(data stored in SCRATCH3701 zone)

HOGENOM6: CLOB2_1_PE7

ID   CLOB2_1_PE7                          STANDARD;      PRT;   819 AA.
AC   CLOB2_1_PE7; D5W0U3;
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; (CLOB2_1.PE7).
GN   Name=gyrA; OrderedLocusNames=CBF_0007;
OS   CLOSTRIDIUM BOTULINUM F STR. 230613.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=758678;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CLOB2_1.PE7.
CC       Clostridium botulinum (strain 230613 / Type F) chromosome, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D5W0U3_CLOB2
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; D5W0U3; -.
DR   EMBL; CP002011; ADF97860.1; -; Genomic_DNA.
DR   GenomeReviews; CP002011_GR; CBF_0007.
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; CLOB2_1.PE7; -.
DR   PRODOM; CLOB2_1_PE7.
DR   SWISS-2DPAGE; CLOB2_1_PE7.
KW   ADF97860.1000011385old_1320000031;
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   819 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLNEGKILPV DVSKEMKKCY IDYAMSVIAG RALPDVRDGL KPVHRRIIYS MQGLGLAPEK
     GYRKCARIVG DVLGKYHPHG DTAVYEALVR MAQDFSIRYT LVDGHGNFGS VDGDGAAAMR
     YTEAKMSKIS MELIKDINKN TVDFIPNFDG EEEEPSVLPS RFPNLLVNGS AGIAVGMATN
     IPPHNLTEVI DGIIMLIDNE DVNILDLMTK IKGPDFPTFG LIVGTRGIRE AYETGRGKVI
     IRAKAEIEEE KGRNRIVVTE IPYQVNKSKL IENMANLVKD KKINGISDLR DESDRDGMRI
     VIELKRDANP NIVLNQLYKH TKLQDTFGII MLALVNNQPQ VLNLKEILVN YVEFQKEVIR
     RRTKFDLDKA LARAHILEGL RIALDHIDEV IKLIRSSKNA AEAKEGLMNN FNLSEKQAQA
     ILDMKLQRLT GLEREKIEEE YKELMEKISY FREILDKEEL VLSIIKEELI EIKNKYGDER
     KTEIVKGEHD IDIEDLIEDK KVIVTLTHGG YIKRLDMDTY SSQKRGGKGI QATSTKQDDF
     IENMFVTSTH STILFFTNRG KVYKLKAYEI PEAGRTAKGT NIVNIIPIEN NEKIQTVIGL
     KDIDDMKHFV MCTRNGIIKK TEISKYSSIR KGGLNAINLR EDDELIDVKM TKGNNEIIIV
     TQNGYCIRFN EEDVRPMGRV ATGVKGITLR EDDKAVSMEV VLGDEALLSI SENGFGKRTD
     IEEYPIHRRG GKGVITYKIT DKTGPIVGAR FVKEDDELML VNSGDVAIRI NVSEISKTSR
     NAMGVKLMRT SEEEKIVAIA KIKSEDIIEE EILNEVNFK
//

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