(data stored in SCRATCH3701 zone)

HOGENOM6: STPYO1_1_PE880

ID   STPYO1_1_PE880                       STANDARD;      PRT;   828 AA.
AC   STPYO1_1_PE880; Q9L7Q5; Q48YT0;
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   RecName: Full=DNA gyrase subunit A; EC=5.99.1 3; (STPYO1_1.PE880).
GN   Name=gyrA; OrderedLocusNames=SPy_1152, M5005_Spy0874;
OS   STREPTOCOCCUS PYOGENES M1 GAS.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
OX   NCBI_TaxID=160490;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STPYO1_1.PE880.
CC       Streptococcus pyogenes M1 GAS chromosome, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:GYRA_STRP1
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.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q9L7Q5; Q48YT0; -.
DR   EMBL; AF220945; AAF63266.1; -; Genomic_DNA.
DR   EMBL; AE004092; AAK34024.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51492.1; -; Genomic_DNA.
DR   RefSeq; NP_269303.1; NC_002737.1.
DR   RefSeq; YP_282237.1; NC_007297.1.
DR   ProteinModelPortal; Q9L7Q5; -.
DR   SMR; Q9L7Q5; 31-484.
DR   EnsemblBacteria; EBSTRT00000001522; EBSTRP00000001522; EBSTRG00000001522.
DR   EnsemblBacteria; EBSTRT00000029015; EBSTRP00000028033; EBSTRG00000029015.
DR   GeneID; 3572044; -.
DR   GeneID; 901268; -.
DR   GenomeReviews; AE004092_GR; SPy_1152.
DR   GenomeReviews; CP000017_GR; M5005_Spy0874.
DR   KEGG; spy:SPy_1152; -.
DR   KEGG; spz:M5005_Spy_0874; -.
DR   GeneTree; EBGT00050000028052; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; SPYO160490:SPY1152-MON; -.
DR   BioCyc; SPYO293653:M5005_SPY0874-MON; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   HAMAP; MF_01897; GyrA; 1; -.
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; STPYO1_1.PE880; -.
DR   PRODOM; STPYO1_1_PE880.
DR   SWISS-2DPAGE; STPYO1_1_PE880.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   828 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQDRNLIDVN LTSEMKTSFI DYAMSVIVAR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
     HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRHML VDGHGNFGSM DGDGAAAQRY
     TEARMSKIAL ELLRDINKNT VNFQDNYDGS EREPVVLPAR FPNLLVNGAT GIAVGMATNI
     PPHNLAESID AVKMVMEHPD CTTRELMEVI PGPDFPTGAL VMGRSGIHRA YDTGKGSIVL
     RSRTEIETTQ TGRERIVVTE FPYGVNKTKV HEHIVRLAQE KRLEGITAVR DESSREGVRF
     VIEIRREASA TVILNNLFKL TSLQTNFSFN MLAIENGVPK ILSLRQIIDN YISHQKEVII
     RRTRFDKDKA EARAHILEGL LIALDHLDEV IAIIRNSETD VIAQTELMSR FDLSERQSQA
     ILDMRLRRLT GLERDKIQSE YDDLLALIAD LSDILAKPER IITIIKEEMD EIKRKYANPR
     RTELMVGEVL SLEDEDLIEE EDVLITLSNK GYIKRLAQDE FRAQKRGGRG VQGTGVNNDD
     FVRELISTST HDTLLFFTNF GRVYRLKAYE IPEYGRTAKG LPIVNLLKLE DGETIQTIIN
     ARKEETAGKS FFFTTKQGIV KRTEVSEFNN IRQNGLRALK LKEGDQLINV LLTSGQDDII
     IGTHSGYSVR FNEASIRNMG RSATGVRGVK LREDDRVVGA SRIQDNQEVL VITENGFGKR
     TSATDYPTKG RGGKGIKTAN ITPKNGQLAG LVTVDGTEDI MVITNKGVII RTNVANISQT
     GRATLGVKIM KLDADAKIVT FTLVQPEDSS IAEINTDREN SISKNKDN
//

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