GYRA_STAAU
ID GYRA_STAAU Reviewed; 889 AA.
AC P20831;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 130.
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};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1311298; DOI=10.1128/jb.174.5.1596-1603.1992;
RA Margerrison E.E.C., Hopewell R., Fisher L.M.;
RT "Nucleotide sequence of the Staphylococcus aureus gyrB-gyrA locus encoding
RT the DNA gyrase A and B proteins.";
RL J. Bacteriol. 174:1596-1603(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-16.
RC STRAIN=601055;
RX PubMed=8388872; DOI=10.1128/jb.175.11.3269-3277.1993;
RA Brockbank S.M.V., Barth P.T.;
RT "Cloning, sequencing, and expression of the DNA gyrase genes from
RT Staphylococcus aureus.";
RL J. Bacteriol. 175:3269-3277(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12600 / DSM 20231 / IAM 12544 / NCDO 949 / NCTC 8532;
RX PubMed=7811012; DOI=10.1128/aac.38.9.2014;
RA Ito H., Yoshida H., Bogaki-Shonai M., Niga T., Hattori H., Nakamura S.;
RT "Quinolone resistance mutations in the DNA gyrase gyrA and gyrB genes of
RT Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 38:2014-2023(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
RX PubMed=2160946; DOI=10.1128/jb.172.6.3481-3484.1990;
RA Hopewell R., Oram M., Briesewitz R., Fisher L.M.;
RT "DNA cloning and organization of the Staphylococcus aureus gyrA and gyrB
RT genes: close homology among gyrase proteins and implications for 4-
RT quinolone action and resistance.";
RL J. Bacteriol. 172:3481-3484(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-91.
RX PubMed=2174869; DOI=10.1128/jb.172.12.7260-7262.1990;
RA Sreedharan S., Oram M., Jensen B., Peterson L.R., Fisher L.M.;
RT "DNA gyrase gyrA mutations in ciprofloxacin-resistant strains of
RT Staphylococcus aureus: close similarity with quinolone resistance mutations
RT in Escherichia coli.";
RL J. Bacteriol. 172:7260-7262(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-129.
RX PubMed=1510411; DOI=10.1128/aac.36.5.1166;
RA Goswitz J.J., Willard K.E., Fasching C.E., Peterson L.R.;
RT "Detection of gyrA gene mutations associated with ciprofloxacin resistance
RT in methicillin-resistant Staphylococcus aureus: analysis by polymerase
RT chain reaction and automated direct DNA sequencing.";
RL Antimicrob. Agents Chemother. 36:1166-1169(1992).
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; M86227; AAA73952.1; -; Genomic_DNA.
DR EMBL; X71437; CAA50571.1; -; Genomic_DNA.
DR EMBL; D10489; BAA01370.1; -; Genomic_DNA.
DR EMBL; M37915; AAA26636.1; -; Genomic_DNA.
DR PIR; B40585; B40585.
DR RefSeq; WP_000819084.1; NZ_WSFM01000002.1.
DR RefSeq; WP_000819086.1; NZ_WKIB01000016.1.
DR PDB; 4PLB; X-ray; 2.69 A; B/D=2-491.
DR PDB; 5BS3; X-ray; 2.65 A; B/D=2-491.
DR PDB; 6Z1A; X-ray; 2.30 A; B/D=2-491.
DR PDBsum; 4PLB; -.
DR PDBsum; 5BS3; -.
DR PDBsum; 6Z1A; -.
DR AlphaFoldDB; P20831; -.
DR SMR; P20831; -.
DR BindingDB; P20831; -.
DR ChEMBL; CHEMBL2424506; -.
DR DrugBank; DB00537; Ciprofloxacin.
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;
KW Direct protein sequencing; DNA-binding; Isomerase; Nucleotide-binding;
KW Topoisomerase.
FT CHAIN 1..889
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145254"
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"
FT MUTAGEN 85
FT /note="S->P: Resistant to fluoroquinolones."
FT CONFLICT 439
FT /note="D -> N (in Ref. 2; CAA50571)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="D -> E (in Ref. 2; CAA50571)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="E -> G (in Ref. 2; CAA50571)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="A -> E (in Ref. 1; AAA73952)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="Missing (in Ref. 2; CAA50571)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="T -> V (in Ref. 2; CAA50571)"
FT /evidence="ECO:0000305"
FT CONFLICT 825..826
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="D -> E (in Ref. 1; AAA73952)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="N -> T (in Ref. 1; AAA73952)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="E -> D (in Ref. 1; AAA73952)"
FT /evidence="ECO:0000305"
FT CONFLICT 884..886
FT /note="LDE -> S (in Ref. 3; BAA01370)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="L -> S (in Ref. 2; CAA50571)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 14..32
FT /evidence="ECO:0007829|PDB:6Z1A"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:6Z1A"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6Z1A"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:6Z1A"
FT TURN 137..142
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:6Z1A"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:6Z1A"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 348..389
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 437..459
FT /evidence="ECO:0007829|PDB:6Z1A"
FT HELIX 462..480
FT /evidence="ECO:0007829|PDB:6Z1A"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:6Z1A"
SQ SEQUENCE 889 AA; 99621 MW; 3B826115E06C2250 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 QQSLDEDEE
