(data stored in SCRATCH3701 zone)

HOGENOM6: LEPBD_1_PE2213

ID   LEPBD_1_PE2213                       STANDARD;      PRT;   855 AA.
AC   LEPBD_1_PE2213; C7NEF8;
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; (LEPBD_1.PE2213).
GN   OrderedLocusNames=Lebu_2299;
OS   LEPTOTRICHIA BUCCALIS C-1013-B.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Leptotrichia.
OX   NCBI_TaxID=523794;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEPBD_1.PE2213.
CC       Leptotrichia buccalis DSM 1135, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C7NEF8_LEPBD
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; C7NEF8; -.
DR   EMBL; CP001685; ACV40150.1; -; Genomic_DNA.
DR   RefSeq; YP_003165141.1; NC_013192.1.
DR   STRING; C7NEF8; -.
DR   GeneID; 8409042; -.
DR   GenomeReviews; CP001685_GR; Lebu_2299.
DR   KEGG; lba:Lebu_2299; -.
DR   OMA; TSIPPHR; -.
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; LEPBD_1.PE2213; -.
DR   PRODOM; LEPBD_1_PE2213.
DR   SWISS-2DPAGE; LEPBD_1_PE2213.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   855 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDDFRDDDE REEEITEMDE NDDREIIVEG LPKATDLSNE SNVYIEDEIK AAYLDYSMSV
     IVSRALPDVR DGLKPVHRRI LFSMSEMGMS HKTPFKKSAR IVGDVLGKYH PHGDSSVYGA
     MVRMAQDFNM RYELIDGHGN FGSIDGDEAA AMRYTEARMA KITEELLEDI RKDTIDYRKN
     FDESLDEPVV LPAKLPNLLL NGANGIAVGM ATNIPPHNLG EVVDGIIALI DNPEISIDEL
     ITYIKGPDFP TGGIINGKQG IYDAYRTGRG KLRVAGRVEV ETSKTGKESI IVTELPYQVN
     KARLIEKIAD LVRQKKITGI SDLRDETDRD GIRIVIELKK GEESELILNS LYKFTDLQNT
     FGVIMLALVD NAPRVLNLKQ ILQKYLEHRF EVITRRTEFE LKKAKNRAHI LEGFKIALDN
     IEEVIRIIRA SKDANVARAE LIAKFGFSEI QAKAILDMRL QRLTGLERDK INQEYNELML
     LIEELTGILS DDSKIYGIIK EEGLKLKEDF GDERRTEIRN ARAEISIEDL IKDEEVVVTL
     TEKGYVKRVA IDTYRSQKRG GIGVNATNTV EDDVVKDMYI AKALDTLLIF TTKGKVFSIK
     VYEIPETGKQ ARGKLIGNII NLDDDEKVST IIKVREFEKN KNLFFVTRNG VVKKSELTLF
     DNIKKAGKRA IRLNEDDEVM FIGLTSGSGE DEIFAATKNG IAIRFSEKDV RSMGTGAAGV
     RGINLRDEDK IVGAAIISSE MNKDDARILT ITEEGYGKRT KLLEYRLTSR GGKGIINAKL
     NEKTGKIVDV KIVKDDDEIM LITSEGTLIR TSVKDVSVIG RSATGVRIMK VRNNEKIASI
     VKITEEPKLD DEVKK
//

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