Transcriptional regulatory protein TyrR - Enterobacter agglomerans (Erwinia herbicola)

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Q9ZIB7 (TYRR_ENTAG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transcriptional regulatory protein TyrR

Gene names

Name:

tyrR

Organism

Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)

Taxonomic identifier

549 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pantoea

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

Homodimer. In presence of tyrosine (to the lesser extent, phenylalanine or tryptophan) and excess of ATP it undergoes a ligand-induced hexamerization. It is suggested that the hexameric form of TyrR is the active repressing species, interacting with two or three tyrR boxes in the targeted regulatory DNA By similarity.

Sequence similarities

Contains 1 ACT domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Contains 1 sigma-54 factor interaction domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism Transcription Transcription regulation Two-component regulatory system
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Activator Repressor
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay signal transduction system Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid binding Inferred from electronic annotation. Source: InterPro nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 521

521

Transcriptional regulatory protein TyrR

PRO_0000081340

Regions

Domain

1 – 70

ACT

Domain

207 – 436

230

Sigma-54 factor interaction

Nucleotide binding

235 – 242

ATP Potential

Nucleotide binding

298 – 307

ATP Potential

DNA binding

490 – 509

H-T-H motif Potential

Experimental info

Mutagenesis

V → A: Decrease in ability to repress DNA transcription. Loss of activity; when associated with C-72 and G-201. Ref.1

Mutagenesis

Y → C: Decrease in ability to repress DNA transcription. Loss of activity; when associated with A-67 and G-201. Ref.1

Mutagenesis

D → G: Decrease in ability to repress DNA transcription; when associated with V-402. Ref.1

Mutagenesis

201

E → G: No effect. Loss of activity; when associated with A-67 and C-72. Ref.1

Mutagenesis

402

I → V: Decrease in ability to repress DNA transcription; when associated with G-97. Ref.1

Mutagenesis

499

V → I: No effect. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ZIB7 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 05896D0CFF5314BE
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FASTA

521

59,023

        10         20         30         40         50         60 
MRLEVFCQDR IGLARELLDL LVARSIDLRG IEVAASGRIY LNFSTLEFEQ FSNLMAEIRR 

        70         80         90        100        110        120 
TPGVTDVRTV PYMPSEREHR VLSALLVAMP EPVFSVDLRT KVELANPAAQ NLFNLDENKI 

       130        140        150        160        170        180 
RNFTADHLIN GFNFARWLES ERVQAQAQHV VIEGRDFLME AHPIYLSEDN DQADQLVGAM 

       190        200        210        220        230        240 
VMLKSTARMG RQLQNLVVTD ETEFDHIVAV TPRMRQVVEQ ARKLAMHDAP LLIIGDTGTG 

       250        260        270        280        290        300 
KDMLARACHL RSARGKMPFL ALNCASLPDD VAESELFGHA AGAYPNALEG KKGFFEQANG 

       310        320        330        340        350        360 
GSVLLDEIGE MSPTMQTKLL RFLNDGTFRR VGEEHEVHVN VRVICATQKN LFELVQRGEF 

       370        380        390        400        410        420 
REDLFYRLNV LTLNLPPLRE RVQDIMPLTE IFVARFADEQ GIPRPRLSSQ LNAFLMRYNW 

       430        440        450        460        470        480 
PGNVRQLKNA LYRALTQLEG HELRPQDIVL PEQALDVSLG EEAMEGTLDQ ITSRFERSIL 

       490        500        510        520 
TRLYLSYPST RKLAKRLGVS HTAIANKLRE YGLGQKRGDN E

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References

[1]

"Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression of tyrosine phenol-lyase."
Katayama T., Suzuki H., Koyanagi T., Kumagai H.
Appl. Environ. Microbiol. 66:4764-4771(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF VAL-67; TYR-72; ASP-97; GLU-201; ILE-402 AND VAL-499.
Strain: ATCC 21434 / AJ 2985.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF035010 Genomic DNA. Translation: AAD02000.1.
3D structure databases
ProteinModelPortal	Q9ZIB7.
SMR	Q9ZIB7. Positions 1-191.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.10.60. 1 hit.
InterPro	IPR003593. AAA+_ATPase. IPR002912. ACT_dom. IPR009057. Homeodomain-like. IPR000014. PAS. IPR002078. Sigma_54_int. IPR025662. Sigma_54_int_dom_ATP-bd_1. IPR025943. Sigma_54_int_dom_ATP-bd_2. IPR025944. Sigma_54_int_dom_CS. [Graphical view]
Pfam	PF01842. ACT. 1 hit. PF00158. Sigma54_activat. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. SM00091. PAS. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit.
PROSITE	PS50112. PAS. False negative. PS00675. SIGMA54_INTERACT_1. 1 hit. PS00676. SIGMA54_INTERACT_2. 1 hit. PS00688. SIGMA54_INTERACT_3. 1 hit. PS50045. SIGMA54_INTERACT_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TYRR_ENTAG

Accession

Primary (citable) accession number: Q9ZIB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents