(data stored in SCRATCH3701 zone)

HOGENOM6: BACAS_1_PE7

ID   BACAS_1_PE7                          STANDARD;      PRT;   819 AA.
AC   BACAS_1_PE7; E1UJ75;
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 (BACAS_1.PE7) (Subunit A); EC=5.99.1 3; .
GN   Name=gyrA; OrderedLocusNames=BAMF_0007;
OS   BACILLUS AMYLOLIQUEFACIENS DSM 7.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=692420;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACAS_1.PE7.
CC       Bacillus amyloliquefaciens DSM 7, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:E1UJ75_BACAS
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; E1UJ75; -.
DR   EMBL; FN597644; CBI41133.1; -; Genomic_DNA.
DR   RefSeq; YP_003918603.1; NC_014551.1.
DR   GeneID; 9778985; -.
DR   GenomeReviews; FN597644_GR; BAMF_0007.
DR   KEGG; bao:BAMF_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; BACAS_1.PE7; -.
DR   PRODOM; BACAS_1_PE7.
DR   SWISS-2DPAGE; BACAS_1_PE7.
KW   DNA gyrase (subunit A);
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   819 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSEQNTPQVR EVNISQEMRT SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YAMNDLGMTS
     DKPYKKSARI VGEVIGKYHP HGDSAVYESM VRMAQDFNYR YMLVDGHGNF GSVDGDSAAA
     MRYTEARMSK IAMEILRDIT KDTIDYQDNY DGSEREPAVM PSRFPNLLVN GAAGIAVGMA
     TNIPPHQLGE VIDGVLAVSE NPEITIQELM EYIPGPDFPT AGQILGRSGI RKAYESGRGS
     ITIRAKAEIE QTSSGKERII VTELPYQVNK ARLIEKIADL VRDKKIEGIT DLRDESDRNG
     MRVVIELRRD ANAHVILNNL YKQTALQTSF GINLLALVDG QPKVLSLKQC LEHYLDHQKV
     VIRRRTAYEL RKAEARAHIL EGLRIALDHL DAVISLIRNS QTAEIARTGL IEQFSLTEKQ
     AQAILDMRLQ RLTGLEREKI EEEYQSLVAL IAELKDILAN EERVLEIIRE ELNEIKERFN
     DERRTEIVTS GLETIEDEDL IERENIVITL THNGYVKRLP ASTYRSQKRG GKGVQGMGTN
     EDDFVEHLIS TSTHDTILFF SNKGKVYRSK GYEIPEYGRT AKGIPIINLL EVEKGEWINA
     IIPVSTFDEE LYLFFTTKQG VSKRTALSQF ANIRNNGLIA LGLREDDELM AVRLTDGKKQ
     IIIGTKNGLL IRFPEEDVRQ MGRTAAGVKG ITLTDDDVVV GMEILEEDSH VLIVTENGYG
     KRTPASEYRV QSRGGKGLKT CKITDSNGPL VTVKATRGEE DLMIITASGV LIRMDINDIS
     TTGRVTQGVR LIRMSDQEHV ATVALVEKNE EEPEETEEV
//

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