HSLV_ECOLI
ID HSLV_ECOLI Reviewed; 176 AA.
AC P0A7B8; P31059; P97542; Q2M8M8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP-dependent protease subunit HslV {ECO:0000255|HAMAP-Rule:MF_00248};
DE EC=3.4.25.2 {ECO:0000255|HAMAP-Rule:MF_00248};
DE AltName: Full=Heat shock protein HslV {ECO:0000255|HAMAP-Rule:MF_00248};
GN Name=hslV {ECO:0000255|HAMAP-Rule:MF_00248}; Synonyms=htpO, yiiC;
GN OrderedLocusNames=b3932, JW3903;
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 INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8244018; DOI=10.1016/0378-1119(93)90167-2;
RA Chuang S.E., Burland V., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "Sequence analysis of four new heat-shock genes constituting the
RT hslTS/ibpAB and hslVU operons in Escherichia coli.";
RL Gene 134:1-6(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 1-125.
RX PubMed=9013898; DOI=10.1016/s0014-5793(96)01485-8;
RA Ohya S., Takii T., Yamazaki H., Matsumori M., Onozaki K., Watanabe M.,
RA Imaizumi Y.;
RT "Molecular cloning of a novel gene involved in serotonin receptor-mediated
RT signal transduction in rat stomach.";
RL FEBS Lett. 401:252-258(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
RA Dai K., Xu Y., Lutkenhaus J.;
RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=8662828; DOI=10.1074/jbc.271.24.14035;
RA Yoo S.J., Seol J.H., Shin D.H., Rohrwild M., Kang M.-S., Tanaka K.,
RA Goldberg A.L., Chung C.H.;
RT "Purification and characterization of the heat shock proteins HslV and HslU
RT that form a new ATP-dependent protease in Escherichia coli.";
RL J. Biol. Chem. 271:14035-14040(1996).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=8650174; DOI=10.1073/pnas.93.12.5808;
RA Rohrwild M., Coux O., Huang H.-C., Moerschell R.P., Yoo S.J., Seol J.H.,
RA Chung C.H., Goldberg A.L.;
RT "HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli
RT related to the eukaryotic proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5808-5813(1996).
RN [9]
RP EFFECTS OF ATP BINDING ON COMPLEX FORMATION.
RX PubMed=9299555; DOI=10.1006/bbrc.1997.7341;
RA Yoo S.J., Seol J.H., Seong I.S., Kang M.-S., Chung C.H.;
RT "ATP binding, but not its hydrolysis, is required for assembly and
RT proteolytic activity of the HslVU protease in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 238:581-585(1997).
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 FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=9288941; DOI=10.1111/j.1432-1033.1997.01143.x;
RA Seol J.H., Yoo S.J., Shin D.H., Shim Y.K., Kang M.-S., Goldberg A.L.,
RA Chung C.H.;
RT "The heat-shock protein HslVU from Escherichia coli is a protein-activated
RT ATPase as well as an ATP-dependent proteinase.";
RL Eur. J. Biochem. 247:1143-1150(1997).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9393683; DOI=10.1128/jb.179.23.7219-7225.1997;
RA Kanemori M., Nishihara K., Yanagi H., Yura T.;
RT "Synergistic roles of HslVU and other ATP-dependent proteases in
RT controlling in vivo turnover of sigma32 and abnormal proteins in
RT Escherichia coli.";
RL J. Bacteriol. 179:7219-7225(1997).
RN [13]
RP MUTAGENESIS OF THR-2; THR-3; SER-6; SER-104; SER-125; SER-144 AND SER-173,
RP AND ACTIVE SITE.
RX PubMed=9257689; DOI=10.1016/s0014-5793(97)00742-4;
RA Yoo S.J., Shim Y.K., Seong I.S., Seol J.H., Kang M.-S., Chung C.H.;
RT "Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the
RT proteolytic component of the ATP-dependent HslVU protease.";
RL FEBS Lett. 412:57-60(1997).
RN [14]
RP MUTAGENESIS OF CYS-160.
RX PubMed=9722513; DOI=10.1074/jbc.273.36.22929;
RA Yoo S.J., Kim H.H., Shin D.H., Lee C.S., Seong I.S., Seol J.H.,
RA Shimbara N., Tanaka K., Chung C.H.;
RT "Effects of the cys mutations on structure and function of the ATP-
RT dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in
RT HslU uncouples the ATP-dependent proteolysis by HslvU from ATP
RT hydrolysis.";
RL J. Biol. Chem. 273:22929-22935(1998).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10452560; DOI=10.1016/s0014-5793(99)00935-7;
RA Seong I.S., Oh J.Y., Yoo S.J., Seol J.H., Chung C.H.;
RT "ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU
RT protease in Escherichia coli.";
RL FEBS Lett. 456:211-214(1999).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX PubMed=10419524; DOI=10.1074/jbc.274.31.22002;
RA Kanemori M., Yanagi H., Yura T.;
RT "Marked instability of the sigma(32) heat shock transcription factor at
RT high temperature. Implications for heat shock regulation.";
RL J. Biol. Chem. 274:22002-22007(1999).
RN [17]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15696175; DOI=10.1038/nsmb898;
RA Burton R.E., Baker T.A., Sauer R.T.;
RT "Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.";
RL Nat. Struct. Mol. Biol. 12:245-251(2005).
RN [18]
RP REACTION MECHANISM.
RX PubMed=19801685; DOI=10.1074/jbc.m109.045807;
RA Lee J.W., Park E., Jeong M.S., Jeon Y.J., Eom S.H., Seol J.H., Chung C.H.;
RT "HslVU ATP-dependent protease utilizes maximally six among twelve threonine
RT active sites during proteolysis.";
RL J. Biol. Chem. 284:33475-33484(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=9177170; DOI=10.1073/pnas.94.12.6070;
RA Bochtler M., Ditzel L., Groll M., Huber R.;
RT "Crystal structure of heat shock locus V (HslV) from Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6070-6074(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP
RP ANALOG.
RX PubMed=10693812; DOI=10.1038/35001629;
RA Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D.,
RA Huber R.;
RT "The structures of HslU and the ATP-dependent protease HslU-HslV.";
RL Nature 403:800-805(2000).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-176.
RX PubMed=11114186; DOI=10.1073/pnas.250491797;
RA Song H.K., Hartmann C., Ramachandran R., Bochtler M., Behrendt R.,
RA Moroder L., Huber R.;
RT "Mutational studies on HslU and its docking mode with HslV.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14103-14108(2000).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-175.
RX PubMed=11250202; DOI=10.1016/s0969-2126(01)00570-6;
RA Wang J., Song J.J., Franklin M.C., Kamtekar S., Im Y.J., Rho S.H.,
RA Seong I.S., Lee C.S., Chung C.H., Eom S.H.;
RT "Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-
RT dependent proteolysis mechanism.";
RL Structure 9:177-184(2001).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-176.
RX PubMed=11709174; DOI=10.1016/s0969-2126(01)00670-0;
RA Wang J., Song J.J., Seong I.S., Franklin M.C., Kamtekar S., Eom S.H.,
RA Chung C.H.;
RT "Nucleotide-dependent conformational changes in a protease-associated
RT ATPase HslU.";
RL Structure 9:1107-1116(2001).
CC -!- FUNCTION: Protease subunit of a proteasome-like degradation complex
CC believed to be a general protein degrading machinery. The complex has
CC been shown to be involved in the specific degradation of heat shock
CC induced transcription factors such as RpoH and SulA. In addition, small
CC hydrophobic peptides are also hydrolyzed by HslV. HslV has weak
CC protease activity even in the absence of HslU, but this activity is
CC induced more than 100-fold in the presence of HslU. HslU recognizes
CC protein substrates and unfolds these before guiding them to HslV for
CC hydrolysis. HslV is not believed to degrade folded proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00248, ECO:0000269|PubMed:10419524,
CC ECO:0000269|PubMed:10452560, ECO:0000269|PubMed:15696175,
CC ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:8662828,
CC ECO:0000269|PubMed:9288941, ECO:0000269|PubMed:9393683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent cleavage of peptide bonds with broad
CC specificity.; EC=3.4.25.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00248,
CC ECO:0000269|PubMed:10419524, ECO:0000269|PubMed:10452560,
CC ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:9288941,
CC ECO:0000269|PubMed:9393683};
CC -!- ACTIVITY REGULATION: Allosterically activated by HslU binding.
CC {ECO:0000305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15696175};
CC Note=Arc is a repressor protein, Arc-MYL-st11 is a hyperstable
CC variant of Arc.;
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:15696175};
CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC complex is dependent on binding of ATP. {ECO:0000255|HAMAP-
CC Rule:MF_00248, ECO:0000269|PubMed:9177170}.
CC -!- INTERACTION:
CC P0A7B8; P0A6H5: hslU; NbExp=16; IntAct=EBI-552265, EBI-369317;
CC P0A7B8; P0A7B8: hslV; NbExp=6; IntAct=EBI-552265, EBI-552265;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_00248,
CC ECO:0000269|PubMed:8244018}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00248}.
CC -!- CAUTION: PubMed:9013898 sequence is supposed to originate from rat but,
CC based on sequence similarity, it seems that this is a case of bacterial
CC contamination from E.coli. {ECO:0000305}.
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DR EMBL; L19201; AAB03064.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76914.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77378.1; -; Genomic_DNA.
DR EMBL; D89965; BAA14040.1; ALT_SEQ; mRNA.
DR EMBL; L14281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JT0760; JT0760.
DR RefSeq; NP_418367.1; NC_000913.3.
DR RefSeq; WP_000208242.1; NZ_STEB01000017.1.
DR PDB; 1E94; X-ray; 2.80 A; A/B/C/D=2-176.
DR PDB; 1G4A; X-ray; 3.00 A; A/B/C/D=2-176.
DR PDB; 1G4B; X-ray; 7.00 A; M/N/O/P=2-176.
DR PDB; 1HQY; X-ray; 2.80 A; A/B/C/D=2-176.
DR PDB; 1HT1; X-ray; 2.80 A; A/B/C/D/V/X/Y/Z=2-176.
DR PDB; 1HT2; X-ray; 2.80 A; A/B/C/D/I/J/K/L=2-176.
DR PDB; 1NED; X-ray; 3.80 A; A/B/C=2-176.
DR PDB; 4G4E; X-ray; 2.89 A; A/B/C/D/E/F/G/H/I/J/K/L=2-175.
DR PDB; 5JI3; X-ray; 3.00 A; A/B/C/D=1-176.
DR PDB; 6PXI; X-ray; 3.45 A; A/B/C/D=2-175.
DR PDBsum; 1E94; -.
DR PDBsum; 1G4A; -.
DR PDBsum; 1G4B; -.
DR PDBsum; 1HQY; -.
DR PDBsum; 1HT1; -.
DR PDBsum; 1HT2; -.
DR PDBsum; 1NED; -.
DR PDBsum; 4G4E; -.
DR PDBsum; 5JI3; -.
DR PDBsum; 6PXI; -.
DR AlphaFoldDB; P0A7B8; -.
DR SMR; P0A7B8; -.
DR BioGRID; 4261781; 287.
DR ComplexPortal; CPX-2104; HslUV protease complex.
DR DIP; DIP-35866N; -.
DR IntAct; P0A7B8; 33.
DR STRING; 511145.b3932; -.
DR MEROPS; T01.006; -.
DR SWISS-2DPAGE; P0A7B8; -.
DR jPOST; P0A7B8; -.
DR PaxDb; P0A7B8; -.
DR PRIDE; P0A7B8; -.
DR EnsemblBacteria; AAC76914; AAC76914; b3932.
DR EnsemblBacteria; BAE77378; BAE77378; BAE77378.
DR GeneID; 67417555; -.
DR GeneID; 948429; -.
DR KEGG; ecj:JW3903; -.
DR KEGG; eco:b3932; -.
DR PATRIC; fig|1411691.4.peg.2773; -.
DR EchoBASE; EB1627; -.
DR eggNOG; COG5405; Bacteria.
DR HOGENOM; CLU_093872_1_0_6; -.
DR InParanoid; P0A7B8; -.
DR OMA; IMKGNAR; -.
DR PhylomeDB; P0A7B8; -.
DR BioCyc; EcoCyc:EG11676-MON; -.
DR BioCyc; MetaCyc:EG11676-MON; -.
DR BRENDA; 3.4.25.2; 2026.
DR EvolutionaryTrace; P0A7B8; -.
DR PRO; PR:P0A7B8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009376; C:HslUV protease complex; IDA:CAFA.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IMP:EcoCyc.
DR GO; GO:0034605; P:cellular response to heat; IC:ComplexPortal.
DR GO; GO:0030164; P:protein denaturation; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IDA:CAFA.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR CDD; cd01913; protease_HslV; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00248; HslV; 1.
DR InterPro; IPR022281; ATP-dep_Prtase_HsIV_su.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194; PTHR32194; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF039093; HslV; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03692; ATP_dep_HslV; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Sodium;
KW Stress response; Threonine protease.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..176
FT /note="ATP-dependent protease subunit HslV"
FT /id="PRO_0000148105"
FT ACT_SITE 2
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248,
FT ECO:0000269|PubMed:9257689"
FT BINDING 157
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 160
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 163
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT MUTAGEN 2
FT /note="T->S: 80% reduced protease activity in the absence
FT of HslU. Almost no effect in the presence of HslU."
FT /evidence="ECO:0000269|PubMed:9257689"
FT MUTAGEN 2
FT /note="T->V: No protease activity."
FT /evidence="ECO:0000269|PubMed:9257689"
FT MUTAGEN 3
FT /note="T->S,V: 80% reduced protease activity."
FT /evidence="ECO:0000269|PubMed:9257689"
FT MUTAGEN 6
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:9257689"
FT MUTAGEN 104
FT /note="S->A: 50% reduced protease activity."
FT /evidence="ECO:0000269|PubMed:9257689"
FT MUTAGEN 125
FT /note="S->A: Almost no protease activity."
FT /evidence="ECO:0000269|PubMed:9257689"
FT MUTAGEN 144
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:9257689"
FT MUTAGEN 160
FT /note="C->A,S: No protease activity. Cannot form complexes
FT with HslU."
FT /evidence="ECO:0000269|PubMed:9722513"
FT MUTAGEN 173
FT /note="S->A: Almost no protease activity."
FT /evidence="ECO:0000269|PubMed:9257689"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1E94"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:1E94"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1E94"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1E94"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1G4A"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1E94"
SQ SEQUENCE 176 AA; 19093 MW; 3B35E01F51486965 CRC64;
MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG TADAFTLFEL
FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD ETASLIITGN GDVVQPENDL
IAIGSGGPYA QAAARALLEN TELSAREIAE KALDIAGDIC IYTNHFHTIE ELSYKA
