YFIA_ECOLI
ID YFIA_ECOLI Reviewed; 113 AA.
AC P0AD49; P11285;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ribosome-associated inhibitor A {ECO:0000303|PubMed:11375931};
DE AltName: Full=Protein Y {ECO:0000303|PubMed:10535924};
DE Short=pY {ECO:0000303|PubMed:11375931};
DE AltName: Full=Ribosome associated factor Y {ECO:0000303|PubMed:12392550};
DE AltName: Full=Spot Y {ECO:0000303|PubMed:10535924};
GN Name=raiA {ECO:0000303|PubMed:11375931}; Synonyms=yfiA {ECO:0000305};
GN OrderedLocusNames=b2597, JW2578;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6396419; DOI=10.1016/0022-2836(84)90269-9;
RA Hudson G.S., Davidson B.E.;
RT "Nucleotide sequence and transcription of the phenylalanine and tyrosine
RT operons of Escherichia coli K12.";
RL J. Mol. Biol. 180:1023-1051(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Faber F., van Giezen M., van Gorcom R.F.M., Harder W.;
RT "Identification of two Escherichia coli K12 proteins which are induced in
RT response to pollutant stress.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 77-113.
RX PubMed=2254312; DOI=10.1016/s0021-9258(18)45772-9;
RA Gavini N., Davidson B.E.;
RT "pheAo mutants of Escherichia coli have a defective pheA attenuator.";
RL J. Biol. Chem. 265:21532-21535(1990).
RN [7]
RP PROTEIN SEQUENCE OF 2-18, FUNCTION IN STABILIZATION OF THE RIBOSOME,
RP INTERACTION WITH THE RIBOSOMAL 30S SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=MRE-600;
RX PubMed=10535924; DOI=10.1073/pnas.96.22.12345;
RA Agafonov D.E., Kolb V.A., Nazimov I.V., Spirin A.S.;
RT "A protein residing at the subunit interface of the bacterial ribosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12345-12349(1999).
RN [8]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 2-13, FUNCTION, INTERACTION WITH 70S AND 100S
RP RIBOSOMES, AND INDUCTION.
RC STRAIN=K12 / MC4100 / AD202;
RX PubMed=11168583; DOI=10.1046/j.1365-2443.2000.00389.x;
RA Maki Y., Yoshida H., Wada A.;
RT "Two proteins, YfiA and YhbH, associated with resting ribosomes in
RT stationary phase Escherichia coli.";
RL Genes Cells 5:965-974(2000).
RN [10]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [12]
RP FUNCTION IN BLOCKING OF THE RIBOSOMAL A-SITE, FUNCTION IN INHIBITION OF
RP TRANSLATION, INDUCTION BY COLD SHOCK, AND GENE NAME.
RC STRAIN=MRE-600;
RX PubMed=11375931; DOI=10.1093/embo-reports/kve091;
RA Agafonov D.E., Kolb V.A., Spirin A.S.;
RT "Ribosome-associated protein that inhibits translation at the aminoacyl-
RT tRNA binding stage.";
RL EMBO Rep. 2:399-402(2001).
RN [13]
RP FUNCTION IN THE REDUCTION OF TRANSLATION ERRORS.
RX PubMed=15219834; DOI=10.1016/j.bbrc.2004.05.171;
RA Agafonov D.E., Spirin A.S.;
RT "The ribosome-associated inhibitor A reduces translation errors.";
RL Biochem. Biophys. Res. Commun. 320:354-358(2004).
RN [14]
RP FUNCTION IN THE PREVENTION OF 70S RIBOSOME DIMERIZATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16324148; DOI=10.1111/j.1365-2443.2005.00903.x;
RA Ueta M., Yoshida H., Wada C., Baba T., Mori H., Wada A.;
RT "Ribosome binding proteins YhbH and YfiA have opposite functions during
RT 100S formation in the stationary phase of Escherichia coli.";
RL Genes Cells 10:1103-1112(2005).
RN [15]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17277072; DOI=10.1128/jb.01713-06;
RA Bubunenko M., Baker T., Court D.L.;
RT "Essentiality of ribosomal and transcription antitermination proteins
RT analyzed by systematic gene replacement in Escherichia coli.";
RL J. Bacteriol. 189:2844-2853(2007).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [17]
RP FUNCTION, INDUCTION BY COLD SHOCK, AND DISRUPTION PHENOTYPE.
RC STRAIN=MRE-600;
RX PubMed=23420694; DOI=10.1002/mbo3.68;
RA Di Pietro F., Brandi A., Dzeladini N., Fabbretti A., Carzaniga T.,
RA Piersimoni L., Pon C.L., Giuliodori A.M.;
RT "Role of the ribosome-associated protein PY in the cold-shock response of
RT Escherichia coli.";
RL MicrobiologyOpen 2:293-307(2013).
RN [18]
RP STRUCTURE BY NMR.
RX PubMed=12470636; DOI=10.1016/s0006-291x(02)02721-3;
RA Rak A., Kalinin A., Shcherbakov D., Bayer P.;
RT "Solution structure of the ribosome-associated cold shock response protein
RT Yfia of Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 299:710-714(2002).
RN [19]
RP STRUCTURE BY NMR OF 2-113.
RX PubMed=12392550; DOI=10.1046/j.1432-1033.2002.03222.x;
RA Ye K., Serganov A., Hu W., Garber M., Patel D.J.;
RT "Ribosome-associated factor Y adopts a fold resembling a double-stranded
RT RNA binding domain scaffold.";
RL Eur. J. Biochem. 269:5182-5191(2002).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (11.50 ANGSTROMS) OF 2-91 BOUND TO THE E.COLI 70S
RP RIBOSOME, FUNCTION IN INHIBITION OF TRANSLATION, BLOCKING OF A-AND P-SITES,
RP AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=15502846; DOI=10.1038/nsmb850;
RA Vila-Sanjurjo A., Schuwirth B.S., Hau C.W., Cate J.H.;
RT "Structural basis for the control of translation initiation during
RT stress.";
RL Nat. Struct. Mol. Biol. 11:1054-1059(2004).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) BOUND TO THE T.THERMOPHILUS 70S
RP RIBOSOME, FUNCTION, AND SUBUNIT.
RX PubMed=22605777; DOI=10.1126/science.1218538;
RA Polikanov Y.S., Blaha G.M., Steitz T.A.;
RT "How hibernation factors RMF, HPF, and YfiA turn off protein synthesis.";
RL Science 336:915-918(2012).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) BOUND TO THE T.THERMOPHILUS
RP RIBOSOME, SUBUNIT, AND RRNA-BINDING.
RX PubMed=25775268; DOI=10.1038/nsmb.2992;
RA Polikanov Y.S., Melnikov S.V., Soll D., Steitz T.A.;
RT "Structural insights into the role of rRNA modifications in protein
RT synthesis and ribosome assembly.";
RL Nat. Struct. Mol. Biol. 22:342-344(2015).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-98 BOUND TO THE T.THERMOPHILUS
RP RIBOSOME WITH EUKARYOTIC ANTIMICROBIAL PEPTIDES, AND SUBUNIT.
RX PubMed=26792896; DOI=10.1093/nar/gkv1545;
RA Seefeldt A.C., Graf M., Perebaskine N., Nguyen F., Arenz S.,
RA Mardirossian M., Scocchi M., Wilson D.N., Innis C.A.;
RT "Structure of the mammalian antimicrobial peptide Bac7(1-16) bound within
RT the exit tunnel of a bacterial ribosome.";
RL Nucleic Acids Res. 44:2429-2438(2016).
CC -!- FUNCTION: During stationary phase prevents 70S dimer formation,
CC probably in order to regulate translation efficiency during transition
CC between the exponential and the stationary phases (PubMed:16324148).
CC During environmental stress such as cold shock or excessive cell
CC density at stationary phase, stabilizes the 70S ribosome against
CC dissociation, inhibits translation elongation and increases translation
CC accuracy (PubMed:11375931, PubMed:15219834). When normal growth
CC conditions are restored, is quickly released from the ribosome
CC (PubMed:11375931). Has been suggested to inhibit translation elongation
CC by blocking the A-site (aminoacyl-tRNA site) (PubMed:11375931). Has
CC also been suggested to inhibit translation initiation by blocking the
CC A-site and P-site (peptidyl-tRNA site) of the ribosome
CC (PubMed:15502846, PubMed:23420694). At 15 degrees Celsius binds 30S
CC subunits and stimulates their association with 50S subunits into idle
CC 70S ribosomes (PubMed:23420694). Crystallization with T.thermophilus
CC 70S ribosomes shows it binds in the channel between the head and body
CC of the 30S subunit, where mRNA, tRNAs, initiation factors IF1 and IF3
CC and elongation factor G would bind; this protein's extended tail
CC follows the mRNA channel and probably prevents RMF binding, which would
CC prevent ribosome dimerization (PubMed:22605777). This protein also
CC stabilizes the 30S head relative to the rest of the ribosome, which may
CC also prevent dimerization (PubMed:22605777). Counteracts miscoding
CC (translation errors) particularly efficiently at magnesium
CC concentrations close to those observed in vivo but less efficiently at
CC higher concentrations (PubMed:15219834). Counteraction of miscoding was
CC shown to be stronger than inhibition of translation, suggesting that
CC the former activity could be the main function of this protein in vivo
CC (PubMed:15219834). {ECO:0000269|PubMed:10535924,
CC ECO:0000269|PubMed:11168583, ECO:0000269|PubMed:11375931,
CC ECO:0000269|PubMed:15219834, ECO:0000269|PubMed:15502846,
CC ECO:0000269|PubMed:16324148, ECO:0000269|PubMed:22605777,
CC ECO:0000269|PubMed:23420694}.
CC -!- SUBUNIT: Associates mainly with 70S ribosomes (PubMed:11168583,
CC PubMed:11375931). Localized at the surface of the 30S ribosomal
CC subunit, at the interface with the 50S subunit (PubMed:10535924,
CC PubMed:15502846, PubMed:22605777). Binds across the channel in the 30S
CC subunit where tRNAs and mRNA interact during protein biosynthesis
CC (PubMed:15502846, PubMed:22605777). Can also associate with 100S
CC ribosomes, which are inactive dimers of 70S ribosomes
CC (PubMed:11168583). Contacts modifed methylated residues of 16S rRNA (in
CC complex with T.thermophilus ribosome, 2/3 residues are also modified in
CC E.coli) (PubMed:25775268). {ECO:0000269|PubMed:10535924,
CC ECO:0000269|PubMed:11168583, ECO:0000269|PubMed:11375931,
CC ECO:0000269|PubMed:15502846, ECO:0000269|PubMed:22605777,
CC ECO:0000269|PubMed:25775268, ECO:0000269|PubMed:26792896}.
CC -!- INTERACTION:
CC P0AD49; P0A805: frr; NbExp=4; IntAct=EBI-1129692, EBI-1114349;
CC -!- INDUCTION: During stationary phase (at protein level) (PubMed:11168583,
CC PubMed:11375931). Also by cold stress, remains ribosome-associated for
CC the 4 hours tested, then disappears when cells are warmed (at protein
CC level) (PubMed:11375931, PubMed:23420694).
CC {ECO:0000269|PubMed:11168583, ECO:0000269|PubMed:11375931,
CC ECO:0000269|PubMed:23420694}.
CC -!- MASS SPECTROMETRY: Mass=12640; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10535924};
CC -!- DISRUPTION PHENOTYPE: Non-essential gene, increased formation of
CC inactive 100S ribosomes in stationary phase, which persist longer than
CC in wild-type. Double hpr-yfiA deletion mutants form 90S ribosomes
CC (PubMed:16324148). A quadruple yfiA-hpf-rmf-sra knockout strain is
CC significantly outcompeted by wild-type after 4 days growth
CC (PubMed:17277072). No visible effect on viability or growth rate at 37
CC or 10 degrees Celsius, slight effect on bulk translation and timing of
CC expression of some cold-shock proteins (PubMed:23420694).
CC {ECO:0000269|PubMed:16324148, ECO:0000269|PubMed:17277072,
CC ECO:0000269|PubMed:23420694}.
CC -!- SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family.
CC YfiA subfamily. {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; M10431; AAA24328.1; -; Genomic_DNA.
DR EMBL; Z70523; CAA94436.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75646.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16481.1; -; Genomic_DNA.
DR EMBL; M58024; AAA62782.1; -; Genomic_DNA.
DR PIR; A30275; Q5ECPA.
DR RefSeq; NP_417088.1; NC_000913.3.
DR RefSeq; WP_000178456.1; NZ_STEB01000040.1.
DR PDB; 1L4S; NMR; -; A=2-113.
DR PDB; 1N3G; NMR; -; A=1-113.
DR PDB; 4V4G; X-ray; 11.50 A; a=2-91.
DR PDB; 4V8I; X-ray; 2.70 A; AY/CY=1-113.
DR PDB; 4Y4O; X-ray; 2.30 A; 1y/2y=1-113.
DR PDB; 5FDU; X-ray; 2.90 A; 1x/2x=2-98.
DR PDB; 5FDV; X-ray; 2.80 A; 1x/2x=2-98.
DR PDB; 5V8I; X-ray; 3.25 A; 1y/2y=1-113.
DR PDB; 6CFK; X-ray; 2.70 A; 1y/2y=1-113.
DR PDB; 6FKR; X-ray; 3.20 A; 1z/2z=2-98.
DR PDB; 6XHX; X-ray; 2.55 A; 1y/2y=1-113.
DR PDB; 7MD7; X-ray; 2.80 A; 1y/2y=1-113.
DR PDB; 7RQA; X-ray; 2.40 A; 1y/2y=1-113.
DR PDB; 7RQB; X-ray; 2.45 A; 1y/2y=1-113.
DR PDB; 7RQC; X-ray; 2.50 A; 1y/2y=1-113.
DR PDB; 7RQD; X-ray; 2.50 A; 1y/2y=1-113.
DR PDB; 7RQE; X-ray; 2.40 A; 1y/2y=1-113.
DR PDBsum; 1L4S; -.
DR PDBsum; 1N3G; -.
DR PDBsum; 4V4G; -.
DR PDBsum; 4V8I; -.
DR PDBsum; 4Y4O; -.
DR PDBsum; 5FDU; -.
DR PDBsum; 5FDV; -.
DR PDBsum; 5V8I; -.
DR PDBsum; 6CFK; -.
DR PDBsum; 6FKR; -.
DR PDBsum; 6XHX; -.
DR PDBsum; 7MD7; -.
DR PDBsum; 7RQA; -.
DR PDBsum; 7RQB; -.
DR PDBsum; 7RQC; -.
DR PDBsum; 7RQD; -.
DR PDBsum; 7RQE; -.
DR AlphaFoldDB; P0AD49; -.
DR BMRB; P0AD49; -.
DR SMR; P0AD49; -.
DR BioGRID; 4261618; 36.
DR BioGRID; 851463; 2.
DR DIP; DIP-36014N; -.
DR IntAct; P0AD49; 7.
DR STRING; 511145.b2597; -.
DR iPTMnet; P0AD49; -.
DR SWISS-2DPAGE; P0AD49; -.
DR jPOST; P0AD49; -.
DR PaxDb; P0AD49; -.
DR PRIDE; P0AD49; -.
DR EnsemblBacteria; AAC75646; AAC75646; b2597.
DR EnsemblBacteria; BAA16481; BAA16481; BAA16481.
DR GeneID; 67414085; -.
DR GeneID; 947129; -.
DR KEGG; ecj:JW2578; -.
DR KEGG; eco:b2597; -.
DR PATRIC; fig|1411691.4.peg.4141; -.
DR EchoBASE; EB1140; -.
DR eggNOG; COG1544; Bacteria.
DR HOGENOM; CLU_071472_3_0_6; -.
DR InParanoid; P0AD49; -.
DR OMA; DMYVAIN; -.
DR PhylomeDB; P0AD49; -.
DR BioCyc; EcoCyc:EG11151-MON; -.
DR EvolutionaryTrace; P0AD49; -.
DR PRO; PR:P0AD49; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoliWiki.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:EcoCyc.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045900; P:negative regulation of translational elongation; IDA:EcoCyc.
DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
DR GO; GO:0044238; P:primary metabolic process; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IEP:EcoCyc.
DR CDD; cd00552; RaiA; 1.
DR Gene3D; 3.30.160.100; -; 1.
DR InterPro; IPR036567; RHF-like.
DR InterPro; IPR003489; RHF/RaiA.
DR Pfam; PF02482; Ribosomal_S30AE; 1.
DR SUPFAM; SSF69754; SSF69754; 1.
DR TIGRFAMs; TIGR00741; yfiA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Reference proteome;
KW RNA-binding; rRNA-binding; Stress response; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10535924,
FT ECO:0000269|PubMed:11168583, ECO:0000269|PubMed:9298646,
FT ECO:0000269|Ref.10"
FT CHAIN 2..113
FT /note="Ribosome-associated inhibitor A"
FT /id="PRO_0000169261"
FT REGION 23..26
FT /note="Interaction with 16S rRNA"
FT /evidence="ECO:0000305|PubMed:25775268"
FT REGION 83..91
FT /note="Interaction with 16S rRNA"
FT /evidence="ECO:0000305|PubMed:25775268"
FT REGION 91..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1L4S"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1L4S"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1L4S"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1L4S"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1L4S"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1L4S"
FT HELIX 70..89
FT /evidence="ECO:0007829|PDB:1L4S"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1N3G"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1L4S"
SQ SEQUENCE 113 AA; 12785 MW; 562901F819836A87 CRC64;
MTMNITSKQM EITPAIRQHV ADRLAKLEKW QTHLINPHII LSKEPQGFVA DATINTPNGV
LVASGKHEDM YTAINELINK LERQLNKLQH KGEARRAATS VKDANFVEEV EEE
