P07012 (RF2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptide chain release factor 2
Short name=RF-2

Gene names

Name:	prfB
Synonyms:	supK
Ordered Locus Names:	b2891, JW5847

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. HAMAP MF_00094
Subcellular location	Cytoplasm HAMAP MF_00094.
Post-translational modification	Methylated by PrmC. Methylation increases the termination efficiency of RF2. Is absent when the factor is overproduced. Ref.3 Ref.7 Ref.8 Ref.9
Miscellaneous	The gene for this protein contains a UGA in-frame termination codon after Leu-25; a naturally occurring frameshift enables complete translation of RF-2. This provides a mechanism for the protein to regulate its own production. HAMAP MF_00094
Sequence similarities	Belongs to the prokaryotic/mitochondrial release factor family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Ribosomal frameshifting
PTM	Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	translation release factor activity, codon specific Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 365

365

Peptide chain release factor 2 HAMAP MF_00094

PRO_0000166816

Amino acid modifications

Modified residue

252

1

N5-methylglutamine Ref.3 Ref.7

Natural variations

Natural variant

246

1

T → A in strain: BL21 and MRE-600; increased termination efficiency. Ref.10

Experimental info

Mutagenesis

252

1

Q → E: Loss of methylation. Ref.7

Sequence conflict

201

1

L → V Ref.1

Sequence conflict

201

1

L → V Ref.2

Secondary structure

1

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365

Helix Strand Turn

Details...

Helix

6 – 24

19

Helix

27 – 42

16

Helix

44 – 48

5

Helix

50 – 90

41

Helix

93 – 113

21

Helix

114 – 118

5

Turn

122 – 125

4

Beta strand

128 – 134

7

Helix

138 – 158

21

Beta strand

162 – 170

9

Beta strand

172 – 185

14

Helix

188 – 192

5

Helix

193 – 195

3

Beta strand

197 – 204

8

Beta strand

208 – 210

3

Beta strand

213 – 224

12

Helix

236 – 238

3

Beta strand

239 – 244

6

Beta strand

260 – 265

6

Turn

266 – 268

3

Beta strand

271 – 274

4

Beta strand

276 – 278

3

Helix

280 – 306

27

Beta strand

321 – 327

7

Helix

328 – 330

3

Beta strand

332 – 335

4

Turn

336 – 338

3

Beta strand

341 – 343

3

Helix

345 – 349

5

Helix

354 – 362

9

Sequences

	Sequence		Length	Mass (Da)
	P07012 [UniParc]. Last modified November 1, 1997. Version 3. Checksum: EB8C802FDDE0A76D	FASTA	365	41,251
	10 20 30 40 50 60 MFEINPVNNR IQDLTERSDV LRGYLDYDAK KERLEEVNAE LEQPDVWNEP ERAQALGKER 70 80 90 100 110 120 SSLEAVVDTL DQMKQGLEDV SGLLELAVEA DDEETFNEAV AELDALEEKL AQLEFRRMFS 130 140 150 160 170 180 GEYDSADCYL DIQAGSGGTE AQDWASMLER MYLRWAESRG FKTEIIEESE GEVAGIKSVT 190 200 210 220 230 240 IKISGDYAYG WLRTETGVHR LVRKSPFDSG GRRHTSFSSA FVYPEVDDDI DIEINPADLR 250 260 270 280 290 300 IDVYRTSGAG GQHVNRTESA VRITHIPTGI VTQCQNDRSQ HKNKDQAMKQ MKAKLYELEM 310 320 330 340 350 360 QKKNAEKQAM EDNKSDIGWG SQIRSYVLDD SRIKDLRTGV ETRNTQAVLD GSLDQFIEAS LKAGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacterial peptide chain release factors: conserved primary structure and possible frameshift regulation of release factor 2." Craigen W.J., Cook R.G., Tate W.P., Caskey C.T. Proc. Natl. Acad. Sci. U.S.A. 82:3616-3620(1985) [PubMed: 3889910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-44.
[2]	"Rapid and precise mapping of the Escherichia coli release factor genes by two physical approaches." Lee C.C., Kohara Y., Akiyama K., Smith C.L., Craigen W.J., Caskey C.T. J. Bacteriol. 170:4537-4541(1988) [PubMed: 3049538] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation." Dincbas-Renqvist V., Engstroem A., Mora L., Heurgue-Hamard V., Buckingham R., Ehrenberg M. EMBO J. 19:6900-6907(2000) [PubMed: 11118225] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 246-256, METHYLATION AT GLN-252, MASS SPECTROMETRY. Strain: B / BL21, K12 / W3110 / ATCC 27325 / DSM 5911, K12 / Xac and MRE-600.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Chromosomal location and structure of the operon encoding peptide-chain-release factor 2 of Escherichia coli." Kawakami K., Joensson Y.H., Bjoerk G.R., Ikeda H., Nakamura Y. Proc. Natl. Acad. Sci. U.S.A. 85:5620-5624(1988) [PubMed: 2456575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-365.
[7]	"The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors." Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H. EMBO J. 21:769-778(2002) [PubMed: 11847124] [Abstract] Cited for: METHYLATION AT GLN-252 BY PRMC, MUTAGENESIS OF GLN-252. Strain: K12.
[8]	"HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination." Nakahigashi K., Kubo N., Narita S., Shimaoka T., Goto S., Oshima T., Mori H., Maeda M., Wada C., Inokuchi H. Proc. Natl. Acad. Sci. U.S.A. 99:1473-1478(2002) [PubMed: 11805295] [Abstract] Cited for: METHYLATION BY PRMC. Strain: K12.
[9]	"Methylation of bacterial release factors RF1 and RF2 is required for normal translation termination in vivo." Mora L., Heurgue-Hamard V., de Zamaroczy M., Kervestin S., Buckingham R.H. J. Biol. Chem. 282:35638-35645(2007) [PubMed: 17932046] [Abstract] Cited for: PTM, EFFECT OF METHYLATION. Strain: K12.
[10]	"Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1." Vestergaard B., Van L.B., Andersen G.R., Nyborg J., Buckingham R.H., Kjeldgaard M. Mol. Cell 8:1375-1382(2001) [PubMed: 11779511] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF MUTANT ALA-246. Strain: K12.
[11]	"A cryo-electron microscopic study of ribosome-bound termination factor RF2." Rawat U.B., Zavialov A.V., Sengupta J., Valle M., Grassucci R.A., Linde J., Vestergaard B., Ehrenberg M., Frank J. Nature 421:87-90(2003) [PubMed: 12511960] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.8 ANGSTROMS).
[12]	"Structure of the Escherichia coli ribosomal termination complex with release factor 2." Klaholz B.P., Pape T., Zavialov A.V., Myasnikov A.G., Orlova E.V., Vestergaard B., Ehrenberg M., van Heel M. Nature 421:90-94(2003) [PubMed: 12511961] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (14.0 ANGSTROMS) IN COMPLEX WITH THE RIBOSOME.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M11520 Genomic DNA. Translation: AAA24520.1.
U28375 Genomic DNA. Translation: AAA83072.1.
U00096 Genomic DNA. Translation: AAC75929.1.
AP009048 Genomic DNA. Translation: BAE76956.1.
J03795 Genomic DNA. Translation: AAA23958.1.

PIR

FCECR2. C65073.

RefSeq

NP_417367.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQE	X-ray	1.81	A	1-365	[»]
1MI6	electron microscopy	10.90	A	1-365	[»]
1ML5	electron microscopy	14.00	Z	1-365	[»]

ProteinModelPortal

P07012.

SMR

P07012. Positions 4-365.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10559N.

IntAct

P07012. 18 interactions.

MINT

MINT-1238444.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002308; EBESCP00000002308; EBESCG00000001883.
EBESCT00000016130; EBESCP00000015421; EBESCG00000015190.

GeneID

947369.

GenomeReviews

Gene locus JW5847 in contig AP009048_GR.
Gene locus b2891 in contig U00096_GR.

KEGG

ecj:JW5847.
eco:b2891.

PATRIC

32121192. VBIEscCol129921_2984.

Organism-specific databases

EchoBASE

EB0755.

EcoGene

EG10762. prfB.

Phylogenomic databases

eggNOG

COG1186.

GeneTree

EBGT00050000010290.

HOGENOM

HBG629764.

OMA

KNRAKAW.

PhylomeDB

P07012.

ProtClustDB

PRK00578.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10762-MONOMER.

Gene expression databases

Genevestigator

P07012.

Family and domain databases

HAMAP

MF_00094. Rel_fac_2.
[Tree]

InterPro

IPR005139. PCRF.
IPR000352. Pep_chain_release_fac_I_II.
IPR020853. Peptide_chain_release_fac2_bac.
IPR004374. PrfB.
[Graphical view]

KO

K02836.

PANTHER

PTHR11075:SF6. PrfB. 1 hit.

Pfam

PF03462. PCRF. 1 hit.
PF00472. RF-1. 1 hit.
[Graphical view]

SMART

SM00937. PCRF. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00020. PrfB. 1 hit.

PROSITE

PS00745. RF_PROK_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RF2_ECOLI

Accession

Primary (citable) accession number: P07012
Secondary accession number(s): P76642, Q2M9V0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program