ID A0A0R0D9J7_9GAMM Unreviewed; 747 AA.
AC A0A0R0D9J7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=ABB28_06590 {ECO:0000313|EMBL:KRG74759.1};
OS Stenotrophomonas chelatiphaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG74759.1, ECO:0000313|Proteomes:UP000051386};
RN [1] {ECO:0000313|EMBL:KRG74759.1, ECO:0000313|Proteomes:UP000051386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG74759.1,
RC ECO:0000313|Proteomes:UP000051386};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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:KRG74759.1}.
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DR EMBL; LDJK01000020; KRG74759.1; -; Genomic_DNA.
DR RefSeq; WP_057507876.1; NZ_LDJK01000020.1.
DR AlphaFoldDB; A0A0R0D9J7; -.
DR PATRIC; fig|517011.3.peg.939; -.
DR Proteomes; UP000051386; 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 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:UP000051386};
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 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 747 AA; 82125 MW; 49476B0900F8234F CRC64;
MTDLARPVFH GFEQLPLREY AERAYLDYSM YVVLDRALPF LGDGLKPVQR RIIYAMSELG
LNAASKPKKS ARTVGDVIGK YHPHGDSACY EALVLMAQPF SYRYPLIEGQ GNFGSSDDPK
SFAAMRYTES KLTPIAEVLL GELGHGTTDW TPNFDGTLQE PTWMPARLPH LLLNGTTGIA
VGMATDVPPH NLNEIVSALL HLLEDPDASV RDLCEHVKGP DYPSNAEIIT PAADLLHMYE
TGHGSVRARA TFLKENGNVV VNALPFQVSP SKVIEQIAAQ MRAKKLPWIE DVRDESDHAN
PVRVVLVPRS NRVDADQLMG HLFATTDMER SYRVNLNVIG LDGRPQVKNL KTLLSEWLAF
RSSTVTRRLQ HRLQKVERRL HLLEGLLVAF LNLDEVIHII RTEDEPKAAL IARFGLSDDQ
AEYILETKLK QLARLEEMKI RGEQDELAKE RDKILGILDS KAKLKKLIKD ELTADAKKFG
DARRSPLVQR TAAQAIDETE LVPSEPMTVV LSEKGWIRAA KGHDVDASSM NYRDGDSMLA
SVRARSTQQV AFLDSEGRAY STPVHTLPSA RGNGEPLTGR FSPAPGTSFV TLASAEPNGR
FVLASTHGYG FVTRFENLIG RNKAGKAMLN LASGSSVLQP ALVANVDTDR IVAVTSSGNL
LAIAASDLPE LDKGKGNKII EIPKAKLATE RVVAVVAISP GQTLQVRSGQ RTMGLKFSEL
DAYLGSRATR GHLLPRGWQK VEGLSVD
//
