ID   GYRA_NICBE              Reviewed;         935 AA.
AC   Q5YLB5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=DNA gyrase subunit A, chloroplastic/mitochondrial;
DE            EC=5.6.2.2 {ECO:0000250|UniProtKB:P0AES4};
DE   Flags: Precursor;
GN   Name=GYRA;
OS   Nicotiana benthamiana.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15367714; DOI=10.1105/tpc.104.024281;
RA   Cho H.S., Lee S.S., Kim K.D., Hwang I., Lim J.-S., Park Y.-I., Pai H.-S.;
RT   "DNA gyrase is involved in chloroplast nucleoid partitioning.";
RL   Plant Cell 16:2665-2682(2004).
CC   -!- FUNCTION: A type II topoisomerase that seems to play a critical role in
CC       chloroplast nucleoid partitioning by regulating DNA topology. DNA
CC       gyrase negatively supercoils closed circular double-stranded DNA in an
CC       ATP-dependent manner. {ECO:0000269|PubMed:15367714}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000250|UniProtKB:P0AES4};
CC   -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC       breakage and rejoining; the B chain catalyzes ATP hydrolysis.
CC       {ECO:0000250|UniProtKB:Q9CAF6}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:15367714}. Mitochondrion
CC       {ECO:0000269|PubMed:15367714}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15367714}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during seed germination and leaf
CC       expansion. {ECO:0000269|PubMed:15367714}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000250|UniProtKB:P0AES4}.
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DR   EMBL; AY351386; AAR07942.1; -; mRNA.
DR   AlphaFoldDB; Q5YLB5; -.
DR   SMR; Q5YLB5; -.
DR   PRIDE; Q5YLB5; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; DNA-binding; Isomerase; Mitochondrion;
KW   Nucleotide-binding; Plastid; Topoisomerase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast and mitochondrion"
FT   CHAIN           ?..935
FT                   /note="DNA gyrase subunit A, chloroplastic/mitochondrial"
FT                   /id="PRO_0000247946"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           611..617
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000250|UniProtKB:P0AES4"
FT   COMPBIAS        55..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AES4"
SQ   SEQUENCE   935 AA;  103416 MW;  35CD6D27077119ED CRC64;
     MKLHTLNPQT PLTQSKPMAF STGITPSRFS GLRKTSSELR FLSSVTPPPR KQLRPVSARR
     KEEEVGDEGN GSVILRDRGE NEDRNGGERV VLTELHKEAT EAYMSYAMSV LLGRALPDVR
     DGLKPVHRRI LYAMHELGLS SKKPYKKCAR VVGEVLGKFH PHGDTAVYDS LVRMAQDFSL
     RSPLIRGHGN FGSIDADPPA AMRYTECRLE ALTESMLLAD LEQNTVDFVP NFDNSQKEPS
     LLPARVPNLL LNGASGIAVG MATNIPPHNL GELVDALSAL IHNPEATLQE LLEYMPGPDF
     PTGGIIMGNI GILEAFRTGR GRVVIRGKTD IELLDSKTKR AAIIIQEIPY QTNKASLVEK
     IADLVENKIL EGVSDIRDES DRSGMRIVIE LKRGSDPAIV LNNLYRLTAL QSSFSCNMVG
     ILNGQPKLMG LKELLQAFLD FRCSVVERRA RFKLSQAQER NHIVEGIIVG LDNLDEVINT
     IRKASSNALA AASLRKEFEL SEKQAEAILD ISLRRLTALE RNKFVEEGKS LRTQISKLEE
     LLSSKKQILQ LIEEEAIEIK NKFFNPRRSM LEDTDSGDLE DIDVIPNEEM LLAISEKGYV
     KRMKPDTFNL QNRGTIGKSV GKLRVNDAMS DFLVCRAHDK VLYFSDKGTV YSSPAYKIPE
     CSRTAAGTPL VQILSLSDGE RITSIIPVSE FAADQYLVML TVNGYIKKVS LNYFASIRCT
     GIIAIQLVPD DELKWVKCCS NNDFVAMASQ NGMVILTPCA NIRALGRNTR GSVAMRLKEG
     DKVASMDIIP DALQKELDKT LEVQQRQYRS MKGPWLLFVS ESGYGKRVPV SRFRTSPLNR
     VGLFGYKFSS EDCLAAVFVV GFSLGEDGES DEQVVLVSQS GTVNRIKVRD ISIQSRYARG
     VILMRLEHAG KIQSASLISA ADADPEDEDA TAVAA