TOP4A_AQUAE
ID TOP4A_AQUAE Reviewed; 769 AA.
AC O67108;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Type 2 topoisomerase subunit A {ECO:0000303|PubMed:21076033};
DE EC=5.6.2.2 {ECO:0000269|PubMed:21076033};
DE AltName: Full=DNA gyrase subunit A;
GN Name=gyrA; OrderedLocusNames=aq_980;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 494-769, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND DOMAIN.
RX PubMed=21076033; DOI=10.1073/pnas.1012938107;
RA Tretter E.M., Lerman J.C., Berger J.M.;
RT "A naturally chimeric type IIA topoisomerase in Aquifex aeolicus highlights
RT an evolutionary path for the emergence of functional paralogs.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22055-22059(2010).
CC -!- FUNCTION: A type II topoisomerase. Despite its similarity to DNA
CC gyrase, this enzyme is not able to supercoil DNA, and instead acts like
CC topoisomerase IV. Relaxes both positively and negatively supercoiled
CC DNA in an ATP-dependent fashion, decatenates interlocked circles. This
CC the first bacteria shown to not contain DNA gyrase, although it has 2
CC copies of a reverse gyrase that introduces positive supercoils. Type II
CC topoisomerases break and join 2 DNA strands simultaneously in an ATP-
CC dependent manner (PubMed:21076033). {ECO:0000269|PubMed:21076033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000269|PubMed:21076033};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius, active between 37 and 90
CC degrees Celsius. {ECO:0000269|PubMed:21076033};
CC -!- SUBUNIT: Heterotetramer, composed of two 'GyrA' and two 'GyrB' chains.
CC In the heterotetramer, 'GyrA' contains the active site tyrosine that
CC forms a transient covalent intermediate with the DNA, while 'GyrB'
CC binds cofactors and catalyzes ATP hydrolysis (PubMed:21076033).
CC {ECO:0000305|PubMed:21076033}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AES4}.
CC -!- DOMAIN: The C-terminal domain (CTD, residues 494-769) contains 6
CC tandemly repeated subdomains known as blades, each of which is composed
CC of a 4-stranded antiparallel beta-sheet. The blades form a flat,
CC toroidal beta-pinwheel fold, to which DNA probably binds. Unlike most
CC CTDs, this organism is missing the canonical GyrA-box. The isolated CTD
CC does not impart writhe, DNA wrapping necessary for supercoil
CC introduction. The ability to supercoil DNA is recovered if the CTD is
CC swapped with the CTD of T.maritima (residues 482-804).
CC {ECO:0000269|PubMed:21076033}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC07064.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE000657; AAC07064.1; ALT_FRAME; Genomic_DNA.
DR PIR; A70385; A70385.
DR RefSeq; NP_213671.1; NC_000918.1.
DR PDB; 3NO0; X-ray; 1.30 A; A/B/C=494-769.
DR PDBsum; 3NO0; -.
DR AlphaFoldDB; O67108; -.
DR SMR; O67108; -.
DR STRING; 224324.aq_980; -.
DR PRIDE; O67108; -.
DR EnsemblBacteria; AAC07064; AAC07064; aq_980.
DR KEGG; aae:aq_980; -.
DR PATRIC; fig|224324.8.peg.771; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_4_1_0; -.
DR InParanoid; O67108; -.
DR OrthoDB; 217468at2; -.
DR EvolutionaryTrace; O67108; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IPI:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 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 Pfam; PF03989; DNA_gyraseA_C; 3.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..769
FT /note="Type 2 topoisomerase subunit A"
FT /id="PRO_0000145219"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AES4"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:3NO0"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:3NO0"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:3NO0"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 583..589
FT /evidence="ECO:0007829|PDB:3NO0"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:3NO0"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:3NO0"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 661..669
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 671..677
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 680..686
FT /evidence="ECO:0007829|PDB:3NO0"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 709..725
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:3NO0"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:3NO0"
FT STRAND 760..768
FT /evidence="ECO:0007829|PDB:3NO0"
SQ SEQUENCE 769 AA; 86996 MW; 2732CEA3A606F5F5 CRC64;
MENRENLVEI PIEEEVKQAY IDYAMSVIVG RAIPDVRDGL KPVQRRILYS MYEMGLLPDK
PFKKSARIVG ETLGKYHPHG DQAVYEALVR MAQDFTMRYP LIIGQGNFGS IDGDPAAQMR
YTEAKLSPLA VEMLTDIDKD TVDFQPNFDD TLMEPEVLPS KFPNLLCNGT SGIAVGLATS
IPPHNLTEVG NALVKLAQNP QISVDEIMEI LKGPDFPTGG VIENFAQVKE IYKTGRGIIK
VKGKAHVEKV QGGRERIVIT EIPYQVNKAE LIKKIADNVR NGKIKEISDI RDETDKEGIR
IVVELKRDAK GEEVLKKLYK YTPLEKGFPV NLVVLIDKEP KLVDIKTLLR EFIKHRLEVI
LRRSKYFLKK VQDRLHIVEG LLKAINFIDD IIERIRRSKD ASEARNYLME EFGLSEKQAQ
AVLDLRLQRL TSLEREKLLE EEKELREKIE YYKKLVASEG ERIKVFIEET EELVKKYGDK
RRTFIGGVKE VKEGSITVAV LQDGSIIPVE ELPLEKAPVV NILRVPFTEG LFLVSNRGRV
YWIAGSQALQ GSKVSLKSRE EKIVGAFIRE KFGNRLLLAT KKGYVKKIPL AEFEYKAQGM
PIIKLTEGDE VVSIASSVDE THILLFTKKG RVARFSVREV PPSTPGARGV QGIKLEKNDE
TSGLRIWNGE PYLLVITAKG RVKKISHEEI PKTNRGVKGT EVSGTKDTLV DLIPIKEEVE
LLITTKNGKA FYDKINQKDI PLSTKKSIPR TRWKLEDDEI IKVVIKKSE
