ID A0A1H7HIQ1_9SPHN Unreviewed; 752 AA.
AC A0A1H7HIQ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN05216382_0501 {ECO:0000313|EMBL:SEK48800.1};
OS Sphingomonas palmae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1855283 {ECO:0000313|EMBL:SEK48800.1, ECO:0000313|Proteomes:UP000199214};
RN [1] {ECO:0000313|Proteomes:UP000199214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS21-1 {ECO:0000313|Proteomes:UP000199214};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNZZ01000001; SEK48800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7HIQ1; -.
DR STRING; 1855283.SAMN05216382_0501; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000199214; 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; 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; 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:UP000199214};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 19..471
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 130
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 50
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 88
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 129
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 752 AA; 82826 MW; 08A0623012AE3A27 CRC64;
MPTKITDLPD NPPVGVLDAP FDSALSERYL VYALSTITAR SLPDVRDGLK PVHRRLLWAM
RLLRLDPAAG YKKCARVVGD VIGKYHPHGD QSVYDAMVRL AQDFALRYPL VDGQGNFGNI
DGDNAAAYRY TEARLTQVAI DLMDGLDEDA VEFRPTYNGE EQEPELFPGA FPNLLANGAA
GIAVGMATAI PPHNAAELLD AAVMLVDTPE ASDADVLALV KGPDFPTGGL VVDPQAAITE
AYVTGRGAFR VRARWSVERE KGGTWQIVVS EIPYGVQKGK LIEQIASLIN DKKLPILADV
RDESDAEVRL VLEPRSRTVD AQVLMDGLFR LSDLETRVPL NLNVLDKDRT PRVMSLRDAL
AAWVEHQFVV LRRRTEHRLG KIADRLELVG GYIIAFLNLD RVIEIIRTED EPKAVMIAEF
ALTDRQAEAI LNMRLRSLRR LEEMELKREQ ASLEKEQADL TLLLGSEARQ RTRLKRDFGR
VRARYGPDTP LGHRRTAIEE AAPTRDIPLE AMIEREPITV ILSERGWIRA MKGHVDLSAP
ETMKFKEGDG PAFAFHAQTT DKLLLAAANG RFYTLAADRL PGGRGFGEPV RASIDLDGSV
GIIALFPARG ADRLLLAATD GRGFVVSTAD TVAETRKGKN VMTPRAGATL SVVRAVAADD
DYVAVIGDNR KLLVFPLAEL PAMARGQGVQ LQRYREGGLA DAKTFVFAQG LSWTMRGEAK
RTRTEVDLNA WRTARGAAGR MPPNGFPRDN RF
//
