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P03034

- RPC1_LAMBD

UniProt

P03034 - RPC1_LAMBD

Protein

Repressor protein cI

Gene

cI

Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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 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 – 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.
    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

    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

    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:
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 119 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