RF2_ECOLI
ID RF2_ECOLI Reviewed; 365 AA.
AC P07012; P76642; Q2M9V0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Peptide chain release factor RF2;
DE Short=RF-2;
GN Name=prfB; Synonyms=supK; OrderedLocusNames=b2891, JW5847;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-44, AND EXPRESSION
RP REGULATION.
RX PubMed=3889910; DOI=10.1073/pnas.82.11.3616;
RA Craigen W.J., Cook R.G., Tate W.P., Caskey C.T.;
RT "Bacterial peptide chain release factors: conserved primary structure and
RT possible frameshift regulation of release factor 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3616-3620(1985).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=3049538; DOI=10.1128/jb.170.10.4537-4541.1988;
RA Lee C.C., Kohara Y., Akiyama K., Smith C.L., Craigen W.J., Caskey C.T.;
RT "Rapid and precise mapping of the Escherichia coli release factor genes by
RT two physical approaches.";
RL J. Bacteriol. 170:4537-4541(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 246-256, FUNCTION,
RP METHYLATION AT GLN-252, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21, K12 / W3110 / ATCC 27325 / DSM 5911, K12 / Xac, and
RC MRE-600;
RX PubMed=11118225; DOI=10.1093/emboj/19.24.6900;
RA Dincbas-Renqvist V., Engstroem A., Mora L., Heurgue-Hamard V.,
RA Buckingham R., Ehrenberg M.;
RT "A post-translational modification in the GGQ motif of RF2 from Escherichia
RT coli stimulates termination of translation.";
RL EMBO J. 19:6900-6907(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-365.
RX PubMed=2456575; DOI=10.1073/pnas.85.15.5620;
RA Kawakami K., Joensson Y.H., Bjoerk G.R., Ikeda H., Nakamura Y.;
RT "Chromosomal location and structure of the operon encoding peptide-chain-
RT release factor 2 of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5620-5624(1988).
RN [7]
RP METHYLATION AT GLN-252 BY PRMC, AND MUTAGENESIS OF GLN-252.
RC STRAIN=K12;
RX PubMed=11847124; DOI=10.1093/emboj/21.4.769;
RA Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H.;
RT "The hemK gene in Escherichia coli encodes the N(5)-glutamine
RT methyltransferase that modifies peptide release factors.";
RL EMBO J. 21:769-778(2002).
RN [8]
RP METHYLATION BY PRMC.
RC STRAIN=K12;
RX PubMed=11805295; DOI=10.1073/pnas.032488499;
RA Nakahigashi K., Kubo N., Narita S., Shimaoka T., Goto S., Oshima T.,
RA Mori H., Maeda M., Wada C., Inokuchi H.;
RT "HemK, a class of protein methyl transferase with similarity to DNA methyl
RT transferases, methylates polypeptide chain release factors, and hemK
RT knockout induces defects in translational termination.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1473-1478(2002).
RN [9]
RP FUNCTION, PTM, AND EFFECT OF METHYLATION.
RC STRAIN=K12;
RX PubMed=17932046; DOI=10.1074/jbc.m706076200;
RA Mora L., Heurgue-Hamard V., de Zamaroczy M., Kervestin S., Buckingham R.H.;
RT "Methylation of bacterial release factors RF1 and RF2 is required for
RT normal translation termination in vivo.";
RL J. Biol. Chem. 282:35638-35645(2007).
RN [10]
RP FUNCTION IN RIBOSOME RESCUE, AND MUTAGENESIS OF PRO-206 AND GLN-252.
RC STRAIN=B, and K12;
RX PubMed=22857598; DOI=10.1111/j.1365-2958.2012.08190.x;
RA Chadani Y., Ito K., Kutsukake K., Abo T.;
RT "ArfA recruits release factor 2 to rescue stalled ribosomes by peptidyl-
RT tRNA hydrolysis in Escherichia coli.";
RL Mol. Microbiol. 86:37-50(2012).
RN [11]
RP FUNCTION IN RIBOSOME RESCUE, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22922063; DOI=10.1016/j.jmb.2012.08.007;
RA Shimizu Y.;
RT "ArfA recruits RF2 into stalled ribosomes.";
RL J. Mol. Biol. 423:624-631(2012).
RN [12]
RP FUNCTION IN RIBOSOME RESCUE, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25355516; DOI=10.1093/nar/gku1069;
RA Kurita D., Chadani Y., Muto A., Abo T., Himeno H.;
RT "ArfA recognizes the lack of mRNA in the mRNA channel after RF2 binding for
RT ribosome rescue.";
RL Nucleic Acids Res. 42:13339-13352(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF MUTANT ALA-246.
RC STRAIN=K12;
RX PubMed=11779511; DOI=10.1016/s1097-2765(01)00415-4;
RA Vestergaard B., Van L.B., Andersen G.R., Nyborg J., Buckingham R.H.,
RA Kjeldgaard M.;
RT "Bacterial polypeptide release factor RF2 is structurally distinct from
RT eukaryotic eRF1.";
RL Mol. Cell 8:1375-1382(2001).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.8 ANGSTROMS) IN COMPLEX WITH 70S
RP RIBOSOME, AND SUBUNIT.
RX PubMed=12511960; DOI=10.1038/nature01224;
RA Rawat U.B., Zavialov A.V., Sengupta J., Valle M., Grassucci R.A., Linde J.,
RA Vestergaard B., Ehrenberg M., Frank J.;
RT "A cryo-electron microscopic study of ribosome-bound termination factor
RT RF2.";
RL Nature 421:87-90(2003).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (14.0 ANGSTROMS) IN COMPLEX WITH 70S
RP RIBOSOME, AND SUBUNIT.
RX PubMed=12511961; DOI=10.1038/nature01225;
RA Klaholz B.P., Pape T., Zavialov A.V., Myasnikov A.G., Orlova E.V.,
RA Vestergaard B., Ehrenberg M., van Heel M.;
RT "Structure of the Escherichia coli ribosomal termination complex with
RT release factor 2.";
RL Nature 421:90-94(2003).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH 70S
RP RIBOSOME AND ARFA, FUNCTION IN RIBOSOME RESCUE, INTERACTION WITH ARFA, AND
RP MUTAGENESIS OF ARG-200; SER-205; 221-PHE--TYR-223 AND 322-GLN-ILE-323.
RC STRAIN=B;
RX PubMed=27906160; DOI=10.1038/nature20822;
RA Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
RT "Mechanistic insights into the alternative translation termination by ArfA
RT and RF2.";
RL Nature 541:550-553(2017).
RN [17] {ECO:0007744|PDB:5MGP}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 6-364 IN COMPLEX WITH
RP 70S RIBOSOME AND ARFA, FUNCTION IN RIBOSOME RESCUE, INTERACTION WITH ARFA,
RP AND MUTAGENESIS OF GLN-252.
RX PubMed=27906161; DOI=10.1038/nature20821;
RA Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R.,
RA Wilson D.N.;
RT "Structural basis for ArfA-RF2-mediated translation termination on mRNAs
RT lacking stop codons.";
RL Nature 541:546-549(2017).
RN [18] {ECO:0007744|PDB:5MDV, ECO:0007744|PDB:5MDW}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) IN COMPLEX WITH 70S
RP RIBOSOME AND ARFA, FUNCTION IN RIBOSOME RESCUE, AND INTERACTION WITH ARFA.
RX PubMed=27934701; DOI=10.1126/science.aai9127;
RA James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
RT "Translational termination without a stop codon.";
RL Science 354:1437-1440(2016).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 1-365 IN COMPLEX WITH
RP 70S RIBOSOME AND ARFA, FUNCTION IN RIBOSOME RESCUE, INTERACTION WITH RF2,
RP INTERACTION WITH 16S RRNA, AND METHYLATION AT GLN-252.
RX PubMed=28077875; DOI=10.1038/nature21053;
RA Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
RA Jin H.;
RT "Structural basis of co-translational quality control by ArfA and RF2 bound
RT to ribosome.";
RL Nature 541:554-557(2017).
CC -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC translation in response to the peptide chain termination codons UGA and
CC UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA
CC hydrolase (PubMed:22857598, PubMed:27934701). In the presence of
CC truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the
CC GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase
CC center and releases the ribosome (PubMed:27906160, PubMed:27906161,
CC PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled
CC ribosomes in the absence of a normal stop codon (PubMed:22857598,
CC PubMed:22922063, PubMed:25355516). {ECO:0000269|PubMed:11118225,
CC ECO:0000269|PubMed:17932046, ECO:0000269|PubMed:22857598,
CC ECO:0000269|PubMed:22922063, ECO:0000269|PubMed:25355516,
CC ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
CC ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875,
CC ECO:0000305|PubMed:22857598}.
CC -!- SUBUNIT: Interacts with the ribosome (PubMed:22857598, PubMed:22922063,
CC PubMed:25355516, PubMed:12511960, PubMed:12511961). Recruited to
CC stalled ribosomes by ArfA, in the presence of truncated mRNA, ArfA
CC influences RF2 conformation so RF2 can hydrolyze the peptidyl-tRNA bond
CC (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875).
CC {ECO:0000269|PubMed:12511960, ECO:0000269|PubMed:12511961,
CC ECO:0000269|PubMed:22857598, ECO:0000269|PubMed:22922063,
CC ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27906160,
CC ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701,
CC ECO:0000269|PubMed:28077875}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Recruited to the 70S ribosome by
CC ArfA even in the absence of mRNA (PubMed:22922063, PubMed:25355516,
CC PubMed:27934701). {ECO:0000269|PubMed:22922063,
CC ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27934701}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. Is absent when the factor is overproduced.
CC {ECO:0000269|PubMed:11118225, ECO:0000269|PubMed:11805295,
CC ECO:0000269|PubMed:11847124, ECO:0000269|PubMed:17932046}.
CC -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC termination codon after Leu-25; a naturally occurring frameshift
CC enables complete translation of RF-2. This provides a mechanism for the
CC protein to regulate its own production. {ECO:0000269|PubMed:22857598}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M11520; AAA24520.1; -; Genomic_DNA.
DR EMBL; U28375; AAA83072.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75929.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76956.1; -; Genomic_DNA.
DR EMBL; J03795; AAA23958.1; -; Genomic_DNA.
DR PIR; C65073; FCECR2.
DR RefSeq; NP_417367.1; NC_000913.3.
DR RefSeq; WP_010723217.1; NZ_LN832404.1.
DR PDB; 1GQE; X-ray; 1.81 A; A=1-365.
DR PDB; 1MI6; EM; 10.90 A; A=1-365.
DR PDB; 1ML5; EM; 14.00 A; Z=1-365.
DR PDB; 5CZP; X-ray; 3.30 A; QY/XY=1-365.
DR PDB; 5DFE; X-ray; 3.10 A; QY/XY=1-365.
DR PDB; 5H5U; EM; 3.00 A; 4=1-365.
DR PDB; 5MDV; EM; 2.97 A; 7=1-365.
DR PDB; 5MDW; EM; 3.06 A; 7=1-365.
DR PDB; 5MGP; EM; 3.10 A; z=6-364.
DR PDB; 5U4I; EM; 3.50 A; v=1-365.
DR PDB; 5U4J; EM; 3.70 A; v=1-365.
DR PDB; 5U9F; EM; 3.20 A; Z=1-365.
DR PDB; 5U9G; EM; 3.20 A; Z=1-365.
DR PDB; 6C4H; EM; 3.10 A; v=1-365.
DR PDB; 6C4I; EM; 3.24 A; v=1-365.
DR PDB; 6OG7; EM; 3.30 A; 8=1-365.
DR PDB; 6OST; EM; 4.20 A; 7=4-365.
DR PDB; 6OT3; EM; 3.90 A; A=6-362.
DR PDB; 6OUO; EM; 3.70 A; A=6-362.
DR PDB; 7O1C; EM; 2.60 A; B9=1-365.
DR PDB; 7OJ0; EM; 3.50 A; 8=1-365.
DR PDBsum; 1GQE; -.
DR PDBsum; 1MI6; -.
DR PDBsum; 1ML5; -.
DR PDBsum; 5CZP; -.
DR PDBsum; 5DFE; -.
DR PDBsum; 5H5U; -.
DR PDBsum; 5MDV; -.
DR PDBsum; 5MDW; -.
DR PDBsum; 5MGP; -.
DR PDBsum; 5U4I; -.
DR PDBsum; 5U4J; -.
DR PDBsum; 5U9F; -.
DR PDBsum; 5U9G; -.
DR PDBsum; 6C4H; -.
DR PDBsum; 6C4I; -.
DR PDBsum; 6OG7; -.
DR PDBsum; 6OST; -.
DR PDBsum; 6OT3; -.
DR PDBsum; 6OUO; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7OJ0; -.
DR AlphaFoldDB; P07012; -.
DR SMR; P07012; -.
DR BioGRID; 4259706; 136.
DR BioGRID; 851692; 1.
DR DIP; DIP-10559N; -.
DR IntAct; P07012; 65.
DR STRING; 511145.b2891; -.
DR iPTMnet; P07012; -.
DR jPOST; P07012; -.
DR PaxDb; P07012; -.
DR PRIDE; P07012; -.
DR EnsemblBacteria; AAC75929; AAC75929; b2891.
DR EnsemblBacteria; BAE76956; BAE76956; BAE76956.
DR GeneID; 947369; -.
DR KEGG; ecj:JW5847; -.
DR KEGG; eco:b2891; -.
DR PATRIC; fig|511145.12.peg.2984; -.
DR EchoBASE; EB0755; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_220733_1_0_6; -.
DR InParanoid; P07012; -.
DR OMA; YVFHPYQ; -.
DR PhylomeDB; P07012; -.
DR BioCyc; EcoCyc:EG10762-MON; -.
DR EvolutionaryTrace; P07012; -.
DR PRO; PR:P07012; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IDA:EcoCyc.
DR GO; GO:0006415; P:translational termination; IDA:EcoCyc.
DR HAMAP; MF_00094; Rel_fac_2; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004374; PrfB.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00020; prfB; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Methylation;
KW Protein biosynthesis; Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..365
FT /note="Peptide chain release factor RF2"
FT /id="PRO_0000166816"
FT MOTIF 250..252
FT /note="GGQ motif"
FT MOD_RES 252
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:11118225,
FT ECO:0000269|PubMed:11847124, ECO:0000269|PubMed:28077875"
FT VARIANT 246
FT /note="T -> A (in strain: BL21 and MRE-600; increased
FT termination efficiency)"
FT /evidence="ECO:0000269|PubMed:11118225,
FT ECO:0000305|PubMed:17932046"
FT MUTAGEN 200
FT /note="R->C: About 50% ribosome rescue activity with ArfA,
FT initial rate."
FT /evidence="ECO:0000269|PubMed:27906160"
FT MUTAGEN 205
FT /note="S->C: About 50% ribosome rescue activity with ArfA,
FT initial rate."
FT /evidence="ECO:0000269|PubMed:27906160"
FT MUTAGEN 206
FT /note="P->T: No effect on ArfA rescue of stalled
FT ribosomes."
FT /evidence="ECO:0000269|PubMed:22857598"
FT MUTAGEN 221..223
FT /note="FVY->AVA: About 5% ribosome rescue activity with
FT ArfA, initial rate."
FT /evidence="ECO:0000269|PubMed:27906160"
FT MUTAGEN 252
FT /note="Q->E: Loss of methylation. No longer allows ArfA to
FT rescue stalled ribosomes."
FT /evidence="ECO:0000269|PubMed:11847124,
FT ECO:0000269|PubMed:22857598, ECO:0000269|PubMed:27906161"
FT MUTAGEN 322..323
FT /note="QI->AA: About 20% ribosome rescue activity with
FT ArfA, initial rate."
FT /evidence="ECO:0000269|PubMed:27906160"
FT CONFLICT 201
FT /note="L -> V (in Ref. 1; AAA24520 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 6..24
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 50..90
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 93..113
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:1GQE"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 138..158
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 172..185
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 213..224
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1GQE"
FT TURN 252..256
FT /evidence="ECO:0007829|PDB:6C4H"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:1GQE"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 280..306
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1GQE"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:1GQE"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 345..349
FT /evidence="ECO:0007829|PDB:1GQE"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:1GQE"
SQ SEQUENCE 365 AA; 41251 MW; EB8C802FDDE0A76D CRC64;
MFEINPVNNR IQDLTERSDV LRGYLDYDAK KERLEEVNAE LEQPDVWNEP ERAQALGKER
SSLEAVVDTL DQMKQGLEDV SGLLELAVEA DDEETFNEAV AELDALEEKL AQLEFRRMFS
GEYDSADCYL DIQAGSGGTE AQDWASMLER MYLRWAESRG FKTEIIEESE GEVAGIKSVT
IKISGDYAYG WLRTETGVHR LVRKSPFDSG GRRHTSFSSA FVYPEVDDDI DIEINPADLR
IDVYRTSGAG GQHVNRTESA VRITHIPTGI VTQCQNDRSQ HKNKDQAMKQ MKAKLYELEM
QKKNAEKQAM EDNKSDIGWG SQIRSYVLDD SRIKDLRTGV ETRNTQAVLD GSLDQFIEAS
LKAGL
