ATDA_ECOLI
ID ATDA_ECOLI Reviewed; 186 AA.
AC P0A951; P37354;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Spermidine N(1)-acetyltransferase {ECO:0000303|PubMed:7052085};
DE Short=SAT {ECO:0000303|PubMed:8077207};
DE EC=2.3.1.57 {ECO:0000269|PubMed:33826189, ECO:0000269|PubMed:7052085, ECO:0000269|PubMed:8077207};
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase {ECO:0000303|PubMed:7052085};
DE Short=SSAT {ECO:0000303|PubMed:7052085};
GN Name=speG; OrderedLocusNames=b1584, JW1576;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8077207; DOI=10.1016/s0021-9258(17)31685-x;
RA Fukuchi J., Kashiwagi K., Takio K., Igarashi K.;
RT "Properties and structure of spermidine acetyltransferase in Escherichia
RT coli.";
RL J. Biol. Chem. 269:22581-22585(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=7052085; DOI=10.1016/0006-291x(82)91233-5;
RA Matsui I., Kamei M., Otani S., Morisawa S., Pegg A.E.;
RT "Occurrence and induction of spermidine-N1-acetyltransferase in Escherichia
RT coli.";
RL Biochem. Biophys. Res. Commun. 106:1155-1160(1982).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=6297970; DOI=10.1016/0014-5793(82)81336-7;
RA Matsui I., Otani S., Kamei M., Morisawa S.;
RT "Inactivation of spermidine N1-acetyltransferase with alkaline
RT phosphatase.";
RL FEBS Lett. 150:211-213(1982).
RN [7]
RP ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=2061318; DOI=10.1016/s0021-9258(18)98917-9;
RA Carper S.W., Willis D.G., Manning K.A., Gerner E.W.;
RT "Spermidine acetylation in response to a variety of stresses in Escherichia
RT coli.";
RL J. Biol. Chem. 266:12439-12441(1991).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=7642535; DOI=10.1074/jbc.270.32.18831;
RA Fukuchi J., Kashiwagi K., Yamagishi M., Ishihama A., Igarashi K.;
RT "Decrease in cell viability due to the accumulation of spermidine in
RT spermidine acetyltransferase-deficient mutant of Escherichia coli.";
RL J. Biol. Chem. 270:18831-18835(1995).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=10986239; DOI=10.1128/jb.182.19.5373-5380.2000;
RA Limsuwun K., Jones P.G.;
RT "Spermidine acetyltransferase is required to prevent spermidine toxicity at
RT low temperatures in Escherichia coli.";
RL J. Bacteriol. 182:5373-5380(2000).
RN [10]
RP FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH RCSB, AND
RP MUTAGENESIS OF TYR-135.
RX PubMed=30562360; DOI=10.1371/journal.pone.0207563;
RA Hu L.I., Filippova E.V., Dang J., Pshenychnyi S., Ruan J., Kiryukhina O.,
RA Anderson W.F., Kuhn M.L., Wolfe A.J.;
RT "The spermidine acetyltransferase SpeG regulates transcription of the small
RT RNA rprA.";
RL PLoS ONE 13:e0207563-e0207563(2018).
RN [11]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND
RP MUTAGENESIS OF TYR-135.
RX PubMed=33826189; DOI=10.1002/pro.4078;
RA Le V.T.B., Dang J., Lim E.Q., Kuhn M.L.;
RT "Criticality of a conserved tyrosine residue in the SpeG protein from
RT Escherichia coli.";
RL Protein Sci. 30:1264-1269(2021).
RN [12]
RP CRYSTALLIZATION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=23908034; DOI=10.1107/s1744309113017132;
RA Niiyama M., Sugiyama S., Hirose M., Ishikawa S., Tomitori H., Higashi K.,
RA Yamashita T., Adachi H., Takano K., Murakami S., Murata M., Inoue T.,
RA Mori Y., Kashiwagi K., Matsumura H., Igarashi K.;
RT "Expression, purification, crystallization and preliminary crystallographic
RT analysis of spermidine acetyltransferase from Escherichia coli.";
RL Acta Crystallogr. F 69:884-887(2013).
RN [13] {ECO:0007744|PDB:4R9M, ECO:0007744|PDB:6CY6}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=31205017; DOI=10.1107/s2059798319006545;
RA Filippova E.V., Weigand S., Kiryukhina O., Wolfe A.J., Anderson W.F.;
RT "Analysis of crystalline and solution states of ligand-free spermidine N-
RT acetyltransferase (SpeG) from Escherichia coli.";
RL Acta Crystallogr. D 75:545-553(2019).
CC -!- FUNCTION: Involved in the protection against polyamine toxicity by
CC regulating their concentration (PubMed:7642535, PubMed:10986239).
CC Catalyzes the transfer of an acetyl group from acetyl coenzyme A
CC (AcCoA) to the primary amino groups of spermidine to yield N(1)- and
CC N(8)-acetylspermidine (PubMed:8077207, PubMed:7052085, PubMed:6297970).
CC It can also use spermine, but not putrescine (PubMed:7052085).
CC {ECO:0000269|PubMed:10986239, ECO:0000269|PubMed:6297970,
CC ECO:0000269|PubMed:7052085, ECO:0000269|PubMed:7642535,
CC ECO:0000269|PubMed:8077207}.
CC -!- FUNCTION: In addition, may act as a modulator of transcription through
CC its ability to interact with the two-component response regulator RcsB.
CC Inhibits transcription of the small RNA regulator rprA in an
CC acetylation-independent manner. Interaction with the DNA-binding domain
CC of RcsB might be responsible for SpeG-dependent inhibition of RcsB-
CC dependent rprA transcription (PubMed:30562360). SpeG does not acetylate
CC RcsB in vitro (PubMed:30562360). {ECO:0000269|PubMed:30562360}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-
CC acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116,
CC Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977,
CC ChEBI:CHEBI:70988; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:33826189, ECO:0000269|PubMed:7052085,
CC ECO:0000269|PubMed:8077207};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(1)-acetylspermidine;
CC Xref=Rhea:RHEA:28150, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58324; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:7052085, ECO:0000269|PubMed:8077207,
CC ECO:0000305|PubMed:33826189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(8)-acetylspermidine;
CC Xref=Rhea:RHEA:28270, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:7052085, ECO:0000269|PubMed:8077207,
CC ECO:0000305|PubMed:33826189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermine = CoA + H(+) + N(1)-acetylspermine;
CC Xref=Rhea:RHEA:33099, ChEBI:CHEBI:15378, ChEBI:CHEBI:45725,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58101; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:33826189, ECO:0000269|PubMed:7052085,
CC ECO:0000269|PubMed:8077207};
CC -!- ACTIVITY REGULATION: Heat shock, alkaline shift, ethanol treatment and
CC poor nutrient availability produce increased concentrations of
CC monoacetylated spermidine (PubMed:2061318). Inhibited by alkaline
CC phosphatase, N(1),N(8)-bis(ethyl)spermidine (BESPD) and N(1),N(12)-
CC bis(ethyl)spermidine (BESPM) (PubMed:8077207, PubMed:6297970).
CC {ECO:0000269|PubMed:2061318, ECO:0000269|PubMed:6297970,
CC ECO:0000269|PubMed:8077207}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for AcCoA (in the presence of 3 mM spermidine at pH 7.5 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:8077207};
CC KM=220 uM for spermine (in the presence of 10 uM AcCoA at pH 7.5 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:8077207};
CC KM=183 uM for spermine {ECO:0000269|PubMed:33826189};
CC KM=1290 uM for spermidine (in the presence of 10 uM AcCoA at pH 7.5
CC and 37 degrees Celsius) {ECO:0000269|PubMed:8077207};
CC KM=328 uM for spermidine {ECO:0000269|PubMed:33826189};
CC Temperature dependence:
CC The level of spermidine acetyltransferase activity increases at low
CC temperature to prevent spermidine toxicity.
CC {ECO:0000269|PubMed:10986239};
CC -!- PATHWAY: Amine and polyamine degradation; spermidine degradation.
CC {ECO:0000305|PubMed:10986239, ECO:0000305|PubMed:7642535}.
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305|PubMed:10986239, ECO:0000305|PubMed:7642535}.
CC -!- SUBUNIT: Homododecamer (PubMed:31205017). Ligand-free SpeG forms closed
CC symmetric dodecamers in the crystal and open asymmetric dodecamers in
CC solution (PubMed:31205017). In the absence of ligand, also exists in
CC solution as hexamers and tetramers, but not dimers (PubMed:23908034,
CC PubMed:8077207, PubMed:31205017). Can interact with the DNA-binding
CC carboxyl domain of RcsB in the presence or absence of spermidine
CC (PubMed:30562360). {ECO:0000269|PubMed:23908034,
CC ECO:0000269|PubMed:30562360, ECO:0000269|PubMed:31205017,
CC ECO:0000269|PubMed:8077207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed throughout log and plateau phases
CC of growth. {ECO:0000269|PubMed:2061318}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate spermidine at
CC late stationary phase and show a reduced cell viability due to a
CC decrease in protein biosynthesis (PubMed:7642535). At 37 degrees
CC Celsius, growth of mutant is normal in the presence of 0.5 or 1 mM
CC spermidine. However, following a shift to 7 degrees Celsius, the
CC addition of 0.5 or 1 mM spermidine results in inhibition of cellular
CC growth or cell lysis, respectively. Furthermore, at 7 degrees Celsius,
CC spermidine accumulation resulted in a decrease in total protein
CC synthesis accompanied by an increase in the synthesis of the major cold
CC shock proteins CspA, CspB, and CspG (PubMed:10986239).
CC {ECO:0000269|PubMed:10986239, ECO:0000269|PubMed:7642535}.
CC -!- MISCELLANEOUS: Acetylation neutralizes the charge of the polyamine,
CC which is then typically excreted from the cell.
CC {ECO:0000269|PubMed:8077207}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; D25276; BAA04966.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74656.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15286.1; -; Genomic_DNA.
DR PIR; A55345; A55345.
DR RefSeq; NP_416101.1; NC_000913.3.
DR RefSeq; WP_001138581.1; NZ_STEB01000003.1.
DR PDB; 4R9M; X-ray; 2.90 A; A/B/C=1-186.
DR PDB; 6CY6; X-ray; 1.75 A; A=1-186.
DR PDBsum; 4R9M; -.
DR PDBsum; 6CY6; -.
DR AlphaFoldDB; P0A951; -.
DR SMR; P0A951; -.
DR BioGRID; 4260234; 7.
DR BioGRID; 850477; 1.
DR ComplexPortal; CPX-2133; Spermidine N(1)-acetyltransferase complex.
DR IntAct; P0A951; 11.
DR STRING; 511145.b1584; -.
DR jPOST; P0A951; -.
DR PaxDb; P0A951; -.
DR PRIDE; P0A951; -.
DR EnsemblBacteria; AAC74656; AAC74656; b1584.
DR EnsemblBacteria; BAA15286; BAA15286; BAA15286.
DR GeneID; 946117; -.
DR KEGG; ecj:JW1576; -.
DR KEGG; eco:b1584; -.
DR PATRIC; fig|1411691.4.peg.678; -.
DR EchoBASE; EB2341; -.
DR eggNOG; COG1670; Bacteria.
DR InParanoid; P0A951; -.
DR OMA; IYEAKQL; -.
DR PhylomeDB; P0A951; -.
DR BioCyc; EcoCyc:SPERMACTRAN-MON; -.
DR BioCyc; MetaCyc:SPERMACTRAN-MON; -.
DR BRENDA; 2.3.1.57; 2026.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR PRO; PR:P0A951; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990235; C:diamine N-acetyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0015936; P:coenzyme A metabolic process; IDA:ComplexPortal.
DR GO; GO:0006598; P:polyamine catabolic process; IMP:UniProtKB.
DR GO; GO:0046203; P:spermidine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8077207"
FT CHAIN 2..186
FT /note="Spermidine N(1)-acetyltransferase"
FT /id="PRO_0000074588"
FT DOMAIN 7..167
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:33826189"
FT BINDING 30
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31205017,
FT ECO:0007744|PDB:4R9M"
FT BINDING 35
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 35
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 43
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 43
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 51..54
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31205017,
FT ECO:0007744|PDB:4R9M"
FT BINDING 85..87
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 88..90
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 95..101
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 128..137
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT SITE 85
FT /note="Could be important for selectivity toward long
FT polyamines"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT MUTAGEN 135
FT /note="Y->A: 300-fold decrease in activity with spermine as
FT substrate. Retains the ability to inhibit PrprA activity."
FT /evidence="ECO:0000269|PubMed:30562360,
FT ECO:0000269|PubMed:33826189"
FT MUTAGEN 135
FT /note="Y->C,F: 100-fold decrease in activity with spermine
FT as substrate."
FT /evidence="ECO:0000269|PubMed:33826189"
FT MUTAGEN 135
FT /note="Y->S: Loss of activity with spermine as substrate."
FT /evidence="ECO:0000269|PubMed:33826189"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:6CY6"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:6CY6"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:6CY6"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:6CY6"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:6CY6"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6CY6"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:6CY6"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6CY6"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6CY6"
FT STRAND 67..78
FT /evidence="ECO:0007829|PDB:6CY6"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:6CY6"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6CY6"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6CY6"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:6CY6"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:6CY6"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:6CY6"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:6CY6"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:6CY6"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:6CY6"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:6CY6"
SQ SEQUENCE 186 AA; 21887 MW; 27297083B93B3752 CRC64;
MPSAHSVKLR PLEREDLRYV HQLDNNASVM RYWFEEPYEA FVELSDLYDK HIHDQSERRF
VVECDGEKAG LVELVEINHV HRRAEFQIII SPEYQGKGLA TRAAKLAMDY GFTVLNLYKL
YLIVDKENEK AIHIYRKLGF SVEGELMHEF FINGQYRNAI RMCIFQHQYL AEHKTPGQTL
LKPTAQ
