GYRA_HALWD
ID GYRA_HALWD Reviewed; 856 AA.
AC Q18GY3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=HQ_2651A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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 Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
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 -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
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; AM180088; CAJ52762.1; -; Genomic_DNA.
DR RefSeq; WP_011571878.1; NC_008212.1.
DR AlphaFoldDB; Q18GY3; -.
DR SMR; Q18GY3; -.
DR STRING; 362976.HQ_2651A; -.
DR EnsemblBacteria; CAJ52762; CAJ52762; HQ_2651A.
DR GeneID; 4194090; -.
DR KEGG; hwa:HQ_2651A; -.
DR eggNOG; arCOG04367; Archaea.
DR HOGENOM; CLU_002977_6_1_2; -.
DR OMA; THHWLLF; -.
DR Proteomes; UP000001975; 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:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..856
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409831"
FT REGION 822..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 544..550
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 822..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 856 AA; 95180 MW; 5BEB02305C418688 CRC64;
MSSDAPERFD PETGIAAEVE TARIEREMEQ SYIDYAMSVI AGRALPDARD GLKPVHRRIL
YAMHQSGISA RSAHRKSSSI VGETMGDYHP HGDSAIYNAL ARMAQDFSMR NPLVDGQGNF
GSVDGDPPAA MRYTEARMSP IAEELLDNIE MDTVEFTANY DDRLSEPAVL PAAFPNLLVN
GSSGIAVGMS TNIPPHNLGE VIDATIHLIH HPECTVEDLM NHVQGPDFPT GANIVGQNAI
YKAYKTGRGR VRVRAEFDVQ DDRIVITELP FQTNKARLVE RIADNVNAGT IEGIRDLRDE
SDRDGIRVVV ELKRGANPDI VKNQLLEHHL ESTFGVINLA LVDGQPQVLT LKETLHEYLE
HRRTVVRRRS QYELDEKRDR AHILEGRLRA LEQVDDVVDI IRNSTDRDNA KAALRGEHVV
ESDERGESLP TFDFSEDQAN HIVAMQLGSL TSLESDEIED EYESVQERIE RLQTILNNPD
ELDAVVEDEL ATIRDKYADE RRTRIIEDDG TVTHEDLIAQ EDVVVVVTED DYIKRMSLED
FRSQHRGGKG IIGTSLKDGD TVSSVYVANT HDYLLYFTSH GQVYQLKTYQ IPEMSRTARG
KSAVNLLELD DGEQITAVVN TAEMDIDDDE ERYFTMVTQS GYIKRTSVNS FQNIRSTGII
AISLGADDKL IDVEVTDGNR DIILGTRKGM AIRFNEGDVR SVGRSARGVH GIKLEDTDAV
AALAAVDDDQ DDWVLTVTEH GYGKRTDIDR YRQQSRNGKG LIDIKTNERN GHVCEVETVG
ISDELFMMSR KGQILRTPVD DISTVGRNTM GVIVMDLEDT DTVASVDTHP RTDDSSEADS
GDGESESENA TATTPS
