(data stored in SCRATCH3701 zone)

HOGENOM6: CLOBM_2_PE7

ID   CLOBM_2_PE7                          STANDARD;      PRT;   831 AA.
AC   CLOBM_2_PE7; B1L1L2;
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, A subunit; EC=5.99.1 3; (CLOBM_2.PE7).
GN   Name=gyrA; OrderedLocusNames=CLK_3139;
OS   CLOSTRIDIUM BOTULINUM A3 STR. LOCH MAREE.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CLOBM_2.PE7.
CC       Clostridium botulinum A3 str. Loch Maree, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B1L1L2_CLOBM
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; B1L1L2; -.
DR   EMBL; CP000962; ACA53600.1; -; Genomic_DNA.
DR   RefSeq; YP_001785342.1; NC_010520.1.
DR   ProteinModelPortal; B1L1L2; -.
DR   SMR; B1L1L2; 30-484.
DR   STRING; B1L1L2; -.
DR   GeneID; 6153798; -.
DR   GenomeReviews; CP000962_GR; CLK_3139.
DR   KEGG; cbl:CLK_3139; -.
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; 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; CLOBM_2.PE7; -.
DR   PRODOM; CLOBM_2_PE7.
DR   SWISS-2DPAGE; CLOBM_2_PE7.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   831 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLNEGKILPV DVSKEMKKCY IDYAMSVIAG RALPDVRDGL KPVHRRIIYS MQGLGLSPEK
     GYRKCARIVG DVLGKYHPHG DTAVYEALVR LAQDFSIRYT LVDGHGNFGS VDGDSAAAMR
     YTEAKMSKIS MELIKDINKN TVDFIPNFDG EEEEPSVLPS RFPNLLVNGS AGIAVGMATN
     IPPHNLTEVI DGIIMLIENE DVTIMDLMTK IKGPDFPTSG LIVGTRGIRE AYETGRGKVI
     IRAKADIEEE KGRNRIIVTE IPYQVNKARL IENMANLVKD KKINGISDLR DESDRDGMRI
     VIELKRDANP NVVLNQLYKH TKLQDTFGII MLALVNNQPQ VLNLKEILVN YLEFQKEVIR
     RRTKFDLDKA LARAHILEGL RIALDHIDEV IKLIRSSKNA AEAKEGLMNN FNLSEKQAQA
     ILDMKLQRLT GLEREKIEEE YKELMERIGY FRQILDKEEL VLSIIKEELT EIKNKYGDER
     RTEIVKGEHD IDIEDLIEDK KVIVTLTHGG YIKRLDMDTY SSQKRGGKGI QATSTKQDDF
     IENMFVTSTH STILFFTNRG KVYKLKAYEI PEAGRTAKGT NIVNIIPIEN NEKIQTVIGL
     KDIDDMKHFV MCTRNGIIKK TEIVKYSSIR KGGLIAINLR EDDELIDVKM TKGNNEIIIV
     TQNGYCIRFN EKDVRPMGRT ASGVKAITLR EDDKAVSMDV VLEDEALLSI SENGFGKRTD
     IEEYPIHRRG GKGVITYKIT DKTGPIVGAR FVKEDDELML VNSGDVAIRI NVSEISKTSR
     NAMGVKLMRT SEEEKIVAIA KIKSEDIIEE EILNEENSNE ENSNEENSNE E
//

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