  85512 MW;  58A9C5EB2D59786A CRC64;
     MSDVTDPPSM DPHNLSEPLR RALGDRYLTY ALSTIMHRAL PDARDGLKPV HRRILYAMRE
     LRLASNGGFR KSAKISGDVM GNYHPHGDAA IYDAMARLAQ DFNVRYPLVD GQGNFGNIDG
     DNPAASRYTE ARMTAVAEAM LEGLTENAVD FRENYDGTLT EPVVLPAQFP NLLANGSSGI
     AVGMATNIPP HNISELCDAC IHLIKTPDAR DDTLLNYVPG PDFPTGGIIV EPPENIATAY
     RTGKGGFRLR CRYEVEDLGR GQWQIVITEI PYQVQKSKLI EKIAEAIQTK KIPILADVRD
     ESADDIRMIL EPRSKNVDPE VLMGMMYRHS DLEVRFSLNM NVLINGVTPK VCSMKEVLRA
     FVDHRREVLQ RRSVHRMEKI DHRLEVLEGF IVAFLNLDRV IDIIRYDDDP KAALMREDWG
     KTHVRAMDEA DYVSPAPGEG ELSEVQADAI LNMRLRSLRR LEELELLREQ SALMEERAGL
     EDLLESEDLQ WTSITEQLRA TKKQFGKDYA GGARRTTFAE AGEVEEVPIE AMIDREPITV
     VCSEMGWIRA MTGHIDLARE LKFKDGDGPR FIFHAETTDR LLVFGSNGRF YTVSASALPG
     GRGMGEPLRL MVDLPNEVQI VRLFIHRPDR KLLVASSAGD GFIVPENDVV AQTRSGKQVL
     NVRGDVTALI CHEVDGDMVA TVGENRKVLV FGLDELPEMG RGKGVRLQKY KDGGLSDATT
     FDSAQGLSWL DPAGRTRTET DLTEWSGKRA SAGRMAPRGF PRDNTFT
//
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