MG1655
W3110
Search for
Japanese | English
Gene Report : tyrR
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)  
     Deletion 20 (LD)  ,  OCR70,L90-5 (LD 20-1_P/O) (D)  ,  OCR70,L90-6 (LD 20-1_P/O & 20-2TC) (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  tyrR
Related strains
     Strains Search Search strains by gene name:  tyrR   Search strains by all related name:  tyrR b1323 ECK1319 JW1316

General information  (Go to Linear View:)
 Gene Name tyrR  
 Alternative name b1323,ECK1319,JW1316  
 Location, Length 1,384,744 - 1,386,285 (  +  ) ;   29.85 min ; 1542 (bp) ,   513 (aa) Go to Linear View
 Product DNA-binding transcriptional dual regulator, tyrosine-binding  
 Operon Name ycjXF-tyrR  
 Note transcriptional regulation of aroF, aroG, tyrA and aromatic amino acid transport; GO_component: GO:0005737 - cytoplasm; GO_function: GO:0016563 - transcription activator activity; GO_function: GO:0016564 - transcription repressor activity; GO_process: GO:0006350 - transcription  
 Function regulator; Transport of small molecules: Amino acids, amines  
 Gene Ontology GO:0000160 ; two-component signal transduction system (phosphorelay) ( tyrR )
GO:0000166 ; nucleotide binding ( tyrR )
GO:0003677 ; DNA binding ( tyrR )
GO:0004871 ; signal transducer activity ( tyrR )
GO:0005515 ; protein binding ( tyrR )
GO:0005524 ; ATP binding ( tyrR )
GO:0005622 ; intracellular ( tyrR )
GO:0006350 ; transcription ( tyrR )
GO:0006355 ; regulation of transcription, DNA-dependent ( tyrR )
GO:0007165 ; signal transduction ( tyrR )
GO:0008134 ; transcription factor binding ( tyrR )
GO:0008152 ; metabolic process ( tyrR )
GO:0016597 ; amino acid binding ( tyrR )
GO:0017111 ; nucleoside-triphosphatase activity ( tyrR )
GO:0019439 ; aromatic compound catabolic process ( tyrR )
GO:0045449 ; regulation of transcription ( tyrR )
 PID 1787583  
 EC number
  (KEGG Pathway)
 
 
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene tyrR ( EG11042 )  
    Number of removed 0 aa cleaved  
SWISS-PROT  ( Show details [ 2 more] )
  botton Entry name(Acc.no) TYRR_ECOLI ( P07604 )
    -  Protein name Transcriptional regulatory protein tyrR.  
    -  Synonyms  
    -  Gene name Name=tyrR; OrderedLocusNames=b1323;  

 Linear View (Whole Mode)
View Location
   1375.0  –  1400.0 (KBP)

Homology Analysis
BLAST
    Bacteria
         GTOP tyrR (  homologous genes of other bacterias  )  
    PDB     (database updated : 2007.02.20 )
         PSI-BLAST Chain A, Crystal Structure Of A Sigma54-Activator Suggests The Mechanism For The Conformational Switch Necessary For Sigma54 Binding  
    SWISS-PROT     (database updated : 2007.02.20 )
         BLAST Transcriptional regulatory protein tyrR  
         PSI-BLAST Chaperone clpB
    nr     (database updated : 2007.02.20 )
         BLAST DNA-binding transcriptional dual regulator, tyrosine-binding [Escherichia coli K12]  
Pfam 28.0   (database updated : 2015-05 )
    Pfam
PROSITE
    PROSITE ASN_GLYCOSYLATION    PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    MYRISTYL    AMIDATION    SIGMA54_INTERACT_1    SIGMA54_INTERACT_2    SIGMA54_INTERACT_3     

Other Cross-Reference
    COG COG3283KE 
    EcoCyc tyrR 

MMBR References
J Bacteriol. 1994;176:6921-6930
Regulation of aroL expression by TyrR protein and Trp repressor in Escherichia coli K-12.
Lawley, B., and J. Pittard.
J Bacteriol. 1971;107(1):8-15.
Regulation of tyrosine biosynthesis in Escherichia coli K-12: isolation and characterization of operator mutants.
Mattern IE, Pittard J. ( 4397929 )
Mol Microbiol. 1991;5(7):1585-92.
TyrR protein of Escherichia coli and its role as repressor and activator.
Pittard AJ, Davidson BE. ( 1943694 )
J Bacteriol. 1969;97(3):1234-41.
Regulator gene controlling enzymes concerned in tyrosine biosynthesis in Escherichia coli.
Wallace BJ, Pittard J. ( 4887504 )
Mol Gen Genet. 1981;181(3):373-8.
D-Amino acid dehydrogenase of Escherichia coli K12: positive selection of mutants defective in enzyme activity and localization of the structural gene.
Wild J, Klopotowski T. ( 6113535 )
J Bacteriol. 1993;175:6372-6375
Mutations in the tyrR gene of Escherichia coli which affect TyrR-mediated activation but not TyrR-mediated repression.
Yang, J., H. Camakaris, and A. J. Pittard.
J Bacteriol. 1993;175:1767-1776
A genetic analysis of various functions of the TyrR protein of Escherichia coli.
Yang, J., S. Ganesan, J. P. Sarsero, and A. J. Pittard.
J Bacteriol. 1971;108(1):386-99.
Repression of aromatic amino acid biosynthesis in Escherichia coli K-12.
Brown KD, Somerville RL. ( 4399341 )
J Bacteriol. 1982;150(1):70-5.
Autoregulation of the tyrR gene.
Camakaris H, Pittard J. ( 6120934 )
Mol Gen Genet. 1978;160(2):225-9.
Laboratoire de Chimie Bacterienne C.N.R.S., Marsielle, France.
Chippaux M, Giudici D, Abou-Jaoude A, Casse F, Pascal MC. ( 349355 )
J Bacteriol. 1980;144(3):877-83.
Formation of a lambda (Tn10) tyrR+ specialized transducing bacteriophage from Escherichia coli K-12.
Cobbett CS, Pittard J. ( 6254949 )
J Bacteriol. 1982;152(3):1276-9.
Cloning and characterization of Escherichia coli K-12 regulator gene tyrR.
Cornish EC, Davidson BE, Pittard J. ( 6754703 )
J Biol Chem. 1986;261:403-410
Structure of the Escherichia coli K12 regulatory gene tyrR: nucleotide sequence and sites of initiation of transcription and translation.
Cornish, E. C., V. P. Argyropoulos, J. Pittard, and B. E. Davidson.
J Bacteriol. 1992;174(11):3832-3.
Physical map location and transcriptional orientation of the tyrR gene of Escherichia coli K-12.
Cui J, Somerville RL. ( 1592836 )
J Bacteriol. 1993;175:1777-1784
A mutational analysis of the structural basis for transcriptional activation and monomer-monomer interaction in the TyrR system of Escherichia coli.
Cui, J., and R. L. Somerville.

Sequences
Amino acid
FASTA format
0001 MRLEVFCEDR LGLTRELLDL LVLRGIDLRG IEIDPIGRIY LNFAELEFES FSSLMAEIRR IAGVTDVRTV 
0071 PWMPSEREHL ALSALLEALP EPVLSVDMKS KVDMANPASC QLFGQKLDRL RNHTAAQLIN GFNFLRWLES 
0141 EPQDSHNEHV VINGQNFLME ITPVYLQDEN DQHVLTGAVV MLRSTIRMGR QLQNVAAQDV SAFSQIVAVS 
0211 PKMKHVVEQA QKLAMLSAPL LITGDTGTGK DLFAYACHQA SPRAGKPYLA LNCASIPEDA VESELFGHAP 
0281 EGKKGFFEQA NGGSVLLDEI GEMSPRMQAK LLRFLNDGTF RRVGEDHEVH VDVRVICATQ KNLVELVQKG 
0351 MFREDLYYRL NVLTLNLPPL RDCPQDIMPL TELFVARFAD EQGVPRPKLA ADLNTVLTRY AWPGNVRQLK 
0421 NAIYRALTQL DGYELRPQDI LLPDYDAATV AVGEDAMEGS LDEITSRFER SVLTQLYRNY PSTRKLAKRL 
0491 GVSHTAIANK LREYGLSQKK NEE

Nucleotide
FASTA format

View sequence out neighbor 100bp
-100                                             TTTCCGTCTT TGTGTCAATG ATTGTTGACA 
-070 GAAACCTTCC TGCTATCCAA ATAGTGTCAT ATCATCATAT TAATTGTTCT TTTTTCAGGT GAAGGTTCCC 
0001 atgcgtctgg aagtcttttg tgaagaccga ctcggtctga cccgcgaatt actcgatcta ctcgtgctaa 
0071 gaggcattga tttacgcggt attgagattg atcccattgg gcgaatctac ctcaattttg ctgaactgga 
0141 gtttgagagt ttcagcagtc tgatggccga aatacgccgt attgcgggtg ttaccgatgt gcgtactgtc 
0211 ccgtggatgc cttccgaacg tgagcatctg gcgttgagcg cgttactgga ggcgttgcct gaacctgtgc 
0281 tctctgtcga tatgaaaagc aaagtggata tggcgaaccc ggcgagctgt cagctttttg ggcaaaaatt 
0351 ggatcgcctg cgcaaccata ccgccgcaca attgattaac ggctttaatt ttttacgttg gctggaaagc 
0421 gaaccgcaag attcgcataa cgagcatgtc gttattaatg ggcagaattt cctgatggag attacgcctg 
0491 tttatcttca ggatgaaaat gatcaacacg tcctgaccgg tgcggtggtg atgttgcgat caacgattcg 
0561 tatgggccgc cagttgcaaa atgtcgccgc ccaggacgtc agcgccttca gtcaaattgt cgccgtcagc 
0631 ccgaaaatga agcatgttgt cgaacaggcg cagaaactgg cgatgctaag cgcgccgctg ctgattacgg 
0701 gtgacacagg tacaggtaaa gatctctttg cctacgcctg ccatcaggca agccccagag cgggcaaacc 
0771 ttacctggcg ctgaactgtg cgtctatacc ggaagatgcg gtcgagagtg aactgtttgg tcatgctccg 
0841 gaagggaaga aaggattctt tgagcaggcg aacggtggtt cggtgctgtt ggatgaaata ggggaaatgt 
0911 caccacggat gcaggcgaaa ttactgcgtt tccttaatga tggcactttc cgtcgggttg gcgaagacca 
0981 tgaggtgcat gtcgatgtgc gggtgatttg cgctacgcag aagaatctgg tcgaactggt gcaaaaaggc 
1051 atgttccgtg aagatctcta ttatcgtctg aacgtgttga cgctcaatct gccgccgcta cgtgactgtc 
1121 cgcaggacat catgccgtta actgagctgt tcgtcgcccg ctttgccgac gagcagggcg tgccgcgtcc 
1191 gaaactggcc gctgacctga atactgtact tacgcgttat gcgtggccgg gaaatgtgcg gcagttaaag 
1261 aacgctatct atcgcgcact gacacaactg gacggttatg agctgcgtcc acaggatatt ttgttgccgg 
1331 attatgacgc cgcaacggta gccgtgggcg aagatgcgat ggaaggttcg ctggacgaaa tcaccagccg 
1401 ttttgaacgc tcggtattaa cccagcttta tcgcaattat cccagcacgc gcaaactggc aaaacgtctc 
1471 ggcgtttcac ataccgcgat tgccaataag ttgcgggaat atggtctgag tcagaagaag aacgaagagt 
1541 aaGCGCGAAT ATGCCTGATG GTGCAACACC ATCAGGCATA TTAAATTATG CTTTCAGTAC AGCCAGAGCT 
1611 GCTTCGTAAT CCGGCTCGGT GGTGATTTCA TC