ID A0A1C2I2U5_ACITH Unreviewed; 780 AA.
AC A0A1C2I2U5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=A6P07_15095 {ECO:0000313|EMBL:OCX70314.1};
OS Acidithiobacillus thiooxidans (Thiobacillus thiooxidans).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=930 {ECO:0000313|EMBL:OCX70314.1, ECO:0000313|Proteomes:UP000094893};
RN [1] {ECO:0000313|EMBL:OCX70314.1, ECO:0000313|Proteomes:UP000094893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A02 {ECO:0000313|EMBL:OCX70314.1,
RC ECO:0000313|Proteomes:UP000094893};
RA Zhang X., Feng X., Tao J., Ma L., Xiao Y., Liang Y., Liu X., Yin H.;
RT "Comparative genomics of the extreme acidophile Acidithiobacillus
RT thiooxidans reveals intraspecific divergence and niche adaptation.";
RL Int. J. Mol. Sci. 0:0-0(2016).
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:OCX70314.1}.
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DR EMBL; LWSA01000202; OCX70314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C2I2U5; -.
DR eggNOG; COG0188; Bacteria.
DR Proteomes; UP000094893; 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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 45..519
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 76
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 112
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 114
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 155
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 780 AA; 85430 MW; 59C87F1EA713E743 CRC64;
MFRKESRMSN TLDLFDGLSP EHASSPPNEP PLPTAEGGNP EDPSPPLAEY AAKAYLAYAM
SVVTGRAIPA LADGQKPVQR RILYAMRDMG LQRSPKHVKS ARVVGEVIGK WHPHGDSSVY
DAMVRMAQHF TLRYPVVDGQ GNFGSLDGDS AAAMRYTEAN LTPISELLLG EIDEGTVDFR
SNYDGTLEEP VTLPARLPFL LMNGASGIAV GMATEIPPHN LRELAAVCAQ LAANPETSND
AILAQIPGPD FPGGGQIISP PEQIREAYLS GRGSIRVRAR WEVEKLARGE WRISIHELPP
GVSTAQVLSE IENLSNPQPR GEGKKKALTP EQQSTKTAML SQIDTVRDES GKDHAVRIVV
EPRSRNQDPQ QLMTYLLART SLESNQSVNL TVLDLEGRAP CLPLTAILRQ WVTYRLRTVR
RRSQFRLDKT LARIHILEGR LRVLLDIDAV IRVIRESDDP KIDLIQHFAL TEIQAEDILE
IRLRQLARLA GIELEKELKD KRDVADYLAG LLAHEDRLRA LLVEEINADA QKFGDDRRTL
LEADVAITSK SAQTIVAAVT DEPVTVIVSR KGWLRSRAGH GIATESLNFK EGDQLLQVFE
VRSVDHLVLL DQTGRAYSVP VSQIPGGRGD GVPASSQVDF QPGASLQSAA CGPADSLWLV
ASSGAYGFVT ALENMAGRNR AGKAFLSLDK DEYPLPLLPV SDLSAEILCV SSDYAGLIFP
LAEIKSLPKG KGVKLMTLAP QAHLQSLYTH PEGQTLPRPI RKNRLEICRG KRAGKGRSLR
//
