| Tag | Content |
|---|
| CPLM ID | CPLM-002514 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Transcriptional regulatory protein TyrR |
Protein Synonyms/Alias | |
Gene Name | tyrR |
Gene Synonyms/Alias | b1323; JW1316 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 116 | SCQLFGQKLDRLRNH | acetylation | [1] | | 222 | HVVEQAQKLAMLSAP | acetylation | [1] | | 256 | QASPRAGKPYLALNC | acetylation | [1] | | 310 | MSPRMQAKLLRFLND | acetylation | [1] | | 349 | NLVELVQKGMFREDL | acetylation | [1] | | 398 | EQGVPRPKLAADLNT | acetylation | [1] | | 420 | PGNVRQLKNAIYRAL | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP gene have been observed at high phenylalanine concentrations. |
Sequence Annotation | DOMAIN 2 72 ACT.
DOMAIN 78 149 PAS.
DOMAIN 206 428 Sigma-54 factor interaction.
NP_BIND 234 241 ATP (Potential).
NP_BIND 290 299 ATP (Potential).
DNA_BIND 483 502 H-T-H motif (Potential). |
Keyword | 3D-structure; Activator; Aromatic hydrocarbons catabolism; ATP-binding; Complete proteome; Direct protein sequencing; DNA-binding; Nucleotide-binding; Reference proteome; Repressor; Transcription; Transcription regulation; Two-component regulatory system. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 513 AA |
Protein Sequence | MRLEVFCEDR LGLTRELLDL LVLRGIDLRG IEIDPIGRIY LNFAELEFES FSSLMAEIRR 60
IAGVTDVRTV PWMPSEREHL ALSALLEALP EPVLSVDMKS KVDMANPASC QLFGQKLDRL 120
RNHTAAQLIN GFNFLRWLES EPQDSHNEHV VINGQNFLME ITPVYLQDEN DQHVLTGAVV 180
MLRSTIRMGR QLQNVAAQDV SAFSQIVAVS PKMKHVVEQA QKLAMLSAPL LITGDTGTGK 240
DLFAYACHQA SPRAGKPYLA LNCASIPEDA VESELFGHAP EGKKGFFEQA NGGSVLLDEI 300
GEMSPRMQAK LLRFLNDGTF RRVGEDHEVH VDVRVICATQ KNLVELVQKG MFREDLYYRL 360
NVLTLNLPPL RDCPQDIMPL TELFVARFAD EQGVPRPKLA ADLNTVLTRY AWPGNVRQLK 420
NAIYRALTQL DGYELRPQDI LLPDYDAATV AVGEDAMEGS LDEITSRFER SVLTQLYRNY 480
PSTRKLAKRL GVSHTAIANK LREYGLSQKK NEE 513 |
Gene Ontology | GO:0032993; C:protein-DNA complex; IDA:EcoCyc. GO:0005524; F:ATP binding; IDA:EcoCyc. GO:0003677; F:DNA binding; IDA:EcoCyc. GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. GO:0004871; F:signal transducer activity; IEA:InterPro. GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:EcoCyc. GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |