(data stored in SCRATCH3701 zone)

HOGENOM6: STAAN_1_PE6

ID   STAAN_1_PE6                          STANDARD;      PRT;   889 AA.
AC   STAAN_1_PE6; Q99XG5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA gyrase subunit A; EC=5.99.1 3; (STAAN_1.PE6).
GN   Name=gyrA; OrderedLocusNames=SA0006;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS N315.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAN_1.PE6.
CC       Staphylococcus aureus subsp. aureus N315, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:GYRA_STAAN
CC   -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC       stranded DNA in an ATP-dependent manner and also catalyzes the
CC       interconversion of other topological isomers of double-stranded
CC       DNA rings, including catenanes and knotted rings (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA.
CC   -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC       breakage and rejoining; the B chain catalyzes ATP hydrolysis. The
CC       enzyme forms an A2B2 tetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q99XG5; -.
DR   EMBL; BA000018; BAB41222.1; -; Genomic_DNA.
DR   PIR; F89758; F89758.
DR   RefSeq; NP_373244.1; 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   PDBsum; 2XCO; -.
DR   PDBsum; 2XCQ; -.
DR   PDBsum; 2XCR; -.
DR   PDBsum; 2XCS; -.
DR   PDBsum; 2XCT; -.
DR   ProteinModelPortal; Q99XG5; -.
DR   SMR; Q99XG5; 31-489.
DR   STRING; Q99XG5; -.
DR   EnsemblBacteria; EBSTAT00000002111; EBSTAP00000002111; EBSTAG00000002111.
DR   GeneID; 1122777; -.
DR   GenomeReviews; BA000018_GR; SA0006.
DR   KEGG; sau:SA0006; -.
DR   eggNOG; COG0188; -.
DR   GeneTree; EBGT00050000024676; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; SAUR158879:SA0006-MON; -.
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-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   HAMAP; MF_01897; GyrA; 1; -.
DR   InterPro; IPR020899; Arg_repress_C.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_pinwhl.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
DR   InterPro; IPR013760; Topo_IIA_cen.
DR   Gene3D; G3DSA:3.30.1360.40; Arg_repress; 1.
DR   Gene3D; G3DSA:3.90.199.10; Topo_IIA_A/C_ab; 1.
DR   Gene3D; G3DSA:1.10.268.10; Topo_IIA_A_a; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   TIGRFAMs; TIGR01063; GyrA; 1.
DR   HOGENOMDNA; STAAN_1.PE6; -.
DR   PRODOM; STAAN_1_PE6.
DR   SWISS-2DPAGE; STAAN_1_PE6.
KW   DNA gyrase subunit A;
KW   3D-structure; Antibiotic resistance; ATP-binding; Complete proteome;
KW   Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   889 AA;  UNKNOWN MW;  UNKNOWN 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
//

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