TIG_ECOLI
ID TIG_ECOLI Reviewed; 432 AA.
AC P0A850; P15299; P22257; P77603; Q2MBZ0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Trigger factor;
DE Short=TF;
DE EC=5.2.1.8 {ECO:0000269|PubMed:8633085};
DE AltName: Full=PPIase;
GN Name=tig; OrderedLocusNames=b0436, JW0426;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=2211496; DOI=10.1128/jb.172.10.5555-5562.1990;
RA Guthrie B., Wickner W.;
RT "Trigger factor depletion or overproduction causes defective cell division
RT but does not block protein export.";
RL J. Bacteriol. 172:5555-5562(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-145.
RX PubMed=2684651; DOI=10.1002/j.1460-2075.1989.tb08573.x;
RA Aldea M., Garrido T., Hernandez-Chico C., Vicente M., Kushner S.R.;
RT "Induction of a growth-phase-dependent promoter triggers transcription of
RT bolA, an Escherichia coli morphogene.";
RL EMBO J. 8:3923-3931(1989).
RN [6]
RP PROTEIN SEQUENCE OF 1-13.
RX PubMed=2843289; DOI=10.1016/0092-8674(88)90115-8;
RA Crooke E., Guthrie B., Lecker S., Lill R., Wickner W.;
RT "ProOmpA is stabilized for membrane translocation by either purified E.
RT coli trigger factor or canine signal recognition particle.";
RL Cell 54:1003-1011(1988).
RN [7]
RP PROTEIN SEQUENCE OF 1-21 AND 38-58.
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 [8]
RP PROTEIN SEQUENCE OF 1-7, FUNCTION AS A PPIASE, SUBCELLULAR LOCATION, AND
RP RIBOSOME-BINDING.
RX PubMed=8633085; DOI=10.1073/pnas.93.9.4437;
RA Hesterkamp T., Hauser S., Lutcke H., Bukau B.;
RT "Escherichia coli trigger factor is a prolyl isomerase that associates with
RT nascent polypeptide chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4437-4441(1996).
RN [9]
RP PROTEIN SEQUENCE OF 145-174.
RX PubMed=8612805; DOI=10.1016/0014-5793(96)00282-7;
RA Stoller G., Tradler T., Ruecknagel K.P., Rahfeld J.-U., Fischer G.;
RT "An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents
RT the domain carrying the peptidyl-prolyl cis/trans isomerase activity.";
RL FEBS Lett. 384:117-122(1996).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 390-432.
RX PubMed=2197275; DOI=10.1016/s0021-9258(19)38378-4;
RA Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B.,
RA Gottesman S.;
RT "Sequence and structure of Clp P, the proteolytic component of the ATP-
RT dependent Clp protease of Escherichia coli.";
RL J. Biol. Chem. 265:12536-12545(1990).
RN [11]
RP FUNCTION.
RX PubMed=8521806; DOI=10.1002/j.1460-2075.1995.tb00236.x;
RA Valent Q.A., Kendall D.A., High S., Kusters R., Oudega B., Luirink J.;
RT "Early events in preprotein recognition in E. coli: interaction of SRP and
RT trigger factor with nascent polypeptides.";
RL EMBO J. 14:5494-5505(1995).
RN [12]
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 [13]
RP SUBUNIT.
RX PubMed=12452438; DOI=10.1515/bc.2002.182;
RA Patzelt H., Kramer G., Rauch T., Schonfeld H.J., Bukau B., Deuerling E.;
RT "Three-state equilibrium of Escherichia coli trigger factor.";
RL Biol. Chem. 383:1611-1619(2002).
RN [14]
RP BINDING TO RIBOSOMAL PROTEINS L23 AND L29, AND MUTAGENESIS OF
RP 44-PHE--LYS-46.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12226666; DOI=10.1038/nature01047;
RA Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H.,
RA Schulze-Specking A., Ban N., Deuerling E., Bukau B.;
RT "L23 protein functions as a chaperone docking site on the ribosome.";
RL Nature 419:171-174(2002).
RN [15]
RP CROSS-LINKS TO NASCENT PROTEIN CHAINS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12756233; DOI=10.1083/jcb.200302130;
RA Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M.,
RA Brunner J., Oudega B., Harms N., Luirink J.;
RT "Interplay of signal recognition particle and trigger factor at L23 near
RT the nascent chain exit site on the Escherichia coli ribosome.";
RL J. Cell Biol. 161:679-684(2003).
RN [16]
RP DOMAIN, DISPENSABILITY OF PPIASE FOR CHAPERONE FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=14726952; DOI=10.1038/sj.embor.7400067;
RA Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S., Hartl F.U.,
RA Georgopoulos C.;
RT "In vivo analysis of the overlapping functions of DnaK and trigger
RT factor.";
RL EMBO Rep. 5:195-200(2004).
RN [17]
RP MAY BIND TO THE RIBOSOME AS A DIMER.
RC STRAIN=MRE-600;
RX PubMed=12581648; DOI=10.1016/s0022-2836(02)01436-5;
RA Blaha G., Wilson D.N., Stoller G., Fischer G., Willumeit R., Nierhaus K.H.;
RT "Localization of the trigger factor binding site on the ribosomal 50S
RT subunit.";
RL J. Mol. Biol. 326:887-897(2003).
RN [18]
RP SIMULTANEOUS BINDING OF TRIGGER FACTOR AND SRP TO THE RIBOSOME.
RC STRAIN=MRE-600;
RX PubMed=15148364; DOI=10.1073/pnas.0402231101;
RA Buskiewicz I., Deuerling E., Gu S.-Q., Joeckel J., Rodnina M.V., Bukau B.,
RA Wintermeyer W.;
RT "Trigger factor binds to ribosome-signal-recognition particle (SRP)
RT complexes and is excluded by binding of the SRP receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7902-7906(2004).
RN [19]
RP ADP-RIBOSYLATION AT ARG-45 (MICROBIAL INFECTION).
RX PubMed=16112649; DOI=10.1016/j.bbrc.2005.08.023;
RA Depping R., Lohaus C., Meyer H.E., Ruger W.;
RT "The mono-ADP-ribosyltransferases Alt and ModB of bacteriophage T4: target
RT proteins identified.";
RL Biochem. Biophys. Res. Commun. 335:1217-1223(2005).
RN [20]
RP STRUCTURE BY NMR IN COMPLEX WITH PHOA SUBSTRATE, FUNCTION, SUBUNIT, DOMAIN,
RP AND MUTAGENESIS OF MET-140 AND 374-MET--PHE-387.
RX PubMed=24812405; DOI=10.1126/science.1250494;
RA Saio T., Guan X., Rossi P., Economou A., Kalodimos C.G.;
RT "Structural basis for protein antiaggregation activity of the trigger
RT factor chaperone.";
RL Science 344:1250494-1250494(2014).
CC -!- FUNCTION: Involved in protein export. Acts as a chaperone by
CC maintaining the newly synthesized secretory and non-secretory proteins
CC in an open conformation. Binds to 3 regions of unfolded substrate PhoA,
CC preferring aromatic and hydrophobic residues, keeping it stretched out
CC and unable to form aggregates (PubMed:24812405). Binds to nascent
CC polypeptide chains via ribosomal protein L23 (PubMed:12226666).
CC Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this
CC activity is dispensible in vivo for chaperone activity.
CC {ECO:0000269|PubMed:12226666, ECO:0000269|PubMed:24812405,
CC ECO:0000269|PubMed:8521806, ECO:0000269|PubMed:8633085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:8633085};
CC -!- SUBUNIT: Homodimer and monomer. In vivo most of the ribosomes are in
CC complex with monomeric TF (PubMed:12452438); binding as a dimer has
CC also been suggested (PubMed:12581648). Uncomplexed TF is in a monomer-
CC dimer equilibrium with approximately two thirds of TF existing in a
CC dimeric state; binding to substrate PhoA induces monomerization, 3 TF
CC monomers bind somewhat independently to a single substrate molecule
CC (PubMed:12452438, PubMed:24812405). TF and SRP can simultaneously bind
CC to ribosomes; TF binding is abolished when SRP is bound to FtsY in the
CC presence of a non-hydrolyzable GTP analog (PubMed:15148364). Contacts
CC ribosomal proteins L23 and L29 (PubMed:12226666).
CC {ECO:0000269|PubMed:12226666, ECO:0000269|PubMed:12452438,
CC ECO:0000269|PubMed:12581648, ECO:0000269|PubMed:15148364,
CC ECO:0000269|PubMed:24812405}.
CC -!- INTERACTION:
CC P0A850; P0A910: ompA; NbExp=3; IntAct=EBI-544862, EBI-371347;
CC P0A850; P0A7M2: rpmB; NbExp=4; IntAct=EBI-544862, EBI-543024;
CC P0A850; P02359: rpsG; NbExp=4; IntAct=EBI-544862, EBI-543074;
CC P0A850; P0A850: tig; NbExp=2; IntAct=EBI-544862, EBI-544862;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8633085}.
CC Note=About half TF is bound to the ribosome near the polypeptide exit
CC tunnel while the other half is free in the cytoplasm.
CC {ECO:0000269|PubMed:8633085}.
CC -!- DOMAIN: Consists of 3 domains; the N-terminus (residues 1-112) binds
CC the ribosome, the middle domain (residues 150-246) has PPIase activity,
CC while the discontinuous C-terminus (residues 113-149 and 247-432) binds
CC substrate and has intrinsic chaperone activity on its own.
CC {ECO:0000269|PubMed:14726952, ECO:0000269|PubMed:24812405}.
CC -!- PTM: (Microbial infection) ADP-ribosylated by the phage T4 protein
CC ModB. {ECO:0000269|PubMed:16112649}.
CC -!- DISRUPTION PHENOTYPE: Non-essential; synthetic lethality is seen in a
CC triple tig-dnaK-dnaJ disruption, although this depends on temperature
CC (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at
CC all at 43 degrees) and strain background.
CC {ECO:0000269|PubMed:14726952}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC {ECO:0000305}.
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DR EMBL; M34066; AAA62791.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73539.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76216.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40192.1; -; Genomic_DNA.
DR EMBL; X17642; CAA35634.1; -; Genomic_DNA.
DR EMBL; J05534; AAA23587.1; -; Genomic_DNA.
DR PIR; D64773; D64773.
DR RefSeq; NP_414970.1; NC_000913.3.
DR RefSeq; WP_001198386.1; NZ_STEB01000007.1.
DR PDB; 1L1P; NMR; -; A=148-249.
DR PDB; 1OMS; X-ray; 2.30 A; A/B/C=1-118.
DR PDB; 1P9Y; X-ray; 2.15 A; A/B=1-118.
DR PDB; 1W26; X-ray; 2.70 A; A/B=1-432.
DR PDB; 1W2B; X-ray; 3.50 A; 5=1-144.
DR PDB; 2MLX; NMR; -; A=1-432.
DR PDB; 2MLY; NMR; -; A=1-432.
DR PDB; 2MLZ; NMR; -; A=1-432.
DR PDB; 2VRH; EM; 19.00 A; A=1-432.
DR PDB; 4URD; EM; 7.70 A; A=1-115.
DR PDB; 5OWI; NMR; -; A/B=1-432.
DR PDB; 5OWJ; NMR; -; A/B=1-432.
DR PDB; 5ZR0; NMR; -; A=148-249.
DR PDB; 6D6S; NMR; -; A/B=1-432.
DR PDB; 7D6Z; EM; 3.40 A; h=1-117.
DR PDB; 7D80; EM; 4.10 A; 5=1-432.
DR PDBsum; 1L1P; -.
DR PDBsum; 1OMS; -.
DR PDBsum; 1P9Y; -.
DR PDBsum; 1W26; -.
DR PDBsum; 1W2B; -.
DR PDBsum; 2MLX; -.
DR PDBsum; 2MLY; -.
DR PDBsum; 2MLZ; -.
DR PDBsum; 2VRH; -.
DR PDBsum; 4URD; -.
DR PDBsum; 5OWI; -.
DR PDBsum; 5OWJ; -.
DR PDBsum; 5ZR0; -.
DR PDBsum; 6D6S; -.
DR PDBsum; 7D6Z; -.
DR PDBsum; 7D80; -.
DR AlphaFoldDB; P0A850; -.
DR SMR; P0A850; -.
DR BioGRID; 4259841; 557.
DR DIP; DIP-36226N; -.
DR IntAct; P0A850; 131.
DR STRING; 511145.b0436; -.
DR SWISS-2DPAGE; P0A850; -.
DR jPOST; P0A850; -.
DR PaxDb; P0A850; -.
DR PRIDE; P0A850; -.
DR EnsemblBacteria; AAC73539; AAC73539; b0436.
DR EnsemblBacteria; BAE76216; BAE76216; BAE76216.
DR GeneID; 66671262; -.
DR GeneID; 945081; -.
DR KEGG; ecj:JW0426; -.
DR KEGG; eco:b0436; -.
DR PATRIC; fig|1411691.4.peg.1840; -.
DR EchoBASE; EB0996; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_2_0_6; -.
DR InParanoid; P0A850; -.
DR OMA; KGIKTQF; -.
DR PhylomeDB; P0A850; -.
DR BioCyc; EcoCyc:EG11003-MON; -.
DR BioCyc; MetaCyc:EG11003-MON; -.
DR EvolutionaryTrace; P0A850; -.
DR PRO; PR:P0A850; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
DR GO; GO:0044183; F:protein folding chaperone; IDA:EcoCyc.
DR GO; GO:0043022; F:ribosome binding; IDA:EcoCyc.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IDA:EcoCyc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR Gene3D; 1.10.3120.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.30.70.1050; -; 1.
DR HAMAP; MF_00303; Trigger_factor_Tig; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR005215; Trig_fac.
DR InterPro; IPR008880; Trigger_fac_C.
DR InterPro; IPR037041; Trigger_fac_C_sf.
DR InterPro; IPR008881; Trigger_fac_ribosome-bd_bac.
DR InterPro; IPR036611; Trigger_fac_ribosome-bd_sf.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR30560; PTHR30560; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF05698; Trigger_C; 1.
DR Pfam; PF05697; Trigger_N; 1.
DR PIRSF; PIRSF003095; Trigger_factor; 1.
DR SUPFAM; SSF102735; SSF102735; 1.
DR SUPFAM; SSF109998; SSF109998; 1.
DR TIGRFAMs; TIGR00115; tig; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cell cycle; Cell division; Chaperone;
KW Cytoplasm; Direct protein sequencing; Isomerase; Reference proteome;
KW Rotamase.
FT CHAIN 1..432
FT /note="Trigger factor"
FT /id="PRO_0000179347"
FT DOMAIN 161..246
FT /note="PPIase FKBP-type"
FT REGION 1..112
FT /note="Ribosome-binding"
FT /evidence="ECO:0000269|PubMed:14726952"
FT REGION 148..251
FT /note="Dispensable for chaperone activity, although its
FT removal significantly decreases antiaggregation activity"
FT /evidence="ECO:0000269|PubMed:14726952,
FT ECO:0000269|PubMed:24812405"
FT MOD_RES 45
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000269|PubMed:16112649"
FT MUTAGEN 44..46
FT /note="FRK->AAA: Decreases association with ribosomes."
FT /evidence="ECO:0000269|PubMed:12226666"
FT MUTAGEN 140
FT /note="M->E: Significantly decreases antiaggregation
FT activity."
FT /evidence="ECO:0000269|PubMed:24812405"
FT MUTAGEN 374..387
FT /note="MASAYEDPKEVIEF->AASAAEDPKEAIEA: Significantly
FT decreased affinity for substrate PhoA, significantly
FT decreases antiaggregation activity."
FT /evidence="ECO:0000269|PubMed:24812405"
FT CONFLICT 118
FT /note="Q -> E (in Ref. 1; AAA62791)"
FT /evidence="ECO:0000305"
FT CONFLICT 279..287
FT /note="KSAIRNRVK -> RAPSVTALS (in Ref. 1; AAA62791)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1P9Y"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1P9Y"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:1P9Y"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1OMS"
FT HELIX 51..81
FT /evidence="ECO:0007829|PDB:1P9Y"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:1P9Y"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1P9Y"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1P9Y"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5OWI"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1L1P"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6D6S"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1W26"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:5OWI"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:1W26"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 263..297
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:1W26"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:5OWI"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 338..357
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 364..375
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 392..412
FT /evidence="ECO:0007829|PDB:1W26"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1W26"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:1W26"
SQ SEQUENCE 432 AA; 48193 MW; 42C3E3C335074164 CRC64;
MQVSVETTQG LGRRVTITIA ADSIETAVKS ELVNVAKKVR IDGFRKGKVP MNIVAQRYGA
SVRQDVLGDL MSRNFIDAII KEKINPAGAP TYVPGEYKLG EDFTYSVEFE VYPEVELQGL
EAIEVEKPIV EVTDADVDGM LDTLRKQQAT WKEKDGAVEA EDRVTIDFTG SVDGEEFEGG
KASDFVLAMG QGRMIPGFED GIKGHKAGEE FTIDVTFPEE YHAENLKGKA AKFAINLKKV
EERELPELTA EFIKRFGVED GSVEGLRAEV RKNMERELKS AIRNRVKSQA IEGLVKANDI
DVPAALIDSE IDVLRRQAAQ RFGGNEKQAL ELPRELFEEQ AKRRVVVGLL LGEVIRTNEL
KADEERVKGL IEEMASAYED PKEVIEFYSK NKELMDNMRN VALEEQAVEA VLAKAKVTEK
ETTFNELMNQ QA
