(data stored in SCRATCH3701 zone)

HOGENOM6: ESCOL1_1_PE2215

ID   ESCOL1_1_PE2215                      STANDARD;      PRT;   875 AA.
AC   ESCOL1_1_PE2215; P0AES4; P09097;
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; (ESCOL1_1.PE2215).
GN   Name=gyrA; Synonyms=hisW, nalA, parD; OrderedLocusNames=b2231, JW2225;
OS   ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=511145;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ESCOL1_1.PE2215.
CC       Escherichia coli str. K-12 substr. MG1655 chromosome, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:GYRA_ECOLI
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. Can form a 2:2 complex with toxin
CC       CcdB in which GyrA is inactive; rejuvenation of GyrA(2)CcdB(2) is
CC       effected by CcdA.
CC   -!- INTERACTION:
CC       P0AES6:gyrB; NbExp=5; IntAct=EBI-547129, EBI-541911;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- MISCELLANEOUS: When the enzyme transiently cleaves DNA a
CC       phosphotyrosine bond is formed between GyrA and DNA. This enzyme-
CC       DNA intermediate is the target of a number of topoisomerase
CC       poisons, including toxin CcdB.
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P0AES4; P09097; -.
DR   EMBL; X06373; CAA29676.1; -; Genomic_DNA.
DR   EMBL; X06744; CAA29919.1; -; Genomic_DNA.
DR   EMBL; M15631; AAA23948.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75291.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16048.1; -; Genomic_DNA.
DR   EMBL; Y00544; CAA68611.1; -; Genomic_DNA.
DR   PIR; S02340; ITECAP.
DR   RefSeq; AP_002828.1; AC_000091.1.
DR   RefSeq; NP_416734.1; NC_000913.2.
DR   PDB; 1AB4; X-ray; 2.80 A; A=30-522.
DR   PDB; 1X75; X-ray; 2.80 A; A/B=363-494.
DR   PDB; 1ZI0; X-ray; 2.60 A; A/B=535-841.
DR   PDB; 2Y3P; X-ray; 2.62 A; A/B=2-523.
DR   PDB; 3KU8; X-ray; 1.93 A; A/B=363-497.
DR   PDB; 3NUH; X-ray; 3.10 A; A=1-525.
DR   PDBsum; 1AB4; -.
DR   PDBsum; 1X75; -.
DR   PDBsum; 1ZI0; -.
DR   PDBsum; 2Y3P; -.
DR   PDBsum; 3KU8; -.
DR   PDBsum; 3NUH; -.
DR   ProteinModelPortal; P0AES4; -.
DR   SMR; P0AES4; 30-522, 535-841.
DR   DIP; DIP-36179N; -.
DR   IntAct; P0AES4; 52.
DR   MINT; MINT-201682; -.
DR   SWISS-2DPAGE; P0AES4; -.
DR   ECO2DBASE; D101.5; 6TH EDITION.
DR   PRIDE; P0AES4; -.
DR   EnsemblBacteria; EBESCT00000004656; EBESCP00000004656; EBESCG00000003798.
DR   EnsemblBacteria; EBESCT00000017137; EBESCP00000016428; EBESCG00000016196.
DR   GeneID; 946614; -.
DR   GenomeReviews; AP009048_GR; JW2225.
DR   GenomeReviews; U00096_GR; b2231.
DR   KEGG; ecj:JW2225; -.
DR   KEGG; eco:b2231; -.
DR   EchoBASE; EB0418; -.
DR   EcoGene; EG10423; gyrA.
DR   eggNOG; COG0188; -.
DR   GeneTree; EBGT00050000010885; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; EcoCyc:EG10423-MON; -.
DR   BioCyc; MetaCyc:EG10423-MON; -.
DR   Genevestigator; P0AES4; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
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   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; ESCOL1_1.PE2215; -.
DR   PRODOM; ESCOL1_1_PE2215.
DR   SWISS-2DPAGE; ESCOL1_1_PE2215.
KW   3D-structure; Antibiotic resistance; ATP-binding; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; 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 KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG
     VRGIRLGEGD KVVSLIVPRG DGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN
     GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA
     EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE
//

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