GYRA_DEIDV
ID GYRA_DEIDV Reviewed; 811 AA.
AC C1CVF4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Deide_12520;
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001114; ACO46171.1; -; Genomic_DNA.
DR RefSeq; WP_012693294.1; NC_012526.1.
DR AlphaFoldDB; C1CVF4; -.
DR SMR; C1CVF4; -.
DR STRING; 546414.Deide_12520; -.
DR PaxDb; C1CVF4; -.
DR EnsemblBacteria; ACO46171; ACO46171; Deide_12520.
DR KEGG; ddr:Deide_12520; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_0; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000002208; 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; IEA:UniProt.
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..811
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409824"
FT MOTIF 520..526
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 811 AA; 89874 MW; 8E5FC7E6CFB4BE5B CRC64;
MTGIHPVDIT SEVKTNFINY AMNVIVDRAL PDVRDGLKPV QRRIMYAMLL EGLYSNQKHA
KSASVVGEVM KKYHPHGDSS IYDAMVRLAQ WWNMRYPMVH PQGNFGSIDG DPPAAMRYTE
ARMTKVAEEL IADLEKETVD LKPNYDETTE EPSVLPAAVP NLLINGATGI AVGMATNIPP
HNLTEICNGL LAMIDDPNLT LDGLMEHVTG PDFPTGGRIT KTGIREAYAT GHSGLKVRGK
ARIEEKNGRN QIIISEIPYQ VNKTNLIQTI SAMYKAGKIP DISALRDESD RKDPVRIVVE
LKRGAIPTLV LNQLYKYTQL QTTYTVINLS IVGGEPRVLP LLNTMQYFLD HRADVVTRRT
RYDLRKAEER AHVLEGLLKA LDHIDEVISL IRGSNTGAEA RDALMVRFGL TEIQSQAILD
MRLQRLVGLE REKLQAEFDE LQKTIEYLRS ILGDEKLLWR EIKKEIRAIR DNYGDERRST
ITELEEDIGK EDLIAVEDMV ITMTKAGYLK RTKLDAYRAQ GRGGRGSSGG KLREEDVNTR
VFVGSTHDYL LFFTDQGRVF HEKIYDLPEA GRDAKGTHIR NLLPSLREDE NIASVLSVGG
FDEPGCFIFA TRKGVVKKTL ITEYGNITSA GLIAINLQPG DELIGVGIVN DIDHVVLATR
NGKAMRFESD EVRATGRATQ GVIGIRLREG EDDAVVSMAL VPGGDEASEL LAVSECGLGK
RTPVGDYPAK GRGGMGVITL DVTEKTGKLV TLARVAGNEE LMVLTEKGTV IRTRVEEVRV
TGRNAQGVKV INIAERDSVI SAFPIRREDE L
