ENO_ECOLI
ID ENO_ECOLI Reviewed; 432 AA.
AC P0A6P9; P08324; Q2MA53;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318};
GN OrderedLocusNames=b2779, JW2750;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / JM109 / ATCC 53323;
RA Klein M., Freudl R.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
RX PubMed=3514618; DOI=10.1016/s0021-9258(19)57252-0;
RA Weng M., Makaroff C.A., Zalkin H.;
RT "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase.";
RL J. Biol. Chem. 261:5568-5574(1986).
RN [5]
RP PROTEIN SEQUENCE OF 2-16, AND SUBUNIT.
RX PubMed=8610017; DOI=10.1038/381169a0;
RA Py B., Higgins C.F., Krisch H.M., Carpousis A.J.;
RT "A DEAD-box RNA helicase in the Escherichia coli RNA degradosome.";
RL Nature 381:169-172(1996).
RN [6]
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 [7]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=B;
RX PubMed=4942326; DOI=10.1016/s0021-9258(19)45916-4;
RA Spring T.G., Wold F.;
RT "The purification and characterization of Escherichia coli enolase.";
RL J. Biol. Chem. 246:6797-6802(1971).
RN [9]
RP PRELIMINARY CHARACTERIZATION, AND PHOSPHORYLATION.
RC STRAIN=K12 / JA200;
RX PubMed=2513001; DOI=10.1016/0300-9084(89)90116-8;
RA Dannelly H.K., Duclos B., Cozzone A.J., Reeves H.C.;
RT "Phosphorylation of Escherichia coli enolase.";
RL Biochimie 71:1095-1100(1989).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP INTERACTION WITH RNASE E.
RX PubMed=9732274; DOI=10.1101/gad.12.17.2770;
RA Vanzo N.F., Li Y.S., Py B., Blum E., Higgins C.F., Raynal L.C.,
RA Krisch H.M., Carpousis A.J.;
RT "Ribonuclease E organizes the protein interactions in the Escherichia coli
RT RNA degradosome.";
RL Genes Dev. 12:2770-2781(1998).
RN [12]
RP SUBSTRATE BINDING AT LYS-342, ACTIVE SITE, ACTIVITY REGULATION, SECRETION
RP OF SUBSTRATE-BOUND ENOLASE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-168; GLU-209 AND LYS-342.
RX PubMed=15003462; DOI=10.1016/j.jmb.2003.12.082;
RA Boeel G., Pichereau V., Mijakovic I., Maze A., Poncet S., Gillet S.,
RA Giard J.-C., Hartke A., Auffray Y., Deutscher J.;
RT "Is 2-phosphoglycerate-dependent automodification of bacterial enolases
RT implicated in their export?";
RL J. Mol. Biol. 337:485-496(2004).
RN [13]
RP FUNCTION IN MRNA TURNOVER.
RX PubMed=14981237; DOI=10.1073/pnas.0308747101;
RA Bernstein J.A., Lin P.-H., Cohen S.N., Lin-Chao S.;
RT "Global analysis of Escherichia coli RNA degradosome function using DNA
RT microarrays.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2758-2763(2004).
RN [14]
RP FUNCTION IN THE DECAY OF GLUCOSE TRANSPORTER MRNA.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15522087; DOI=10.1111/j.1365-2958.2004.04329.x;
RA Morita T., Kawamoto H., Mizota T., Inada T., Aiba H.;
RT "Enolase in the RNA degradosome plays a crucial role in the rapid decay of
RT glucose transporter mRNA in the response to phosphosugar stress in
RT Escherichia coli.";
RL Mol. Microbiol. 54:1063-1075(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RC STRAIN=PB103;
RX PubMed=17242352; DOI=10.1073/pnas.0610491104;
RA Taghbalout A., Rothfield L.;
RT "RNaseE and the other constituents of the RNA degradosome are components of
RT the bacterial cytoskeleton.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1667-1672(2007).
RN [16]
RP INTERACTION WITH RNASE E, AND SUBCELLULAR LOCATION.
RX PubMed=18337249; DOI=10.1074/jbc.m709118200;
RA Taghbalout A., Rothfield L.;
RT "RNaseE and RNA helicase B play central roles in the cytoskeletal
RT organization of the RNA degradosome.";
RL J. Biol. Chem. 283:13850-13855(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257, 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 [18]
RP HYDROXYBUTYRYLATION AT LYS-342.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=31328167; DOI=10.1126/sciadv.aaw6703;
RA Dong H., Zhai G., Chen C., Bai X., Tian S., Hu D., Fan E., Zhang K.;
RT "Protein lysine de-2-hydroxyisobutyrylation by CobB in prokaryotes.";
RL Sci. Adv. 5:eaaw6703-eaaw6703(2019).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP COFACTOR, AND SUBUNIT.
RX PubMed=11676541; DOI=10.1006/jmbi.2001.5065;
RA Kuhnel K., Luisi B.F.;
RT "Crystal structure of the Escherichia coli RNA degradosome component
RT enolase.";
RL J. Mol. Biol. 313:583-592(2001).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH THE MINIMAL BINDING
RP SEGMENT OF RNASE E AND MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=16516921; DOI=10.1016/j.jmb.2006.02.012;
RA Chandran V., Luisi B.F.;
RT "Recognition of enolase in the Escherichia coli RNA degradosome.";
RL J. Mol. Biol. 358:8-15(2006).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE MINIMAL BINDING
RP SEGMENT OF RNASE E, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20823555; DOI=10.1107/s0907444910030015;
RA Nurmohamed S., McKay A.R., Robinson C.V., Luisi B.F.;
RT "Molecular recognition between Escherichia coli enolase and ribonuclease
RT E.";
RL Acta Crystallogr. D 66:1036-1040(2010).
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis. It is also a component of the RNA
CC degradosome, a multi-enzyme complex involved in RNA processing and
CC messenger RNA degradation. Its interaction with RNase E is important
CC for the turnover of mRNA, in particular on transcripts encoding enzymes
CC of energy-generating metabolic routes. Its presence in the degradosome
CC is required for the response to excess phosphosugar. May play a
CC regulatory role in the degradation of specific RNAs, such as ptsG mRNA,
CC therefore linking cellular metabolic status with post-translational
CC gene regulation. {ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:14981237, ECO:0000269|PubMed:15522087,
CC ECO:0000269|PubMed:4942326}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00318, ECO:0000269|PubMed:4942326};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:11676541, ECO:0000269|PubMed:4942326};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541,
CC ECO:0000269|PubMed:4942326};
CC -!- ACTIVITY REGULATION: The covalent binding to the substrate at Lys-342
CC causes inactivation of the enzyme, and possibly serves as a signal for
CC the export of the protein. Inhibited by fluoride ion.
CC {ECO:0000269|PubMed:15003462, ECO:0000269|PubMed:4942326}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.1. {ECO:0000269|PubMed:4942326};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation. Interacts with
CC the C-terminal region of the endoribonuclease RNase E. Homodimer.
CC {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541,
CC ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:18337249,
CC ECO:0000269|PubMed:20823555, ECO:0000269|PubMed:4942326,
CC ECO:0000269|PubMed:8610017, ECO:0000269|PubMed:9732274}.
CC -!- INTERACTION:
CC P0A6P9; P0A6P9: eno; NbExp=2; IntAct=EBI-368855, EBI-368855;
CC P0A6P9; P21513: rne; NbExp=17; IntAct=EBI-368855, EBI-549958;
CC P0A6P9; P0AG07: rpe; NbExp=3; IntAct=EBI-368855, EBI-546020;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Secreted. Cell surface.
CC Note=Fractions of enolase are present in both the cytoplasm and on the
CC cell surface. As part of the bacterial cytoskeleton in the cytoplasm,
CC is organized as extended coiled structures that wind around the cell,
CC from one cell pole to the other. When covalently bound to the substrate
CC at Lys-342, the inactive enolase is secreted, and remains attached to
CC the cell surface.
CC -!- PTM: Phosphorylated on serine residue(s). {ECO:0000269|PubMed:2513001}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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DR EMBL; X82400; CAA57795.1; -; Genomic_DNA.
DR EMBL; U29580; AAA69289.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75821.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76853.1; -; Genomic_DNA.
DR EMBL; M12843; AAA24486.1; -; mRNA.
DR PIR; G65059; NOEC.
DR RefSeq; NP_417259.1; NC_000913.3.
DR RefSeq; WP_000036723.1; NZ_STEB01000030.1.
DR PDB; 1E9I; X-ray; 2.48 A; A/B/C/D=2-432.
DR PDB; 2FYM; X-ray; 1.60 A; A/C/D/F=2-432.
DR PDB; 3H8A; X-ray; 1.90 A; A/B/C/D=1-432.
DR PDB; 5OHG; X-ray; 2.00 A; A/B/H/I=1-432.
DR PDB; 6BFY; X-ray; 1.81 A; A/B/C/D/E/F=1-432.
DR PDB; 6BFZ; X-ray; 2.21 A; A/B/C/D/E/F=1-432.
DR PDB; 6D3Q; X-ray; 2.24 A; A/B/C/D/E/F=1-432.
DR PDB; 6NPF; X-ray; 2.57 A; A/B/C/D/E/F=1-432.
DR PDBsum; 1E9I; -.
DR PDBsum; 2FYM; -.
DR PDBsum; 3H8A; -.
DR PDBsum; 5OHG; -.
DR PDBsum; 6BFY; -.
DR PDBsum; 6BFZ; -.
DR PDBsum; 6D3Q; -.
DR PDBsum; 6NPF; -.
DR AlphaFoldDB; P0A6P9; -.
DR SMR; P0A6P9; -.
DR BioGRID; 4262297; 354.
DR ComplexPortal; CPX-403; RNA degradosome.
DR DIP; DIP-31847N; -.
DR IntAct; P0A6P9; 38.
DR STRING; 511145.b2779; -.
DR CarbonylDB; P0A6P9; -.
DR iPTMnet; P0A6P9; -.
DR SWISS-2DPAGE; P0A6P9; -.
DR jPOST; P0A6P9; -.
DR PaxDb; P0A6P9; -.
DR PRIDE; P0A6P9; -.
DR EnsemblBacteria; AAC75821; AAC75821; b2779.
DR EnsemblBacteria; BAE76853; BAE76853; BAE76853.
DR GeneID; 67413943; -.
DR GeneID; 945032; -.
DR KEGG; ecj:JW2750; -.
DR KEGG; eco:b2779; -.
DR PATRIC; fig|1411691.4.peg.3956; -.
DR EchoBASE; EB0254; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_6; -.
DR InParanoid; P0A6P9; -.
DR OMA; EFMIIPV; -.
DR PhylomeDB; P0A6P9; -.
DR BioCyc; EcoCyc:ENOLASE-MON; -.
DR BioCyc; MetaCyc:ENOLASE-MON; -.
DR BRENDA; 4.2.1.11; 2026.
DR SABIO-RK; P0A6P9; -.
DR UniPathway; UPA00109; UER00187.
DR EvolutionaryTrace; P0A6P9; -.
DR PRO; PR:P0A6P9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990061; C:bacterial degradosome; IPI:ComplexPortal.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CAFA.
DR GO; GO:0006096; P:glycolytic process; IMP:EcoliWiki.
DR GO; GO:0006401; P:RNA catabolic process; IC:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; IC:ComplexPortal.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Glycolysis; Hydroxylation; Lyase; Magnesium;
KW Metal-binding; Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8610017,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841"
FT CHAIN 2..432
FT /note="Enolase"
FT /id="PRO_0000133882"
FT REGION 5..34
FT /note="Interaction with RNase E"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318,
FT ECO:0000269|PubMed:15003462"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318,
FT ECO:0000269|PubMed:15003462"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11676541,
FT ECO:0000269|PubMed:16516921"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11676541,
FT ECO:0000269|PubMed:16516921"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11676541,
FT ECO:0000269|PubMed:16516921"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 342
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000269|PubMed:15003462"
FT BINDING 369..372
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT SITE 120
FT /note="Interaction with RNase E"
FT /evidence="ECO:0000269|PubMed:16516921,
FT ECO:0000269|PubMed:20823555"
FT SITE 376
FT /note="Interaction with RNase E"
FT /evidence="ECO:0000269|PubMed:16516921,
FT ECO:0000269|PubMed:20823555"
FT SITE 408
FT /note="Interaction with RNase E"
FT /evidence="ECO:0000269|PubMed:16516921,
FT ECO:0000269|PubMed:20823555"
FT MOD_RES 257
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 342
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:31328167"
FT MUTAGEN 168
FT /note="E->Q: 5% activity; not secreted."
FT /evidence="ECO:0000269|PubMed:15003462"
FT MUTAGEN 209
FT /note="E->Q: 1% activity; not secreted."
FT /evidence="ECO:0000269|PubMed:15003462"
FT MUTAGEN 342
FT /note="K->A,Q,R: 1% activity; not secreted."
FT /evidence="ECO:0000269|PubMed:15003462"
FT MUTAGEN 342
FT /note="K->E: 94% activity; not secreted."
FT /evidence="ECO:0000269|PubMed:15003462"
FT CONFLICT 102
FT /note="N -> K (in Ref. 1; CAA57795/AAA24486)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="A -> D (in Ref. 1; CAA57795)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="I -> Y (in Ref. 1; CAA57795)"
FT /evidence="ECO:0000305"
FT CONFLICT 421..432
FT /note="PYNGRKEIKGQA -> RTTVVKRSKARHKTDFI (in Ref. 1;
FT CAA57795)"
FT /evidence="ECO:0000305"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2FYM"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6NPF"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3H8A"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 179..199
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6BFY"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:2FYM"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6BFY"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:2FYM"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:2FYM"
FT TURN 318..322
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 349..361
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:2FYM"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 400..416
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:2FYM"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:2FYM"
SQ SEQUENCE 432 AA; 45655 MW; 0569036E87471B91 CRC64;
MSKIVKIIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE LRDGDKSRFL
GKGVTKAVAA VNGPIAQALI GKDAKDQAGI DKIMIDLDGT ENKSKFGANA ILAVSLANAK
AAAAAKGMPL YEHIAELNGT PGKYSMPVPM MNIINGGEHA DNNVDIQEFM IQPVGAKTVK
EAIRMGSEVF HHLAKVLKAK GMNTAVGDEG GYAPNLGSNA EALAVIAEAV KAAGYELGKD
ITLAMDCAAS EFYKDGKYVL AGEGNKAFTS EEFTHFLEEL TKQYPIVSIE DGLDESDWDG
FAYQTKVLGD KIQLVGDDLF VTNTKILKEG IEKGIANSIL IKFNQIGSLT ETLAAIKMAK
DAGYTAVISH RSGETEDATI ADLAVGTAAG QIKTGSMSRS DRVAKYNQLI RIEEALGEKA
PYNGRKEIKG QA
