(data stored in SCRATCH3701 zone)

SWISSPROT: 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   11-DEC-2019, entry version 97.
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}.
DR   EMBL; AM180088; CAJ52762.1; -; Genomic_DNA.
DR   RefSeq; WP_011571878.1; NC_008212.1.
DR   SMR; Q18GY3; -.
DR   STRING; 362976.HQ_2651A; -.
DR   PRIDE; Q18GY3; -.
DR   EnsemblBacteria; CAJ52762; CAJ52762; HQ_2651A.
DR   GeneID; 4194090; -.
DR   KEGG; hwa:HQ_2651A; -.
DR   eggNOG; arCOG04367; Archaea.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   BioCyc; HWAL362976:G1G1J-1718-MONOMER; -.
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-dependent 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; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
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;
DR   PRODOM; Q18GY3.
DR   SWISS-2DPAGE; Q18GY3.
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   MOTIF           544..550
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
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
//

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