GYRA_THEMA
ID GYRA_THEMA Reviewed; 804 AA.
AC O33926;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 145.
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}; Synonyms=top2A;
GN OrderedLocusNames=TM_1084;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9380682; DOI=10.1073/pnas.94.20.10606;
RA Guipaud O., Marguet E., Noll K.M., Bouthier de la Tour C., Forterre P.;
RT "Both DNA gyrase and reverse gyrase are present in the hyperthermophilic
RT bacterium Thermotoga maritima.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10606-10611(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; U76417; AAB87144.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36161.1; -; Genomic_DNA.
DR PIR; D72297; D72297.
DR RefSeq; NP_228890.1; NC_000853.1.
DR RefSeq; WP_004080399.1; NZ_CP011107.1.
DR AlphaFoldDB; O33926; -.
DR SMR; O33926; -.
DR STRING; 243274.THEMA_08935; -.
DR PRIDE; O33926; -.
DR EnsemblBacteria; AAD36161; AAD36161; TM_1084.
DR KEGG; tma:TM1084; -.
DR eggNOG; COG0188; Bacteria.
DR InParanoid; O33926; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR BRENDA; 5.99.1.3; 6331.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
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..804
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145270"
FT MOTIF 522..528
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT CONFLICT 91
FT /note="Q -> H (in Ref. 1; AAB87144)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="P -> T (in Ref. 1; AAB87144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 804 AA; 90448 MW; 0ED421407D35949F CRC64;
MPEILINKPV EDELVESYLL YSMSVIVGRA IPDVRDGLKP VQRRILYGMY ELGLKHNSPT
KKSARIVGEV MGKYHPHGDA PVYDALVRMA QPFTMRYPLI EGQGNFGSID RDPPAAMRYT
EARLTRLAEE MLEDIEKNTV NMIDNFDGTL KEPEVLPSKV PNLIINGASG IAVGMATNIP
PHNLSETVDA LIYLIDHPEA TVEELMQFIK GPDFPTGAVV VNASELKKVY EEGRGRIIVR
GKVHVEDGKR VKRIVITEIP YGVSKAGLIE QIAKIAKDDE SLPIRNIRDE SDKRGMRIVI
EIPKDANEEV IINNLYKRTA LQDYFNVQML VIDKHKRPRL MNLKGLMEAF LEHRFEVIRR
RARYEYEQYT RRAHVVEGLL KAARAIGVVV DIVRNSKDVE SARQSLMETL EITEEQAKAI
LDMRLSRLTS LEIENLQNEY SDLVRKISEV KEILEKDEKV KEIMKKEFLY LKQQYGDPRR
TEVTDQSIEY NEEELIVEED VVITLSHKGY LKSTPLNSYR SQKRGGKGIT VSKLSEDDEV
EFVVVAKNTS STLFITNLGR AYVLKNYQLE TTGRNTRGRH ITAFLNLEDT EKIVALASLN
GEGRDLVIAT KSGKIKRTAL KEFENATSNR GVRAIKIEPG DEIVSARVVN SEKETLIVAT
KMGMAIRFPV SDVRRMGRNA AGVQAIKLQP GDEVVSVDVI PPGEEGEILT VTEKGFGKRT
PVQLYRIQRR GGTGLRNISD VNKTGYVVAV RYVRGDEEIV VVTRNGMMIR FPVSEIGVIG
RVTKGVKLIE LGDDTISKVA VVKD
