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P0A7I4

- RF3_ECOLI

UniProt

P0A7I4 - RF3_ECOLI

Protein

Peptide chain release factor 3

Gene

prfC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 278GTPBy similarity
    Nucleotide bindingi88 – 925GTPBy similarity
    Nucleotide bindingi142 – 1454GTPBy similarity

    GO - Molecular functioni

    1. GDP binding Source: EcoCyc
    2. GTPase activity Source: EcoCyc
    3. GTP binding Source: UniProtKB-HAMAP
    4. translation release factor activity, codon nonspecific Source: EcoCyc
    5. translation release factor activity, codon specific Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GTP catabolic process Source: GOC
    2. regulation of translational termination Source: UniProtKB-HAMAP
    3. translational termination Source: EcoCyc

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12114-MONOMER.
    ECOL316407:JW5873-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide chain release factor 3
    Short name:
    RF-3
    Gene namesi
    Name:prfC
    Synonyms:miaD, tos
    Ordered Locus Names:b4375, JW5873
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12114. prfC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 529528Peptide chain release factor 3PRO_0000210938Add
    BLAST

    Proteomic databases

    PaxDbiP0A7I4.
    PRIDEiP0A7I4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7I4.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    pfkAP0A7961EBI-556252,EBI-554405

    Protein-protein interaction databases

    DIPiDIP-39402N.
    IntActiP0A7I4. 5 interactions.
    MINTiMINT-1229875.
    STRINGi511145.b4375.

    Structurei

    Secondary structure

    1
    529
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 117
    Beta strandi13 – 164
    Beta strandi21 – 255
    Helixi26 – 3510
    Turni36 – 383
    Helixi63 – 664
    Beta strandi75 – 795
    Beta strandi82 – 865
    Beta strandi93 – 953
    Helixi99 – 1035
    Beta strandi107 – 1148
    Turni115 – 1173
    Helixi121 – 13111
    Turni132 – 1343
    Beta strandi137 – 1426
    Helixi151 – 16212
    Beta strandi165 – 17410
    Helixi176 – 1783
    Beta strandi181 – 1844
    Turni185 – 1884
    Beta strandi189 – 1924
    Helixi213 – 2197
    Helixi221 – 23717
    Helixi243 – 2475
    Beta strandi250 – 2567
    Turni259 – 2624
    Helixi265 – 27511
    Beta strandi284 – 2863
    Beta strandi330 – 3334
    Turni334 – 3374
    Beta strandi338 – 3414
    Beta strandi349 – 3524
    Beta strandi370 – 3723
    Beta strandi379 – 3824
    Beta strandi409 – 4135
    Turni414 – 4185
    Beta strandi419 – 4246
    Beta strandi427 – 4304
    Beta strandi441 – 4433
    Helixi446 – 4527
    Helixi481 – 4888
    Beta strandi505 – 5084
    Helixi509 – 5168

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H5EX-ray2.80A/B1-529[»]
    2O0Felectron microscopy15.50A1-529[»]
    3SFSX-ray3.20W1-529[»]
    3UOQX-ray3.70W1-529[»]
    3ZVOX-ray3.80Y1-529[»]
    ProteinModelPortaliP0A7I4.
    SMRiP0A7I4. Positions 3-527.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7I4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 280270tr-type GAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG4108.
    HOGENOMiHOG000236725.
    KOiK02837.
    OMAiFHKTREH.
    OrthoDBiEOG6677Q1.
    PhylomeDBiP0A7I4.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00072. Rel_fac_3.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR027417. P-loop_NTPase.
    IPR004548. PrfC.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view]
    PfamiPF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54980. SSF54980. 1 hit.
    TIGRFAMsiTIGR00503. prfC. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7I4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLSPYLQEV AKRRTFAIIS HPDAGKTTIT EKVLLFGQAI QTAGTVKGRG    50
    SNQHAKSDWM EMEKQRGISI TTSVMQFPYH DCLVNLLDTP GHEDFSEDTY 100
    RTLTAVDCCL MVIDAAKGVE DRTRKLMEVT RLRDTPILTF MNKLDRDIRD 150
    PMELLDEVEN ELKIGCAPIT WPIGCGKLFK GVYHLYKDET YLYQSGKGHT 200
    IQEVRIVKGL NNPDLDAAVG EDLAQQLRDE LELVKGASNE FDKELFLAGE 250
    ITPVFFGTAL GNFGVDHMLD GLVEWAPAPM PRQTDTRTVE ASEDKFTGFV 300
    FKIQANMDPK HRDRVAFMRV VSGKYEKGMK LRQVRTAKDV VISDALTFMA 350
    GDRSHVEEAY PGDILGLHNH GTIQIGDTFT QGEMMKFTGI PNFAPELFRR 400
    IRLKDPLKQK QLLKGLVQLS EEGAVQVFRP ISNNDLIVGA VGVLQFDVVV 450
    ARLKSEYNVE AVYESVNVAT ARWVECADAK KFEEFKRKNE SQLALDGGDN 500
    LAYIATSMVN LRLAQERYPD VQFHQTREH 529
    Length:529
    Mass (Da):59,574
    Last modified:January 23, 2007 - v2
    Checksum:i2A1E6AE984C6B1C6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti315 – 3151V → L in CAA81223. (PubMed:8016077)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D17724 Genomic DNA. Translation: BAA04578.1.
    Z26313 Genomic DNA. Translation: CAA81223.1.
    U14003 Genomic DNA. Translation: AAA97271.1.
    U00096 Genomic DNA. Translation: AAC77328.1.
    AP009048 Genomic DNA. Translation: BAE78363.1.
    PIRiI59305.
    RefSeqiNP_418792.1. NC_000913.3.
    YP_492504.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77328; AAC77328; b4375.
    BAE78363; BAE78363; BAE78363.
    GeneIDi12932002.
    948897.
    KEGGiecj:Y75_p4258.
    eco:b4375.
    PATRICi32124360. VBIEscCol129921_4520.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D17724 Genomic DNA. Translation: BAA04578.1 .
    Z26313 Genomic DNA. Translation: CAA81223.1 .
    U14003 Genomic DNA. Translation: AAA97271.1 .
    U00096 Genomic DNA. Translation: AAC77328.1 .
    AP009048 Genomic DNA. Translation: BAE78363.1 .
    PIRi I59305.
    RefSeqi NP_418792.1. NC_000913.3.
    YP_492504.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H5E X-ray 2.80 A/B 1-529 [» ]
    2O0F electron microscopy 15.50 A 1-529 [» ]
    3SFS X-ray 3.20 W 1-529 [» ]
    3UOQ X-ray 3.70 W 1-529 [» ]
    3ZVO X-ray 3.80 Y 1-529 [» ]
    ProteinModelPortali P0A7I4.
    SMRi P0A7I4. Positions 3-527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-39402N.
    IntActi P0A7I4. 5 interactions.
    MINTi MINT-1229875.
    STRINGi 511145.b4375.

    Proteomic databases

    PaxDbi P0A7I4.
    PRIDEi P0A7I4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77328 ; AAC77328 ; b4375 .
    BAE78363 ; BAE78363 ; BAE78363 .
    GeneIDi 12932002.
    948897.
    KEGGi ecj:Y75_p4258.
    eco:b4375.
    PATRICi 32124360. VBIEscCol129921_4520.

    Organism-specific databases

    EchoBASEi EB2037.
    EcoGenei EG12114. prfC.

    Phylogenomic databases

    eggNOGi COG4108.
    HOGENOMi HOG000236725.
    KOi K02837.
    OMAi FHKTREH.
    OrthoDBi EOG6677Q1.
    PhylomeDBi P0A7I4.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12114-MONOMER.
    ECOL316407:JW5873-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7I4.
    PROi P0A7I4.

    Gene expression databases

    Genevestigatori P0A7I4.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00072. Rel_fac_3.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR027417. P-loop_NTPase.
    IPR004548. PrfC.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view ]
    Pfami PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54980. SSF54980. 1 hit.
    TIGRFAMsi TIGR00503. prfC. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the prfC gene, which encodes peptide-chain-release factor 3 of Escherichia coli."
      Mikuni O., Ito K., Mofatt J., Matsumura K., McCaughan K., Nobukuni T., Tate W., Nakamura Y.
      Proc. Natl. Acad. Sci. U.S.A. 91:5798-5802(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10.
      Strain: K12.
    2. "Localization and characterization of the gene encoding release factor RF3 in Escherichia coli."
      Grentzmann G., Brechemier-Baey D., Heurgue V., Mora L., Buckingham R.H.
      Proc. Natl. Acad. Sci. U.S.A. 91:5848-5852(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Osmo-expression and fast two-step purification of Escherichia coli translation termination factor RF-3."
      Mortensen K.K., Hansen H.F., Grentzmann G., Buckingham R.H., Sperling-Petersen H.U.
      Eur. J. Biochem. 234:732-736(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-19.
    7. "Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGA-containing stop signals."
      Grentzmann G., Brechemier-Baey D., Heurgue-Hamard V., Buckingham R.H.
      J. Biol. Chem. 270:10595-10600(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiRF3_ECOLI
    AccessioniPrimary (citable) accession number: P0A7I4
    Secondary accession number(s): P33998, Q2M5U3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3