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Protein

Peptide chain release factor 3

Gene

prfC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

  • GDP binding Source: EcoCyc
  • GTPase activity Source: EcoCyc
  • GTP binding Source: UniProtKB-HAMAP
  • translation release factor activity, codon nonspecific Source: EcoCyc
  • translation release factor activity, codon specific Source: UniProtKB-HAMAP

GO - Biological processi

  • regulation of translational termination Source: UniProtKB-HAMAP
  • translational termination Source: EcoCyc
Complete GO annotation...

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12114. prfC.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

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
Helixi6 – 116Combined sources
Beta strandi13 – 208Combined sources
Helixi26 – 3510Combined sources
Beta strandi74 – 796Combined sources
Beta strandi82 – 876Combined sources
Helixi97 – 1015Combined sources
Helixi102 – 1054Combined sources
Beta strandi107 – 1148Combined sources
Turni115 – 1173Combined sources
Helixi121 – 13010Combined sources
Turni131 – 1344Combined sources
Beta strandi137 – 1426Combined sources
Helixi151 – 16212Combined sources
Beta strandi165 – 17410Combined sources
Helixi176 – 1783Combined sources
Beta strandi181 – 1844Combined sources
Turni185 – 1884Combined sources
Beta strandi189 – 1924Combined sources
Helixi213 – 2197Combined sources
Helixi221 – 23717Combined sources
Helixi243 – 2475Combined sources
Beta strandi250 – 2567Combined sources
Turni259 – 2624Combined sources
Helixi265 – 27511Combined sources
Beta strandi282 – 2865Combined sources
Beta strandi297 – 3037Combined sources
Beta strandi309 – 3124Combined sources
Beta strandi316 – 3238Combined sources
Beta strandi330 – 3334Combined sources
Turni334 – 3363Combined sources
Beta strandi339 – 3413Combined sources
Beta strandi364 – 3674Combined sources
Beta strandi378 – 3825Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi396 – 4049Combined sources
Helixi412 – 42110Combined sources
Beta strandi426 – 4305Combined sources
Beta strandi436 – 4427Combined sources
Helixi444 – 45613Combined sources
Beta strandi461 – 4644Combined sources
Beta strandi469 – 4757Combined sources
Helixi479 – 48810Combined sources
Helixi490 – 4923Combined sources
Beta strandi493 – 4953Combined sources
Beta strandi501 – 5077Combined sources
Helixi508 – 51710Combined sources
Beta strandi521 – 5288Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H5EX-ray2.80A/B1-529[»]
2O0Felectron microscopy15.50A1-529[»]
4V85X-ray3.20AW1-529[»]
4V89X-ray3.70AW1-529[»]
4V8OX-ray3.80AY1-529[»]
ProteinModelPortaliP0A7I4.
SMRiP0A7I4. Positions 3-529.
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.
InParanoidiP0A7I4.
KOiK02837.
OMAiPMTWPVG.
OrthoDBiEOG6677Q1.
PhylomeDBiP0A7I4.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00072. Rel_fac_3.
InterProiIPR009022. EFG_III-V.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR004548. PrfC.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF03144. 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

        10         20         30         40         50
MTLSPYLQEV AKRRTFAIIS HPDAGKTTIT EKVLLFGQAI QTAGTVKGRG
60 70 80 90 100
SNQHAKSDWM EMEKQRGISI TTSVMQFPYH DCLVNLLDTP GHEDFSEDTY
110 120 130 140 150
RTLTAVDCCL MVIDAAKGVE DRTRKLMEVT RLRDTPILTF MNKLDRDIRD
160 170 180 190 200
PMELLDEVEN ELKIGCAPIT WPIGCGKLFK GVYHLYKDET YLYQSGKGHT
210 220 230 240 250
IQEVRIVKGL NNPDLDAAVG EDLAQQLRDE LELVKGASNE FDKELFLAGE
260 270 280 290 300
ITPVFFGTAL GNFGVDHMLD GLVEWAPAPM PRQTDTRTVE ASEDKFTGFV
310 320 330 340 350
FKIQANMDPK HRDRVAFMRV VSGKYEKGMK LRQVRTAKDV VISDALTFMA
360 370 380 390 400
GDRSHVEEAY PGDILGLHNH GTIQIGDTFT QGEMMKFTGI PNFAPELFRR
410 420 430 440 450
IRLKDPLKQK QLLKGLVQLS EEGAVQVFRP ISNNDLIVGA VGVLQFDVVV
460 470 480 490 500
ARLKSEYNVE AVYESVNVAT ARWVECADAK KFEEFKRKNE SQLALDGGDN
510 520
LAYIATSMVN LRLAQERYPD VQFHQTREH
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:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

EnsemblBacteriaiAAC77328; AAC77328; b4375.
BAE78363; BAE78363; BAE78363.
GeneIDi948897.
KEGGiecj:Y75_p4258.
eco:b4375.
PATRICi32124360. VBIEscCol129921_4520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H5EX-ray2.80A/B1-529[»]
2O0Felectron microscopy15.50A1-529[»]
4V85X-ray3.20AW1-529[»]
4V89X-ray3.70AW1-529[»]
4V8OX-ray3.80AY1-529[»]
ProteinModelPortaliP0A7I4.
SMRiP0A7I4. Positions 3-529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP0A7I4.
PRIDEiP0A7I4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77328; AAC77328; b4375.
BAE78363; BAE78363; BAE78363.
GeneIDi948897.
KEGGiecj:Y75_p4258.
eco:b4375.
PATRICi32124360. VBIEscCol129921_4520.

Organism-specific databases

EchoBASEiEB2037.
EcoGeneiEG12114. prfC.

Phylogenomic databases

eggNOGiCOG4108.
HOGENOMiHOG000236725.
InParanoidiP0A7I4.
KOiK02837.
OMAiPMTWPVG.
OrthoDBiEOG6677Q1.
PhylomeDBiP0A7I4.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7I4.
PROiP0A7I4.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00072. Rel_fac_3.
InterProiIPR009022. EFG_III-V.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR004548. PrfC.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF03144. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 95 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

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.