(data stored in SCRATCH3701 zone)

HOGENOM6: BACA2_1_PE7

ID   BACA2_1_PE7                          STANDARD;      PRT;   793 AA.
AC   BACA2_1_PE7; A7Z0C9;
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   SubName: Full=GyrA; EC=5.99.1 3; (BACA2_1.PE7).
GN   Name=gyrA; OrderedLocusNames=RBAM_000070;
OS   BACILLUS AMYLOLIQUEFACIENS FZB42.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=326423;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACA2_1.PE7.
CC       Bacillus amyloliquefaciens FZB42, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:A7Z0C9_BACA2
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 (By similarity).
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A7Z0C9; -.
DR   EMBL; CP000560; ABS72455.1; -; Genomic_DNA.
DR   RefSeq; YP_001419686.1; NC_009725.1.
DR   ProteinModelPortal; A7Z0C9; -.
DR   SMR; A7Z0C9; 5-461.
DR   STRING; A7Z0C9; -.
DR   EnsemblBacteria; EBBACT00000005865; EBBACP00000005743; EBBACG00000005857.
DR   GeneID; 5461733; -.
DR   GenomeReviews; CP000560_GR; RBAM_000070.
DR   KEGG; bay:RBAM_000070; -.
DR   eggNOG; COG0188; -.
DR   GeneTree; EBGT00050000002933; -.
DR   OMA; TSIPPHR; -.
DR   ProtClustDB; PRK05560; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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   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; BACA2_1.PE7; -.
DR   PRODOM; BACA2_1_PE7.
DR   SWISS-2DPAGE; BACA2_1_PE7.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   793 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSVIVSRALP DVRDGLKPVH RRILYAMNDL GMTSDKPYKK SARIVGEVIG KYHPHGDSAV
     YESMVRMAQD FNYRYMLVDG HGNFGSVDGD SAAAMRYTEA RMSKIAMEIL RDITKDTIDY
     QDNYDGAERE PVVMPSRFPN LLVNGAAGIA VGMATNIPPH QLGEVIEGVL AVSENPEITN
     QELMEYIPGP DFPTAGQILG RSGIRKAYES GRGSITIRAK AEIEETSSGK ERIIVTELPY
     QVNKARLIEK IADLVRDKKI EGITDLRDES DRNGMRIVIE IRRDANAHVI LNNLYKQTAL
     QTSFGINLLA LVDGQPKVLS LKQCLEHYLD HQKVVIRRRT AYELRKAEAR AHILEGLRIA
     LDHLDAVISL IRNSQTAEIA RTGLIEQFSL TEKQAQAILD MRLQRLTGLE REKIEEEYQS
     LVALIAELKD ILANEARVLE IIREELNEIK ERFNDERRTE IVTSGLETIE DEDLIERENI
     VITLTHNGYV KRLPASTYRS QKRGGKGVQG MGTNEDDFVE HLISTSTHDT ILFFSNKGKV
     YRSKGYEIPE YGRTAKGIPI INLLEVEKGE WINAIIPVST FDEEQYLFFT TKQGVSKRTA
     LSQFANIRNN GLIALGLRED DELMAVRLTD GKKQIIIGTK NGLLIRFPEE DVRQMGRTAA
     GVKGITLTDD DVVVGMEILE EDSHVLIVTE NGYGKRTPAS EYRVQSRGGK GLKTCKITDS
     NGPLVTVKAT KGEEDLMIIT ASGVLIRMDI NDISTTGRVT QGVRLIRMSD QEHVATVALV
     EKNEEEPEET EEV
//

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