(data stored in SCRATCH3701 zone)

HOGENOM6: STAGA3_1_PE949

ID   STAGA3_1_PE949                       STANDARD;      PRT;   819 AA.
AC   STAGA3_1_PE949; Q3K1C7;
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; (STAGA3_1.PE949).
GN   Name=gyrA; OrderedLocusNames=SAK_1055;
OS   STREPTOCOCCUS AGALACTIAE A909.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
OX   NCBI_TaxID=205921;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAGA3_1.PE949.
CC       Streptococcus agalactiae A909, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q3K1C7_STRA1
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; Q3K1C7; -.
DR   EMBL; CP000114; ABA45619.1; -; Genomic_DNA.
DR   RefSeq; YP_329676.1; NC_007432.1.
DR   ProteinModelPortal; Q3K1C7; -.
DR   EnsemblBacteria; EBSTRT00000004282; EBSTRP00000004055; EBSTRG00000004282.
DR   GeneID; 3685338; -.
DR   GenomeReviews; CP000114_GR; SAK_1055.
DR   KEGG; sak:SAK_1055; -.
DR   TIGR; SAK_1055; -.
DR   GeneTree; EBGT00050000028052; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; SAGA205921:SAK_1055-MONOMER; -.
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; STAGA3_1.PE949; -.
DR   PRODOM; STAGA3_1_PE949.
DR   SWISS-2DPAGE; STAGA3_1_PE949.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   819 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQDKNLVDVN LTSEMKTSFI DYAMSVIVAR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
     HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRHML VDGHGNFGSM DGDGAAAQRY
     TEARMSKIAL EMLRDINKNT VDFQDNYDGS EREPLVLPAR FPNLLVNGAT GIAVGMATNI
     PPHNLGESID AVKLVMDNPD VTTRELMEVI PGPDFPTGAL VMGRSGIHRA YETGKGSIVL
     RSRTEIETTS NGKERIVVTE FPYGVNKTKV HEHIVRLAQE KRIEGITAVR DESSREGVRF
     VIEVRRAASA NVILNNLFKL TSLQTNFSFN MLAIEKGVPK ILSLRQIIDN YIEHQKEVIV
     RRTQFDKAKA GARAHILEGL LVALDHLDEV ITIIRNSETD TIAQAELMSR FELSERQSQA
     ILDMRLRRLT GLERDKIQSE YNDLLALIAD LADILAKPER VVTIIKEEMD EVKRKYADAR
     RTELMIGEVL SLEDEDLIEE EDVLITLSNK GYIKRLAQDE FRAQKRGGRG IQGTGVNNDD
     FVRELVSTST HDTVLFFTNL GRVYRLKAYE IPEYGRTAKG LPIVNLLKLD EGETIQTIIN
     ARKEDVANKY FFFTTQQGIV KRTSVSEFSN IRQNGLRAIN LKENDELINV LLIDENEDVI
     IGTRTGYSVR FKVNAVRNMG RTATGVRGVN LREGDKVVGA SRIVNGQEVL IITEKGYGKR
     TEASEYPTKG RGGKGIKTAN ITAKNGPLAR LVTINGNEDI MVITDTGVII RTNVANISQT
     GRSTMGVKVM RLDQEAKIVT VALVEQEIED KSNIEDTKE
//

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