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P03034 (RPC1_LAMBD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Repressor protein CI
Gene names
Name:CI
OrganismEnterobacteria phage lambda (Bacteriophage lambda) [Reference proteome]
Taxonomic identifier10710 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Repressor protein CI allows phage lambda to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein CI to the OR and OL operators, preventing transcription of proteins necessary for lytic development.

Subunit structure

The active form is believed to be composed of 2 identical chains. The dimeric form binds more strongly to the lambda operator sites than does the monomer.

Miscellaneous

Bacterial cells harboring a lysogenic lambda phage are immune to further infection by lambda. The CI repressor protein inhibits the lytic development of any additional infecting phage particles. The region of the genome that codes for the CI repressor protein is known as the immunity region.

Sequence similarities

Contains 1 HTH cro/C1-type DNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host Ref.3
Chain2 – 237236Repressor protein CI
PRO_0000149715

Regions

Domain19 – 7759HTH cro/C1-type
DNA binding30 – 4920H-T-H motif

Experimental info

Sequence conflict671A → T Ref.2
Sequence conflict1181E → K Ref.2

Secondary structure

............................. 237
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03034 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4785A4915479ED97

FASTA23726,212
        10         20         30         40         50         60 
MSTKKKPLTQ EQLEDARRLK AIYEKKKNEL GLSQESVADK MGMGQSGVGA LFNGINALNA 

        70         80         90        100        110        120 
YNAALLAKIL KVSVEEFSPS IAREIYEMYE AVSMQPSLRS EYEYPVFSHV QAGMFSPELR 

       130        140        150        160        170        180 
TFTKGDAERW VSTTKKASDS AFWLEVEGNS MTAPTGSKPS FPDGMLILVD PEQAVEPGDF 

       190        200        210        220        230 
CIARLGGDEF TFKKLIRDSG QVFLQPLNPQ YPMIPCNESC SVVGKVIASQ WPEETFG 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of bacteriophage lambda DNA."
Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.
J. Mol. Biol. 162:729-773(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"DNA sequence of the bacteriophage gama cI gene."
Sauer R.T.
Nature 276:301-302(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Primary structure of the lambda repressor."
Sauer R.T., Anderegg R.
Biochemistry 17:1092-1100(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-237.
[4]"Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda."
Ohlendorf D.H., Anderson W.F., Lewis M., Pabo C.O., Matthews B.W.
J. Mol. Biol. 169:757-769(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-93.
[5]"Structure of the lambda complex at 2.5-A resolution: details of the repressor-operator interactions."
Jordan S.R., Pabo C.O.
Science 242:893-898(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-93.
[6]Chattopadhyaya R., Ghosh K.
Submitted (MAR-1999) to the PDB data bank
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02459 Genomic DNA. Translation: AAA96581.1.
X00166 Genomic DNA. Translation: CAA24991.1.
PIRRPBPL. A14086.
RefSeqNP_040628.1. NC_001416.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F39X-ray1.90A/B137-236[»]
1GFXmodel-A/B/C/D1-237[»]
1J5Gmodel-A/B/C/D1-237[»]
1KCAX-ray2.91A/B/C/D/E/F/G/H137-236[»]
1LLIX-ray2.10A/B2-92[»]
1LMBX-ray1.803/42-92[»]
1LRPX-ray3.20A/B/C2-93[»]
1LWQmodel-A/B/C/D1-237[»]
1RIOX-ray2.30A/B1-91[»]
3BDNX-ray3.91A/B2-237[»]
3KZ3X-ray1.64A/B8-85[»]
ProteinModelPortalP03034.
SMRP03034. Positions 2-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-17006N.
IntActP03034. 2 interactions.

Protein family/group databases

MEROPSS24.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703537.

Phylogenomic databases

ProtClustDBCLSP2509562.

Family and domain databases

Gene3D1.10.260.40. 1 hit.
2.10.109.10. 1 hit.
InterProIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
[Graphical view]
PfamPF01381. HTH_3. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
SMARTSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMSSF47413. SSF47413. 1 hit.
SSF51306. SSF51306. 1 hit.
PROSITEPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03034.

Entry information

Entry nameRPC1_LAMBD
AccessionPrimary (citable) accession number: P03034
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references