(data stored in SCRATCH3701 zone)

HOGENOM6: ECOBB_1_PE2129

ID   ECOBB_1_PE2129                       STANDARD;      PRT;   875 AA.
AC   ECOBB_1_PE2129; C6E9X0; C5W6X0;
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; EC=5.99.1.3;SubName: Full=DNA gyrase,
DE   A subunit; EC=5.99.1.3;SubName: Full=DNA gyrase, subunit A, subunit of
DE   DNA gyrase; EC=5.99.1 3; (ECOBB_1.PE2129).
GN   Name=gyrA; OrderedLocusNames=B21_02116, ECBD_1429, ECD_02157;
OS   ESCHERICHIA COLI BL21.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=511693;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOBB_1.PE2129.
CC       Escherichia coli (strain B / BL21) chromosome, complete sequence.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6E9X0_ECOBD
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; C6E9X0; C5W6X0; -.
DR   EMBL; CP001665; ACT28492.1; -; Genomic_DNA.
DR   EMBL; CP001509; ACT43980.1; -; Genomic_DNA.
DR   EMBL; AM946981; CAQ32633.1; -; Genomic_DNA.
DR   ProteinModelPortal; C6E9X0; -.
DR   STRING; C6E9X0; -.
DR   EnsemblBacteria; EBESCT00000158921; EBESCP00000149381; EBESCG00000156153.
DR   EnsemblBacteria; EBESCT00000189249; EBESCP00000176684; EBESCG00000187813.
DR   EnsemblBacteria; EBESCT00000194370; EBESCP00000180117; EBESCG00000193901.
DR   GenomeReviews; AM946981_GR; B21_02116.
DR   GenomeReviews; CP001509_GR; ECD_02157.
DR   GenomeReviews; CP001665_GR; ECBD_1429.
DR   KEGG; ebd:ECBD_1429; -.
DR   GeneTree; EBGT00050000010885; -.
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: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; ECOBB_1.PE2129; -.
DR   PRODOM; ECOBB_1_PE2129.
DR   SWISS-2DPAGE; ECOBB_1_PE2129.
KW   CAQ32633.1000068575old_1320000031;
KW   DNA gyrase, subunit A, subunit of DNA gyrase ;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   875 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
     KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
     RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT
     NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
     YIRARAEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG
     MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI IAAFVRHRRE
     VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA PTPAEAKTAL VANPWQLGNV
     AAMLERAGDD AARPEWLEPE FGVRDGLYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE
     LLDQIAELLR ILGSADRLME VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV
     VTLSHQGYVK YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY
     SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT ANGTVKKTVL
     TEFNRLRTAG KVAIKLVEGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG
     VRGIRLGEGD KVVSLIVPRG EGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN
     GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA
     EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE
//

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