GYRA_STAA8
ID GYRA_STAA8 Reviewed; 887 AA.
AC Q2G2Q0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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};
GN OrderedLocusNames=SAOUHSC_00006;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP MUTAGENESIS OF SER-84 AND GLU-88.
RX PubMed=7492103; DOI=10.1128/aac.39.7.1554;
RA Ferrero L., Cameron B., Crouzet J.;
RT "Analysis of gyrA and grlA mutations in stepwise-selected ciprofloxacin-
RT resistant mutants of Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 39:1554-1558(1995).
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; CP000253; ABD29197.1; -; Genomic_DNA.
DR RefSeq; WP_000819084.1; NZ_LS483365.1.
DR RefSeq; YP_498614.1; NC_007795.1.
DR AlphaFoldDB; Q2G2Q0; -.
DR SMR; Q2G2Q0; -.
DR STRING; 1280.SAXN108_0007; -.
DR EnsemblBacteria; ABD29197; ABD29197; SAOUHSC_00006.
DR GeneID; 3919179; -.
DR KEGG; sao:SAOUHSC_00006; -.
DR PATRIC; fig|93061.5.peg.6; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; THHWLLF; -.
DR PRO; PR:Q2G2Q0; -.
DR Proteomes; UP000008816; 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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..887
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000249333"
FT REGION 811..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 528..534
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 825..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT MUTAGEN 84
FT /note="S->L,A: Resistant to fluoroquinolones."
FT /evidence="ECO:0000269|PubMed:7492103"
FT MUTAGEN 88
FT /note="E->K: Resistant to fluoroquinolones."
FT /evidence="ECO:0000269|PubMed:7492103"
SQ SEQUENCE 887 AA; 99351 MW; B0A5E07EB2506D46 CRC64;
MAELPQSRIN ERNITSEMRE SFLDYAMSVI VARALPDVRD GLKPVHRRIL YGLNEQGMTP
DKSYKKSARI VGDVMGKYHP HGDSSIYEAM VRMAQDFSYR YPLVDGQGNF GSMDGDGAAA
MRYTEARMTK ITLELLRDIN KDTIDFIDNY DGNEREPSVL PARFPNLLAN GASGIAVGMA
TNIPPHNLTE LINGVLSLSK NPDISIAELM EDIEGPDFPT AGLILGKSGI RRAYETGRGS
IQMRSRAVIE ERGGGRQRIV VTEIPFQVNK ARMIEKIAEL VRDKKIDGIT DLRDETSLRT
GVRVVIDVRK DANASVILNN LYKQTPLQTS FGVNMIALVN GRPKLINLKE ALVHYLEHQK
TVVRRRTQYN LRKAKDRAHI LEGLRIALDH IDEIISTIRE SDTDKVAMES LQQRFKLSEK
QAQAILDMRL RRLTGLERDK IEAEYNELLN YISELEAILA DEEVLLQLVR DELTEIRDRF
GDDRRTEIQL GGFEDLEDED LIPEEQIVIT LSHNNYIKRL PVSTYRAQNR GGRGVQGMNT
LEEDFVSQLV TLSTHDHVLF FTNKGRVYKL KGYEVPELSR QSKGIPVVNA IELENDEVIS
TMIAVKDLES EDNFLVFATK RGVVKRSALS NFSRINRNGK IAISFREDDE LIAVRLTSGQ
EDILIGTSHA SLIRFPESTL RPLGRTATGV KGITLREGDE VVGLDVAHAN SVDEVLVVTE
NGYGKRTPVN DYRLSNRGGK GIKTATITER NGNVVCITTV TGEEDLMIVT NAGVIIRLDV
ADISQNGRAA QGVRLIRLGD DQFVSTVAKV KEDAEDETNE DEQSTSTVSE DGTEQQREAV
VNDETPGNAI HTEVIDSEEN DEDGRIEVRQ DFMDRVEEDI QQSSDEE
