(data stored in SCRATCH3701 zone)

HOGENOM6: LACRL_1_PE7

ID   LACRL_1_PE7                          STANDARD;      PRT;   870 AA.
AC   LACRL_1_PE7; C7TF62;
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; (LACRL_1.PE7).
GN   Name=gyrA; OrderedLocusNames=LC705_00007;
OS   LACTOBACILLUS RHAMNOSUS LC 705.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; Lactobacillus.
OX   NCBI_TaxID=568704;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LACRL_1.PE7.
CC       Lactobacillus rhamnosus Lc 705 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C7TF62_LACRL
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; C7TF62; -.
DR   EMBL; FM179323; CAR88846.1; -; Genomic_DNA.
DR   RefSeq; YP_003172697.1; NC_013199.1.
DR   STRING; C7TF62; -.
DR   GeneID; 8433205; -.
DR   GenomeReviews; FM179323_GR; LC705_00007.
DR   KEGG; lrl:LC705_00007; -.
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: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; LACRL_1.PE7; -.
DR   PRODOM; LACRL_1_PE7.
DR   SWISS-2DPAGE; LACRL_1_PE7.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   870 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDDRQESRIT NVNLGETMRK SFLEYAMSVI VARALPDVRD GLKPVQRRIL YGMNELGVTP
     EKPYKKSARI VGDVMGKYHP HGDSSIYEGL VRMAQDFSYR YMLVDGHGNF GSVDGDGAAA
     MRYTEARMSK IAVEMLRDIN KDTIDFQDNY DGTEKEPVVL PARFPNLLVN GATGIAVGMT
     TNIPPHNLSE TISALHVLMD HPDATTADLM QALPGPDFPT GGVVMGKSGI RHAYETGRGT
     IVLRGKVDVQ TEKSGRERIV ITEIPYMVNK AKMVERIADL VHEKKIDGIV TLRDESDRDG
     MRIVIDVRRD ASASVILNNL YKLTPLQTGF SFNMVAIVNG APKVLSLKQI LQYYLDHQEN
     VIRRRTQYDL KKAKAREHIL EGLRIALDHI DEIITIIRSS ETGDKAKVIL MDKFNLSDKQ
     SQAILDMRLV RLTGLERDKV ESEYKDVEAA IADYTDILAK PERVHQIIYD ELLDIQKKFG
     DKRRTELLVG EVLSLEDEDL IEQEDVVITL SHNGYVKRLA TSEFKTQNRG GRGIQGMNVH
     DDDFVEHLIS TSTHDVLLFF TNKGKVYRSK GYEIPEYSRT AKGIPIINLL GVGAGEKIQT
     VINVHEGDND DRYLFFVTQN GVVKRTPVKE FANIRSNGLI ALNLKDQDEL NNVILTSGQD
     NILIGTHLGY SVAFKEQDVR SMGRTATGVR GIRLRDHDYV VGSDILKPDS EVFVISEKGY
     GKRTAAKEYP IKGRGGKGIK TANITEKNGP LAGVTTVDGT EDILVMTDSG VMIRFNIQNV
     SQTGRATLGV RLIRVDDDAK VATMAKVEPE SDDPDDSSKP DQPTDPQAGP TDEHAQPADG
     QYAGNADEQV NKLLDRAETD KPAPDDGDEA
//

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