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P03034

- RPC1_LAMBD

UniProt

P03034 - RPC1_LAMBD

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Protein
Repressor protein cI
Gene
cI, lambdap88
Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed - 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 motif
Add
BLAST

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
Complete GO annotation...

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: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host1 Publication
Chaini2 – 237236Repressor protein cI
PRO_0000149715Add
BLAST

Interactioni

Subunit structurei

Homooctamer. The DNA loop is maintained by octamers of repressor cI.1 Publication

Protein-protein interaction databases

DIPiDIP-17006N.
IntActiP03034. 2 interactions.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP03034.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 7759HTH cro/C1-type
Add
BLAST

Sequence similaritiesi

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

MSTKKKPLTQ EQLEDARRLK AIYEKKKNEL GLSQESVADK MGMGQSGVGA    50
LFNGINALNA YNAALLAKIL KVSVEEFSPS IAREIYEMYE AVSMQPSLRS 100
EYEYPVFSHV QAGMFSPELR TFTKGDAERW VSTTKKASDS AFWLEVEGNS 150
MTAPTGSKPS FPDGMLILVD PEQAVEPGDF CIARLGGDEF TFKKLIRDSG 200
QVFLQPLNPQ YPMIPCNESC SVVGKVIASQ WPEETFG 237
Length:237
Mass (Da):26,212
Last modified:January 23, 2007 - v2
Checksum:i4785A4915479ED97
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671A → T1 Publication
Sequence conflicti118 – 1181E → K1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
J02459 Genomic DNA. Translation: AAA96581.1 .
X00166 Genomic DNA. Translation: CAA24991.1 .
PIRi A14086. RPBPL.
RefSeqi NP_040628.1. NC_001416.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F39 X-ray 1.90 A/B 137-237 [» ]
1GFX model - A/B/C/D 1-237 [» ]
1J5G model - A/B/C/D 1-237 [» ]
1KCA X-ray 2.91 A/B/C/D/E/F/G/H 133-237 [» ]
1LLI X-ray 2.10 A/B 2-93 [» ]
1LMB X-ray 1.80 3/4 2-93 [» ]
1LRP X-ray 3.20 A/B/C 2-93 [» ]
1LWQ model - A/B/C/D 1-237 [» ]
1RIO X-ray 2.30 A/B 1-92 [» ]
3BDN X-ray 3.91 A/B 2-237 [» ]
3KZ3 X-ray 1.64 A/B 8-85 [» ]
ProteinModelPortali P03034.
SMRi P03034. Positions 2-237.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-17006N.
IntActi P03034. 2 interactions.

Protein family/group databases

MEROPSi S24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2703537.

Miscellaneous databases

EvolutionaryTracei P03034.

Family and domain databases

Gene3Di 1.10.260.40. 1 hit.
2.10.109.10. 1 hit.
InterProi IPR001387. 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 ]
Pfami PF01381. HTH_3. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view ]
SMARTi SM00530. HTH_XRE. 1 hit.
[Graphical view ]
SUPFAMi SSF47413. SSF47413. 1 hit.
SSF51306. SSF51306. 1 hit.
PROSITEi PS50943. HTH_CROC1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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. "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(2001) [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(2009) [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(2011) [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(1983) [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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-93.
  9. Chattopadhyaya R., Ghosh K.
    Submitted (MAR-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: July 9, 2014
This is version 118 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

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