(data stored in SCRATCH3701 zone)

HOGENOM6: CHLTG_1_PE190

ID   CHLTG_1_PE190                        STANDARD;      PRT;   836 AA.
AC   CHLTG_1_PE190; D6YK81;
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; (CHLTG_1.PE190).
GN   OrderedLocusNames=G11074_00975;
OS   CHLAMYDIA TRACHOMATIS G/11074.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=707187;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLTG_1.PE190.
CC       Chlamydia trachomatis (serovar G, strain G/11074) chromosome, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D6YK81_CHLTG
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; D6YK81; -.
DR   EMBL; CP001889; ADH19725.1; -; Genomic_DNA.
DR   GenomeReviews; CP001889_GR; G11074_00975.
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; CHLTG_1.PE190; -.
DR   PRODOM; CHLTG_1_PE190.
DR   SWISS-2DPAGE; CHLTG_1_PE190.
KW   ADH19725.100024376fold_1320000031;
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   836 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLNKEEIIVP KNLEEEMKES YLRYSMSVII SRALPDARDG LKPSQRRILY AMKQLNLTPG
     VKHRKCAKIC GDTSGDYHPH GESVIYPTLV RMAQDWAMRY PLVDGQGNFG SIDGDPAAAM
     RYTEARLTHS AIFLLEDLDK DTVDMVPNYD ETKYEPVVFP SKFPNLLCNG SSGIAVGMAT
     NIPPHNLGEL IEATLLVLAN SQTSIEDILE VMPGPDFPTG GIICGTEGIR STYYTGRGKL
     RLRARMHVEE NSDKQRENII LTEMPYNVNK SRLIEQIVEL INEKTLTGIS DVRDESDKDG
     IRVVLELKKG ESSEVVINRL YKFTDVQVTF GANMLALDKN LPRTMNIHRM ISAWIRHRMD
     VIQRRTRYEL NKAEARAHIL EGFLKALSCM DEVVKTIRES SNKEHAKQQL VELFSFSEAQ
     ALAILELRLY QLTGLEADKV QKEYSELLEK ITYYRKVLAE EELVKDIIRE ELQELHKVHK
     TPRRTRIEMD AGDVRDIEDI ISDESVIITI SGDDYVKRMP VKVFREQKRG GQGVTGFDMK
     KGSDFLKAVY SASTKDYLLI FTNFGQCYWL KVWRLPEGER RAKGKPIINF LEGIRPGEQV
     AAVLNVKRFE QGEYLFLATK KGVVKKVSLD AFGSPRKKGI RALEIDDGDE LIAARHIAND
     EEKVMLFTRL GMAVRFPHDK VRPMGRAARG VRGVSLKNEQ DFVVSCQVVT EDQSVLVVCD
     NGFGKRSLVC DFRETNRGSV GVRSIVINQR NGDVLGAISV TDCDSILLMS AQGQAIRINM
     QDVRVMGRAT QGVRLVNLRE GDTLVAMEKL SINTESVETE ENLAASVQSG QDTIEE
//

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