GYRA_THET8
ID GYRA_THET8 Reviewed; 805 AA.
AC Q5SIL4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=TTHA1355;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11850422; DOI=10.1074/jbc.m111740200;
RA Lamour V., Hoermann L., Jeltsch J.M., Oudet P., Moras D.;
RT "An open conformation of the Thermus thermophilus gyrase B ATP-binding
RT domain.";
RL J. Biol. Chem. 277:18947-18953(2002).
RN [3]
RP FUNCTION, STRUCTURE BY ELECTRON MICROSCOPY (16.8 ANGSTROMS) IN PRESENCE AND
RP ABSENCE OF DNA, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DNA-BINDING.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=23804759; DOI=10.1093/nar/gkt560;
RA Papillon J., Menetret J.F., Batisse C., Helye R., Schultz P., Potier N.,
RA Lamour V.;
RT "Structural insight into negative DNA supercoiling by DNA gyrase, a
RT bacterial type 2A DNA topoisomerase.";
RL Nucleic Acids Res. 41:7815-7827(2013).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state
CC (PubMed:23804759, PubMed:11850422). It probably also catalyzes the
CC interconversion of other topological isomers of double-stranded DNA
CC rings, including catenanes (PubMed:11850422). Relaxes negatively
CC supercoiled DNA in an ATP-independent manner (PubMed:23804759,
CC PubMed:11850422). At comparable concentrations T.thermophilus gyrase
CC does not introduce as many negative supercoils into DNA as the E.coli
CC enzyme (PubMed:23804759). {ECO:0000269|PubMed:11850422,
CC ECO:0000269|PubMed:23804759}.
CC -!- FUNCTION: Negative supercoiling favors strand separation, and DNA
CC replication, transcription, recombination and repair, all of which
CC involve strand separation. Type II topoisomerases break and join 2 DNA
CC strands simultaneously in an ATP-dependent manner.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01897};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius (PubMed:23804759,
CC PubMed:11850422). Active between 25 and 77 degrees Celsius
CC (PubMed:11850422). {ECO:0000269|PubMed:11850422,
CC ECO:0000269|PubMed:23804759};
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
CC (PubMed:23804759). The two subunits form an intertwined dimer where the
CC GyrB ATPase transducer helix of 1 subunit connects to the Toprim domain
CC of the other GyrB subunit through a 10 residue linker
CC (PubMed:23804759). In the heterotetramer, GyrA contains the active site
CC tyrosine that forms a transient covalent intermediate with the DNA,
CC while GyrB binds cofactors and catalyzes ATP hydrolysis.
CC {ECO:0000305|PubMed:23804759}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
CC -!- MISCELLANEOUS: For the electron microscopy studies a GyrB-GyrA fusion
CC protein was made with a Gly-Asp-Leu linker between the 2 subunits. It
CC forms the expected dimer (PubMed:23804759).
CC {ECO:0000269|PubMed:23804759}.
CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC negative supercoils. Not all organisms have 2 type II topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; AP008226; BAD71178.1; -; Genomic_DNA.
DR RefSeq; WP_008632827.1; NC_006461.1.
DR RefSeq; YP_144621.1; NC_006461.1.
DR AlphaFoldDB; Q5SIL4; -.
DR SMR; Q5SIL4; -.
DR STRING; 300852.55772737; -.
DR EnsemblBacteria; BAD71178; BAD71178; BAD71178.
DR GeneID; 3168442; -.
DR KEGG; ttj:TTHA1355; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_0; -.
DR OMA; THHWLLF; -.
DR PhylomeDB; Q5SIL4; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IDA:UniProtKB.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01897; GyrA; 1.
DR InterPro; IPR005743; GyrA.
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; 6.
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 ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..805
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000435480"
FT MOTIF 519..525
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 118
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 805 AA; 89120 MW; 19E04DB23325005D CRC64;
MAQVLPVEIT EELKQSFINY AMSVIVDRAL PDVRDGLKPV QRRILFGAYQ EGVLPGRKHV
KSAKIVGEVM GKYHPHGDAA IYDALVRMAQ PWNLRYPLID GQGNFGSIDG DPPAAQRYTE
ARLSPIGAEM LLDIDKDTVD FRPNYDGSLK EPEVLPAAIP NLLVNGASGI AVGMATSLPP
HNLSEVVDAL VAMIENPAIT LEEVMRHLPG PDFPTGGKLS KKGIKEAYAT GRGSLKVRAK
VRVEEKGQRP VLVVTEIPYQ VNKASLIAQI AALVKAKKIE DIVGLRDESD RQGLRIAIEL
KRGANPQVVL NQLYKHTALQ TSFTVNLLAI VDGEPKVLSL LDLMRHYLDH RKEVVRRRSL
FELRKAEERA HVLEGLLIAL DHIDEVIALI RGSEDAPKAR IALMERFGLS EAQAQAILDM
RLQRLVALER EKLLEEYRGL MEEIARLKAI LEDEARLLAE VKADLLRVKE KYGDARRTLI
TEFEETFNPE DLIEDEPMVI TLTAQGFLKR LPLESYRAQG RGGKGLLAGR TKEEDEATHV
FVADAHDDLL LFTNRGRVYR LKVYELPEMG RQARGVHVKS LLPLAEDEEV AALLSVRGLD
QEGYLVFATE RGLVKRTALK EYQNLGQAGL IAIRLQEGDR LVGVALSDPE DEAILATQEG
QAIRFPLEEV RATGRDTQGV IGVRFKKPED RVVSLVVVKP GEMVDLLSVS TRGYGKRTPL
SEYPLQGRGG MGVITYAVST KVGRLAALLK VRGGEDLLVL SRRGLAIRTP VAEIRQYSRA
TAGVRVMNLP EDDEVASAFV VEEEK
