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Protein

Repressor protein cI

Gene

cI

Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional repressor that allows virus to establish and maintain latency. Prevents both the viral DNA replication and the exit programs. Clamps the two operator OL (operator left made of OL1, OL2 and OL3 sites) and OR (operator right made of OR1, OR2 and OR3 sites) together by binding to them and arranging the intervening DNA in a loop. This step allows repression of lytic pR and pL promoters by binding to OL1, OL2, OR1 and OR2 simultaneously. The binding of cI on OR2 additionally activates the transcription of the cI gene thereby mediating an autoregulatory function to maintain the latent state. Once cI is present in sufficient amount, it can repress its own transcription by binding to OL3 and OR3.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi30 – 4920H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Latency-replication switch, Transcription, Transcription regulation, Viral latency

Keywords - Ligandi

DNA-binding

Protein family/group databases

MEROPSiS24.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Repressor protein cI
Gene namesi
Name:cI
Ordered Locus Names:lambdap88
OrganismiEnterobacteria phage lambda (Bacteriophage lambda)
Taxonomic identifieri10710 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000001711 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host1 Publication
Chaini2 – 237236Repressor protein cIPRO_0000149715Add
BLAST

Interactioni

Subunit structurei

Homooctamer. The DNA loop is maintained by octamers of repressor cI.

Protein-protein interaction databases

DIPiDIP-17006N.
IntActiP03034. 2 interactions.

Structurei

Secondary structure

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3021Combined sources
Helixi34 – 407Combined sources
Helixi45 – 528Combined sources
Helixi60 – 7011Combined sources
Helixi74 – 763Combined sources
Helixi79 – 857Combined sources
Turni90 – 923Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi166 – 1705Combined sources
Beta strandi180 – 1845Combined sources
Beta strandi190 – 1989Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi221 – 23010Combined sources
Helixi233 – 2364Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F39X-ray1.90A/B137-237[»]
1GFXmodel-A/B/C/D1-237[»]
1J5Gmodel-A/B/C/D1-237[»]
1KCAX-ray2.91A/B/C/D/E/F/G/H133-237[»]
1LLIX-ray2.10A/B2-93[»]
1LMBX-ray1.803/42-93[»]
1LRPX-ray3.20A/B/C2-93[»]
1LWQmodel-A/B/C/D1-237[»]
1RIOX-ray2.30A/B1-92[»]
3BDNX-ray3.91A/B2-237[»]
3KZ3X-ray1.64A/B8-85[»]
ProteinModelPortaliP03034.
SMRiP03034. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03034.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 7759HTH cro/C1-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
2.10.109.10. 1 hit.
InterProiIPR001387. 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]
PfamiPF01381. HTH_3. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF51306. SSF51306. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKKKPLTQ EQLEDARRLK AIYEKKKNEL GLSQESVADK MGMGQSGVGA
60 70 80 90 100
LFNGINALNA YNAALLAKIL KVSVEEFSPS IAREIYEMYE AVSMQPSLRS
110 120 130 140 150
EYEYPVFSHV QAGMFSPELR TFTKGDAERW VSTTKKASDS AFWLEVEGNS
160 170 180 190 200
MTAPTGSKPS FPDGMLILVD PEQAVEPGDF CIARLGGDEF TFKKLIRDSG
210 220 230
QVFLQPLNPQ YPMIPCNESC SVVGKVIASQ WPEETFG
Length:237
Mass (Da):26,212
Last modified:January 23, 2007 - v2
Checksum:i4785A4915479ED97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671A → T (PubMed:714163).Curated
Sequence conflicti118 – 1181E → K (PubMed:714163).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96581.1.
X00166 Genomic DNA. Translation: CAA24991.1.
PIRiA14086. RPBPL.
RefSeqiNP_040628.1. NC_001416.1.

Genome annotation databases

GeneIDi2703537.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96581.1.
X00166 Genomic DNA. Translation: CAA24991.1.
PIRiA14086. RPBPL.
RefSeqiNP_040628.1. NC_001416.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F39X-ray1.90A/B137-237[»]
1GFXmodel-A/B/C/D1-237[»]
1J5Gmodel-A/B/C/D1-237[»]
1KCAX-ray2.91A/B/C/D/E/F/G/H133-237[»]
1LLIX-ray2.10A/B2-93[»]
1LMBX-ray1.803/42-93[»]
1LRPX-ray3.20A/B/C2-93[»]
1LWQmodel-A/B/C/D1-237[»]
1RIOX-ray2.30A/B1-92[»]
3BDNX-ray3.91A/B2-237[»]
3KZ3X-ray1.64A/B8-85[»]
ProteinModelPortaliP03034.
SMRiP03034. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-17006N.
IntActiP03034. 2 interactions.

Protein family/group databases

MEROPSiS24.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703537.

Miscellaneous databases

EvolutionaryTraceiP03034.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
2.10.109.10. 1 hit.
InterProiIPR001387. 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]
PfamiPF01381. HTH_3. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF51306. SSF51306. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "DNA sequence of the bacteriophage gama cI gene."
    Sauer R.T.
    Nature 276:301-302(1977) [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(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-237.
  4. "Octamerization of lambda CI repressor is needed for effective repression of P(RM) and efficient switching from lysogeny."
    Dodd I.B., Perkins A.J., Tsemitsidis D., Egan J.B.
    Genes Dev. 15:3013-3022(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, OLIGOMERIZATION.
  5. "The bacteriophage lambda CI protein finds an asymmetric solution."
    Hochschild A., Lewis M.
    Curr. Opin. Struct. Biol. 19:79-86(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  6. "Multilevel autoregulation of lambda repressor protein CI by DNA looping in vitro."
    Lewis D., Le P., Zurla C., Finzi L., Adhya S.
    Proc. Natl. Acad. Sci. U.S.A. 108:14807-14812(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-93.
  8. "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(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-93.
  9. Chattopadhyaya R., Ghosh K.
    Submitted (FEB-1999) to the PDB data bank
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiRPC1_LAMBD
AccessioniPrimary (citable) accession number: P03034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.