(data stored in SCRATCH3701 zone)

HOGENOM6: MYTUB1_1_PE6

ID   MYTUB1_1_PE6                         STANDARD;      PRT;   838 AA.
AC   MYTUB1_1_PE6; Q07702; P71574; P97136;
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; (MYTUB1_1.PE6).
GN   Name=gyrA; OrderedLocusNames=Rv0006, MT0006; ORFNames=MTCY10H4.04;
OS   MYCOBACTERIUM TUBERCULOSIS H37RV.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium
OC   tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MYTUB1_1.PE6.
CC       Mycobacterium tuberculosis H37Rv, complete genome.
CC       1..69269 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:GYRA_MYCTU
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.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- MISCELLANEOUS: When the enzyme transiently cleaves DNA a
CC       phosphotyrosine bond is formed between the gyrA and DNA.
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q07702; P71574; P97136; -.
DR   EMBL; L27512; AAA83017.1; -; Genomic_DNA.
DR   EMBL; BX842572; CAB02427.1; -; Genomic_DNA.
DR   EMBL; AE000516; AAK44229.1; -; Genomic_DNA.
DR   EMBL; L11919; AAC36878.1; -; Unassigned_DNA.
DR   EMBL; X72872; CAA51386.1; -; Genomic_DNA.
DR   PIR; D70698; D70698.
DR   RefSeq; NP_214520.1; NC_000962.2.
DR   RefSeq; NP_334415.1; NC_002755.2.
DR   PDB; 3IFZ; X-ray; 2.70 A; A/B=1-501.
DR   PDB; 3ILW; X-ray; 1.60 A; A/B=34-500.
DR   PDBsum; 3IFZ; -.
DR   PDBsum; 3ILW; -.
DR   ProteinModelPortal; Q07702; -.
DR   EnsemblBacteria; EBMYCT00000001336; EBMYCP00000001336; EBMYCG00000001336.
DR   EnsemblBacteria; EBMYCT00000068956; EBMYCP00000067015; EBMYCG00000068951.
DR   GeneID; 887105; -.
DR   GeneID; 922437; -.
DR   GenomeReviews; AE000516_GR; MT0006.
DR   GenomeReviews; AL123456_GR; Rv0006.
DR   KEGG; mtc:MT0006; -.
DR   KEGG; mtu:Rv0006; -.
DR   TIGR; MT0006; -.
DR   TubercuList; Rv0006; -.
DR   GeneTree; EBGT00050000016653; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR   GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IDA:MTBBASE.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MTBBASE.
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; MYTUB1_1.PE6; -.
DR   PRODOM; MYTUB1_1_PE6.
DR   SWISS-2DPAGE; MYTUB1_1_PE6.
KW   3D-structure; Antibiotic resistance; ATP-binding; Complete proteome;
KW   Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
SQ   SEQUENCE   838 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDTTLPPDD SLDRIEPVDI EQEMQRSYID YAMSVIVGRA LPEVRDGLKP VHRRVLYAMF
     DSGFRPDRSH AKSARSVAET MGNYHPHGDA SIYDSLVRMA 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
     GAVLCSAGDD LLLVSANGQS IRFSATDEAL RPMGRATSGV QGMRFNIDDR LLSLNVVREG
     TYLLVATSGG YAKRTAIEEY PVQGRGGKGV LTVMYDRRRG RLVGALIVDD DSELYAVTSG
     GGVIRTAARQ VRKAGRQTKG VRLMNLGEGD TLLAIARNAE ESGDDNAVDA NGADQTGN
//

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