(data stored in SCRATCH3701 zone)

HOGENOM6: STRSV_1_PE1154

ID   STRSV_1_PE1154                       STANDARD;      PRT;   826 AA.
AC   STRSV_1_PE1154; A3CN69;
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, putative; EC=5.99.1 3;
DE   (STRSV_1.PE1154).
GN   Name=gyrA; OrderedLocusNames=SSA_1220;
OS   STREPTOCOCCUS SANGUINIS SK36.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
OX   NCBI_TaxID=388919;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STRSV_1.PE1154.
CC       Streptococcus sanguinis SK36, complete genome.
CC       1..88329 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:A3CN69_STRSV
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; A3CN69; -.
DR   EMBL; CP000387; ABN44624.1; -; Genomic_DNA.
DR   RefSeq; YP_001035174.1; NC_009009.1.
DR   ProteinModelPortal; A3CN69; -.
DR   SMR; A3CN69; 35-491.
DR   STRING; A3CN69; -.
DR   EnsemblBacteria; EBSTRT00000052926; EBSTRP00000049190; EBSTRG00000052916.
DR   GeneID; 4806571; -.
DR   GenomeReviews; CP000387_GR; SSA_1220.
DR   KEGG; ssa:SSA_1220; -.
DR   NMPDR; fig|388919.8.peg.1095; -.
DR   eggNOG; COG0188; -.
DR   GeneTree; EBGT00050000028052; -.
DR   OMA; TGRGRIY; -.
DR   PhylomeDB; A3CN69; -.
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; STRSV_1.PE1154; -.
DR   PRODOM; STRSV_1_PE1154.
DR   SWISS-2DPAGE; STRSV_1_PE1154.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   826 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKERHFLMQD RNLVNVNLTN EMKTSFIDYA MSVIVARALP DVRDGLKPVH RRILYGMNEL
     GVTPEKPHKK SARITGDVMG KYHPHGDSSI YEAMVRMAQW WSYRYMLVDG HGNFGSMDGD
     GAAAQRYTEA RMSKIALEML RDINKNTVDY IDNYDASERE PVVLPARFPN LLVNGATGIA
     VGMATNIPPH NLGESIDAVK LVMDNPDATT RDIMEVLPGP DFPTGALVMG KSGIHRAYET
     GKGSIVLRSR TEIEEMKNGR ERIVVTEFPY MVNKTKVHEH IVRLVQEKRI DGITAVRDES
     NREGVRFVIE VRRDASAHVI LNNLFKLTQM QTNFSFNMLA IQNGVPKILS LREILLAYIE
     HQKEVVTRRT VFDKEKAEAR AHILAGLLIA LDHIDEVIRI IRNSETDAEA QAELMAKFEL
     SERQSQAILD MRLRRLTGLE RDKIQSEYDE LIALIADLAD ILAKPERVIA IIKEELDEVK
     RKFADDRRTE LMVGEVLSLE DEDLIEEADV LITLSNKGYI KRLNQAEFTA QKRGGRGVQG
     TGVKDDDFVK ELVSTSTHDR LLFFTNKGRV YRLKGYEIPE YGRTAKGLPA VNLLKLDEGE
     TIQTIINVQQ DRSDDSYLFF TTRHGVVKRT SVTEFANIRQ NGLKALNLKD EDELINVFLT
     DGAADVIIGT KFGYSVRFNE TAVRSMGRIA TGVRGVNLRD GDQVVGAGVI AEGDEVLVIT
     EKGYGKRTLA SEYPTKGRGG KGIKTANITD KNGPLAGLMT VTGEEDLMII TNTGVIIRTS
     VANISQTGRS TMGVKVMRLD QNAQIVTFTS VEADDKEDVA EEENES
//

If you have problems or comments...

PBIL Back to PBIL home page