GYRA_STAAN
ID GYRA_STAAN Reviewed; 889 AA.
AC Q99XG5;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=SA0006;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB41222.1; -; Genomic_DNA.
DR PIR; F89758; F89758.
DR RefSeq; WP_000819096.1; NC_002745.2.
DR PDB; 2XCO; X-ray; 3.10 A; A=2-491.
DR PDB; 2XCQ; X-ray; 2.98 A; A=2-491.
DR PDB; 2XCR; X-ray; 3.50 A; B/D/S/U=2-491.
DR PDB; 2XCS; X-ray; 2.10 A; B/D=2-491.
DR PDB; 2XCT; X-ray; 3.35 A; B/D/S/U=2-491.
DR PDB; 4BUL; X-ray; 2.60 A; A/C=2-491.
DR PDB; 5CDM; X-ray; 2.50 A; A/C=9-490.
DR PDB; 5CDN; X-ray; 2.79 A; A/C/R/T=10-490.
DR PDB; 5CDO; X-ray; 3.15 A; A/C/R/T=9-490.
DR PDB; 5CDP; X-ray; 2.45 A; A/C=9-491.
DR PDB; 5CDQ; X-ray; 2.95 A; A/C/R/T=10-490.
DR PDB; 5CDR; X-ray; 2.65 A; A/C=9-491.
DR PDB; 5IWI; X-ray; 1.98 A; A/C=2-491.
DR PDB; 5IWM; X-ray; 2.50 A; A/C=2-491.
DR PDB; 5NPK; X-ray; 1.98 A; B/D/b/d=2-491.
DR PDB; 5NPP; X-ray; 2.22 A; B/D=2-491.
DR PDB; 6FM4; X-ray; 2.70 A; B/D=2-491.
DR PDB; 6FQM; X-ray; 3.06 A; A/C/a/c=2-491.
DR PDB; 6FQS; X-ray; 3.11 A; A/C=2-491.
DR PDB; 6FQV; X-ray; 2.60 A; A/C/R/T=2-491.
DR PDB; 6QTK; X-ray; 2.31 A; A/C=2-491.
DR PDB; 6QTP; X-ray; 2.37 A; A/C=2-491.
DR PDB; 6QX1; X-ray; 2.65 A; A/C=2-491.
DR PDB; 7MVS; X-ray; 2.60 A; A/B=2-491.
DR PDBsum; 2XCO; -.
DR PDBsum; 2XCQ; -.
DR PDBsum; 2XCR; -.
DR PDBsum; 2XCS; -.
DR PDBsum; 2XCT; -.
DR PDBsum; 4BUL; -.
DR PDBsum; 5CDM; -.
DR PDBsum; 5CDN; -.
DR PDBsum; 5CDO; -.
DR PDBsum; 5CDP; -.
DR PDBsum; 5CDQ; -.
DR PDBsum; 5CDR; -.
DR PDBsum; 5IWI; -.
DR PDBsum; 5IWM; -.
DR PDBsum; 5NPK; -.
DR PDBsum; 5NPP; -.
DR PDBsum; 6FM4; -.
DR PDBsum; 6FQM; -.
DR PDBsum; 6FQS; -.
DR PDBsum; 6FQV; -.
DR PDBsum; 6QTK; -.
DR PDBsum; 6QTP; -.
DR PDBsum; 6QX1; -.
DR PDBsum; 7MVS; -.
DR AlphaFoldDB; Q99XG5; -.
DR SMR; Q99XG5; -.
DR EnsemblBacteria; BAB41222; BAB41222; BAB41222.
DR KEGG; sau:SA0006; -.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; THHWLLF; -.
DR BRENDA; 5.6.2.2; 3352.
DR EvolutionaryTrace; Q99XG5; -.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding;
KW Isomerase; Nucleotide-binding; Topoisomerase.
FT CHAIN 1..889
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145253"
FT REGION 810..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"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 14..32
FT /evidence="ECO:0007829|PDB:5IWI"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5CDM"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:5IWI"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2XCT"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:5IWI"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:5IWI"
FT TURN 137..142
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:7MVS"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2XCQ"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:5IWI"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5NPK"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 348..389
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 391..400
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2XCO"
FT HELIX 437..460
FT /evidence="ECO:0007829|PDB:5IWI"
FT HELIX 462..480
FT /evidence="ECO:0007829|PDB:5IWI"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:5IWI"
SQ SEQUENCE 889 AA; 99625 MW; DD5762C23EDC6E2F 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 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
