ID A0A081N0F7_9GAMM Unreviewed; 751 AA.
AC A0A081N0F7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=GZ77_22750 {ECO:0000313|EMBL:KEQ11930.1};
OS Endozoicomonas montiporae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ11930.1, ECO:0000313|Proteomes:UP000028006};
RN [1] {ECO:0000313|EMBL:KEQ11930.1, ECO:0000313|Proteomes:UP000028006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ11930.1,
RC ECO:0000313|Proteomes:UP000028006};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-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:KEQ11930.1}.
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DR EMBL; JOKG01000005; KEQ11930.1; -; Genomic_DNA.
DR RefSeq; WP_034879074.1; NZ_JOKG01000005.1.
DR AlphaFoldDB; A0A081N0F7; -.
DR eggNOG; COG0188; Bacteria.
DR Proteomes; UP000028006; 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; 1.
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:UP000028006};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 14..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 479..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..463
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 479..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 45
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 81
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 83
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 125
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 751 AA; 83621 MW; D946C24804DFB3B5 CRC64;
MEQTVIGDDG IERQSLRAYT ESAYLNYSMY VILDRALPHI GDGLKPVQRR IVYAMSELGL
KNTAKFKKSA RTVGDVLGKF HPHGDSACYE AMVLMAQPFS YRYTLVDGQG NWGSPDDPKS
FAAMRYTESR LTKYSDVLLG ELGQGTVDWV PNFDGTLEEP SILPARLPNL LLNGTTGIAV
GMATDVPPHN LSEVADACVH LLENPKATVA DLVEHIQGPD YPTEAEIITP REDILKMYEQ
GRGSIRMRAV YQKESGDIII TALPHQCSGA KVLEQIAAQM QAKKLPMVAD LRDESDHENP
TRLVIVPKSN RMDVEGLMNH LFATTDLEKT YRVNMNMIGV NGRPQVKSLD RMLTEWLSWR
TDTVRRRLQY RLDKVLARLH LLQGLLVAFL NIDEVIDIIR NEDKPKEALM AKFGLSELQA
DAILEIKLRQ LAKLEEMKIR AEQEELDNER KQLELVLSSE RRLKTLIKKE IIADKEQYGD
ERRSPIEQRQ EARALSETDL MSSEPVTIIL SEKGWVRCAK GHEVDPTTMN YKSGDKYRLS
ARGKSNQSSV FIDSTGRAYS VQTHSLPSAR GQGEPLTGRV NPPSGATFEG LCVGDNSDCY
LMASDAGYGF VVQHGDMVSK NKAGKALLTL PKNARVMLPV PVVGDDQLLA AVTNEGRMLV
FPLSELPKLG RGKGNKIISI ATARAADRVE ILVALAVFSR DDSLVLRAGK RHVKLKPADL
EHYHGERGRR GNKLPRGFQK VDSVEVADDS E
//
