(data stored in SCRATCH3701 zone)

HOGENOM6: BASUB2_1_PE2298

ID   BASUB2_1_PE2298                      STANDARD;      PRT;   821 AA.
AC   BASUB2_1_PE2298; E8VHA1;
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; (BASUB2_1.PE2298).
GN   OrderedLocusNames=BSn5_11590;
OS   BACILLUS SUBTILIS BSN5.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=936156;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BASUB2_1.PE2298.
CC       Bacillus subtilis BSn5 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E8VHA1_BACST
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; E8VHA1; -.
DR   EMBL; CP002468; ADV94934.1; -; Genomic_DNA.
DR   RefSeq; YP_004205961.1; NC_014976.1.
DR   GeneID; 10182984; -.
DR   GenomeReviews; CP002468_GR; BSn5_11590.
DR   KEGG; bsn:BSn5_11590; -.
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:InterPro.
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; BASUB2_1.PE2298; -.
DR   PRODOM; BASUB2_1_PE2298.
DR   SWISS-2DPAGE; BASUB2_1_PE2298.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   821 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSEQNTPQVR EINISQEMRT SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YAMNDLGMTS
     DKPYKKSARI VGEVIGKYHP HGDSAVYESM VRMAQDFNYR YMLVDGHGNF GSVDGDSAAA
     MRYTEARMSK ISMEILRDIT KDTIDYQDNY DGSEREPVVM PSRFPNLLVN GAAGIAVGMA
     TNIPPHQLGE IIDGVLAVSE NPDITIPELM EVIPGPDFPT AGQILGRSGI RKAYESGRGS
     ITIRAKAEIE QTSSGKERII VTELPYQVNK AKLIEKIADL VRDKKIEGIT DLRDESDRTG
     MRIVIEIRRD ANANVILNNL YKQTALQTSF GINLLALVDG QPKVLTLKQC LEHYLDHQKV
     VIRRRTAYEL RKAEARAHIL EGLRVALDHL DAVISLIRNS QTAEIARTGL IEQFSLTEKQ
     AQAILDMRLQ RLTGLEREKI EEEYQSLVKL IAELKDILAN EYKVLEIIRE ELTEIKERFN
     DERRTEIVTS GLETIEDEDL IERENIVVTL THNGYVKRLP ASTYRSQKRG GKGVQGMGTN
     EDDFVEHLIS TSTHDTILFF SNKGKVYRAK GYEIPEYGRT AKGIPIINLL EVEKGEWINA
     IIPVTEFNAE LYLFFTTKHG VSKRTSLSQF ANIRNNGLIA LGLREDDELM GVRLTDGTKQ
     IIIGTKNGLL IRFPETDVRE MGRTAAGVKG ITLTDDDVVV GMEILEEESH VLIVTEKGYG
     KRTPAEEYRT QSRGGKGLKT AKITENNGQL VAVKATKGEE DLMIITASGV LIRMDINDIS
     ITGRVTQGVR LIRMAEEEHV ATVALVEKNE EDENEEEQEE V
//

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