Phage lambda cI:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

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Standard name

cI

Synonyms

cI, lambdap88

Product description

repressor

EC number (for enzymes)


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Notes

Function

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<protect> Gene Ontology See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0004175

endopeptidase activity

PMID:14733611[1]

IDA: Inferred from Direct Assay

F

complete

GO:0097264

self proteolysis

PMID:14733611[1]

IDA: Inferred from Direct Assay

P

complete

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Interactions <protect> See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence
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Notes

Localization

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Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence 
MSTKKKPLTQ EQLEDARRLK AIYEKKKNEL GLSQESVADK MGMGQSGVGA LFNGINALNA
YNAALLAKIL KVSVEEFSPS IAREIYEMYE AVSMQPSLRS EYEYPVFSHV QAGMFSPELR
TFTKGDAERW VSTTKKASDS AFWLEVEGNS MTAPTGSKPS FPDGMLILVD PEQAVEPGDF
CIARLGGDEF TFKKLIRDSG QVFLQPLNPQ YPMIPCNESC SVVGKVIASQ WPEETFG
Length

237

Mol. Wt

26.211 kDa

pI

4.9 (calculated)

Extinction coefficient

26,930 - 27,305 (calc based on 7 Y, 3 W, and 3 C residues)

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Domains/Motifs/Modification Sites

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Type Residues Description Notes References

Domain

19 - 77

HTH cro/C1-type

UniProt:P03034


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Structure

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Structures

<beststructure> gene=Phage_lambda_cI taxon=10710 </beststructure>

Models

View models at:

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Structure figures

See Help:Jmol in EcoliWiki

full length lambda repressor bound to operator DNA
<jmol> <jmolApplet> <color>white</color> <uploadedFileContents >3BDN.pdb</uploadedFileContents> <script> wireframe off; spacefill off; trace off; reset;center {11.954998 19.6415 35.014}; rotate z 95.96; rotate y 86.35; rotate z 117.3; cartoon; select protein; color chain; </script> </jmolApplet> </jmol>
<jmol> <jmolCheckbox > <scriptWhenChecked > rotate on; </scriptWhenChecked > <scriptWhenUnchecked > rotate off; </scriptWhenUnchecked > <checked>false</checked> <text>rotate</text> </jmolCheckbox > <jmolButton><script>reset; reset;center {11.954998 19.6415 35.014}; rotate z 95.96; rotate y 86.35; rotate z 117.3; cartoon; select protein; color chain; </script><text>reset</text></jmolButton> </jmol>









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Notes

Lambda repressor consists of an N-terminal DNA binding domain and a C-terminal oligomerization domain, connected by a flexible linker. The N-terminal domain in isolation dimerizes weakly through helix 5-helix 5 contacts. The C-terminal domain is required for dimerization and DNA binding at normal in vivo expression levels. Induction of phage lambda by the SOS response involves autoproteolysis at a specific site in the linker by the C-domain.

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes
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Notes

Links

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Name URL Comments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 Ghosh, K et al. (2004) pH-dependent autocleavage of lambda repressor occurs in the operator-bound form: characterization of lambda repressor autocleavage. Biochem. J. 379 325-30 PubMed

Categories

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