(data stored in SCRATCH3701 zone)

HOGENOM6: MYCBP_1_PE6

ID   MYCBP_1_PE6                          STANDARD;      PRT;   838 AA.
AC   MYCBP_1_PE6; A1KEE7;
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=DNA gyrase subunit A gyrA; EC=5.99.1.3;SubName: Full=Dna
DE   gyrase subunit A gyrA (MYCBP_1.PE6) (DNA topoisomerase); EC=5.99.1 3; .
GN   Name=gyrA_1; Synonyms=gyrA_2; OrderedLocusNames=BCG_0006, BCG_0036;
OS   MYCOBACTERIUM BOVIS BCG STR. PASTEUR 1173P2.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium
OC   tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MYCBP_1.PE6.
CC       Mycobacterium bovis BCG str. Pasteur 1173P2, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A1KEE7_MYCBP
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; A1KEE7; -.
DR   EMBL; AM408590; CAL69990.1; -; Genomic_DNA.
DR   EMBL; AM408590; CAL70020.1; -; Genomic_DNA.
DR   RefSeq; YP_976112.1; NC_008769.1.
DR   RefSeq; YP_976139.1; NC_008769.1.
DR   ProteinModelPortal; A1KEE7; -.
DR   STRING; A1KEE7; -.
DR   EnsemblBacteria; EBMYCT00000020708; EBMYCP00000020458; EBMYCG00000020703.
DR   EnsemblBacteria; EBMYCT00000021537; EBMYCP00000021287; EBMYCG00000021532.
DR   GeneID; 4695442; -.
DR   GeneID; 4695443; -.
DR   GenomeReviews; AM408590_GR; BCG_0006.
DR   GenomeReviews; AM408590_GR; BCG_0036.
DR   KEGG; mbb:BCG_0006; -.
DR   KEGG; mbb:BCG_0036; -.
DR   eggNOG; COG0188; -.
DR   GeneTree; EBGT00050000016653; -.
DR   OMA; TGRGRIY; -.
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; IPR011042; 6-blade_b-propeller_TolB-like.
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:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
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; MYCBP_1.PE6; -.
DR   PRODOM; MYCBP_1_PE6.
DR   SWISS-2DPAGE; MYCBP_1_PE6.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   838 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDTTLPPDD SLDRIEPVDI QQEMQRSYID YAMSVIVGRA LPEVRDGLKP VHRRVLYAMF
     DSGFRPDRSH AKSARSVAET MGNYHPHGDA SIYDTLVRMA QPWSLRYPLV DGQGNFGSPG
     NDPPAAMRYT EARLTPLAME MLREIDEETV DFIPNYDGRV QEPTVLPSRF PNLLANGSGG
     IAVGMATNIP PHNLRELADA VFWALENHDA DEEETLAAVM GRVKGPDFPT AGLIVGSQGT
     ADAYKTGRGS IRMRGVVEVE EDSRGRTSLV ITELPYQVNH DNFITSIAEQ VRDGKLAGIS
     NIEDQSSDRV GLRIVIEIKR DAVAKVVINN LYKHTQLQTS FGANMLAIVD GVPRTLRLDQ
     LIRYYVDHQL DVIVRRTTYR LRKANERAHI LRGLVKALDA LDEVIALIRA SETVDIARAG
     LIELLDIDEI QAQAILDMQL RRLAALERQR IIDDLAKIEA EIADLEDILA KPERQRGIVR
     DELAEIVDRH GDDRRTRIIA ADGDVSDEDL IAREDVVVTI TETGYAKRTK TDLYRSQKRG
     GKGVQGAGLK QDDIVAHFFV CSTHDLILFF TTQGRVYRAK AYDLPEASRT ARGQHVANLL
     AFQPEERIAQ VIQIRGYTDA PYLVLATRNG LVKKSKLTDF DSNRSGGIVA VNLRDNDELV
     GAVLCSADDD LLLVSANGQS IRFSATDEAL RPMGRATSGV QGMRFNIDDR LLSLNVVREG
     TYLLVATSGG YAKRTAIEEY PVQGRGGKGV LTVMYDRRRG RLVGALIVDD DSELYAVTSG
     GGVIRTAARQ VRKAGRQTKG VRLMNLGEGD TLLAIARNAE ESGDDNAVDA NGADQTGN
//

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