GYRA_STAAM
ID GYRA_STAAM Reviewed; 889 AA.
AC Q932M0;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=SAV0006;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB56168.1; -; Genomic_DNA.
DR RefSeq; WP_000819068.1; NC_002758.2.
DR AlphaFoldDB; Q932M0; -.
DR SMR; Q932M0; -.
DR BindingDB; Q932M0; -.
DR World-2DPAGE; 0002:Q932M0; -.
DR PaxDb; Q932M0; -.
DR EnsemblBacteria; BAB56168; BAB56168; SAV0006.
DR KEGG; sav:SAV0006; -.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; THHWLLF; -.
DR PhylomeDB; Q932M0; -.
DR BioCyc; SAUR158878:SAV_RS00175-MON; -.
DR Proteomes; UP000002481; 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 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 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW Nucleotide-binding; Topoisomerase.
FT CHAIN 1..889
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145252"
FT REGION 811..889
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 COMPBIAS 862..879
FT /note="Basic and acidic 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"
SQ SEQUENCE 889 AA; 99650 MW; 4A533AA0A1AC4943 CRC64;
MAELPQSRIN ERNITSEMRE SFLDYAMSVI VARALPDVRD GLKPVHRRIL YGLNEQGMTP
DKSYKKSARI VGDVMGKYHP HGDLSIYEAM 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 SDTDKVAMKS LQQRFKLSEK
QAQAILDMRL RRLTGLERDK IEAEYNELLN YISELETILA 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 QQSSDEDEE
