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P0A7I4

- RF3_ECOLI

UniProt

P0A7I4 - RF3_ECOLI

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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

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
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12114. prfC.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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.

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.
InParanoidiP0A7I4.
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

        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:
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.
InParanoidi P0A7I4.
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

« 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: October 29, 2014
This is version 88 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