Peptide chain release factor 3 - Escherichia coli (strain K12)

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P0A7I4 (RF3_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Peptide chain release factor 3
Short name=RF-3

Gene names

Name:	prfC
Synonyms:	miaD, tos
Ordered Locus Names:	b4375, JW5873

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP-Rule MF_00072
Subcellular location	Cytoplasm HAMAP-Rule MF_00072.
Sequence similarities	Belongs to the GTP-binding elongation factor family. PrfC subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of translational termination Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GDP binding Inferred from direct assay PubMed 11595190. Source: EcoCyc GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from direct assay PubMed 11595190. Source: EcoCyc translation release factor activity, codon nonspecific Inferred from direct assay PubMed 5289007. Source: EcoCyc translation release factor activity, codon specific Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pfkA	P0A796	1	EBI-556252,EBI-554405

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1 Ref.2 Ref.6

Chain

2 – 529

528

Peptide chain release factor 3 HAMAP-Rule MF_00072

PRO_0000210938

Regions

Nucleotide binding

20 – 27

GTP By similarity

Nucleotide binding

88 – 92

GTP By similarity

Nucleotide binding

142 – 145

GTP By similarity

Experimental info

Sequence conflict

315

V → L in CAA81223. Ref.2

Secondary structure

529

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7I4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2A1E6AE984C6B1C6
Show »

FASTA

529

59,574

        10         20         30         40         50         60 
MTLSPYLQEV AKRRTFAIIS HPDAGKTTIT EKVLLFGQAI QTAGTVKGRG SNQHAKSDWM 

        70         80         90        100        110        120 
EMEKQRGISI TTSVMQFPYH DCLVNLLDTP GHEDFSEDTY RTLTAVDCCL MVIDAAKGVE 

       130        140        150        160        170        180 
DRTRKLMEVT RLRDTPILTF MNKLDRDIRD PMELLDEVEN ELKIGCAPIT WPIGCGKLFK 

       190        200        210        220        230        240 
GVYHLYKDET YLYQSGKGHT IQEVRIVKGL NNPDLDAAVG EDLAQQLRDE LELVKGASNE 

       250        260        270        280        290        300 
FDKELFLAGE ITPVFFGTAL GNFGVDHMLD GLVEWAPAPM PRQTDTRTVE ASEDKFTGFV 

       310        320        330        340        350        360 
FKIQANMDPK HRDRVAFMRV VSGKYEKGMK LRQVRTAKDV VISDALTFMA GDRSHVEEAY 

       370        380        390        400        410        420 
PGDILGLHNH GTIQIGDTFT QGEMMKFTGI PNFAPELFRR IRLKDPLKQK QLLKGLVQLS 

       430        440        450        460        470        480 
EEGAVQVFRP ISNNDLIVGA VGVLQFDVVV ARLKSEYNVE AVYESVNVAT ARWVECADAK 

       490        500        510        520 
KFEEFKRKNE SQLALDGGDN LAYIATSMVN LRLAQERYPD VQFHQTREH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

I59305.

RefSeq

NP_418792.1. NC_000913.2.
YP_492504.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H5E	X-ray	2.80	A/B	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	[»]

ProteinModelPortal

P0A7I4.

SMR

P0A7I4. Positions 3-527.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39402N.

IntAct

P0A7I4. 4 interactions.

MINT

MINT-1229875.

STRING

511145.b4375.

Proteomic databases

PaxDb

P0A7I4.

PRIDE

P0A7I4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77328; AAC77328; b4375.
BAE78363; BAE78363; BAE78363.

GeneID

12932002.
948897.

KEGG

ecj:Y75_p4258.
eco:b4375.

PATRIC

32124360. VBIEscCol129921_4520.

Organism-specific databases

EchoBASE

EB2037.

EcoGene

EG12114. prfC.

Phylogenomic databases

eggNOG

COG4108.

HOGENOM

HOG000236725.

K02837.

OMA

SDFMEIE.

ProtClustDB

PRK00741.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0A7I4.

Family and domain databases

HAMAP

MF_00072. Rel_fac_3.

InterPro

IPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR027417. P-loop_NTPase.
IPR004548. PrfC.
IPR005225. Small_GTP-bd_dom.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

SUPFAM

SSF54980. EFG_III_V. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF50447. Translat_factor. 1 hit.

TIGRFAMs

TIGR00503. prfC. 1 hit.
TIGR00231. small_GTP. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7I4.

Entry information

Entry name

RF3_ECOLI

Accession

Primary (citable) accession number: P0A7I4
Secondary accession number(s): P33998, Q2M5U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents