PSB_MYCTU
ID PSB_MYCTU Reviewed; 291 AA.
AC P9WHT9; L0T8V8; O33245; Q7D7I2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Proteasome subunit beta {ECO:0000255|HAMAP-Rule:MF_02113};
DE EC=3.4.25.1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE AltName: Full=20S proteasome beta subunit {ECO:0000255|HAMAP-Rule:MF_02113};
DE AltName: Full=Proteasome core protein PrcB {ECO:0000255|HAMAP-Rule:MF_02113};
DE Flags: Precursor;
GN Name=prcB {ECO:0000255|HAMAP-Rule:MF_02113}; OrderedLocusNames=Rv2110c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, SUBUNIT, ACTIVITY REGULATION, KINETIC PARAMETERS, AND DOMAIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16468985; DOI=10.1111/j.1365-2958.2005.05035.x;
RA Lin G., Hu G., Tsu C., Kunes Y.Z., Li H., Dick L., Parsons T., Li P.,
RA Chen Z., Zwickl P., Weich N., Nathan C.;
RT "Mycobacterium tuberculosis prcBA genes encode a gated proteasome with
RT broad oligopeptide specificity.";
RL Mol. Microbiol. 59:1405-1416(2006).
RN [3]
RP PROTEIN SUBSTRATES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17082771; DOI=10.1038/sj.emboj.7601405;
RA Pearce M.J., Arora P., Festa R.A., Butler-Wu S.M., Gokhale R.S.,
RA Darwin K.H.;
RT "Identification of substrates of the Mycobacterium tuberculosis
RT proteasome.";
RL EMBO J. 25:5423-5432(2006).
RN [4]
RP ROLE IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18059281; DOI=10.1038/nm1683;
RA Gandotra S., Schnappinger D., Monteleone M., Hillen W., Ehrt S.;
RT "In vivo gene silencing identifies the Mycobacterium tuberculosis
RT proteasome as essential for the bacteria to persist in mice.";
RL Nat. Med. 13:1515-1520(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP ELECTRON MICROSCOPY, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20085764; DOI=10.1016/j.febslet.2009.12.057;
RA Poulsen C., Holton S., Geerlof A., Wilmanns M., Song Y.H.;
RT "Stoichiometric protein complex formation and over-expression using the
RT prokaryotic native operon structure.";
RL FEBS Lett. 584:669-674(2010).
RN [7]
RP ROLE IN PERSISTENCE, DISRUPTION PHENOTYPE, ACTIVE SITE, AND MUTAGENESIS OF
RP THR-58.
RC STRAIN=H37Rv;
RX PubMed=20711362; DOI=10.1371/journal.ppat.1001040;
RA Gandotra S., Lebron M.B., Ehrt S.;
RT "The Mycobacterium tuberculosis proteasome active site threonine is
RT essential for persistence yet dispensable for replication and resistance to
RT nitric oxide.";
RL PLoS Pathog. 6:E1001040-E1001040(2010).
RN [8]
RP PHOSPHORYLATION, AND PROCESSING.
RC STRAIN=H37Rv;
RX PubMed=25224505; DOI=10.1007/s12275-014-4416-2;
RA Anandan T., Han J., Baun H., Nyayapathy S., Brown J.T., Dial R.L.,
RA Moltalvo J.A., Kim M.S., Yang S.H., Ronning D.R., Husson R.N., Suh J.,
RA Kang C.M.;
RT "Phosphorylation regulates mycobacterial proteasome.";
RL J. Microbiol. 52:743-754(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 58-291 IN COMPLEXES WITH THE
RP ALPHA SUBUNIT AND WITH THE MLN-273 INHIBITOR, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16468986; DOI=10.1111/j.1365-2958.2005.05036.x;
RA Hu G., Lin G., Wang M., Dick L., Xu R.-M., Nathan C., Li H.;
RT "Structure of the Mycobacterium tuberculosis proteasome and mechanism of
RT inhibition by a peptidyl boronate.";
RL Mol. Microbiol. 59:1417-1428(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEXES WITH WILD-TYPE AND
RP OPEN-GATE ALPHA SUBUNIT MUTANT; INHIBITOR HT1171 AND INHIBITOR GL1,
RP ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19759536; DOI=10.1038/nature08357;
RA Lin G., Li D., de Carvalho L.P., Deng H., Tao H., Vogt G., Wu K.,
RA Schneider J., Chidawanyika T., Warren J.D., Li H., Nathan C.;
RT "Inhibitors selective for mycobacterial versus human proteasomes.";
RL Nature 461:621-626(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 58-291 IN COMPLEX WITH ALPHA
RP SUBUNIT AND FELLUTAMIDE B INHIBITOR, AND ACTIVITY REGULATION.
RX PubMed=20558127; DOI=10.1016/j.abb.2010.06.009;
RA Lin G., Li D., Chidawanyika T., Nathan C., Li H.;
RT "Fellutamide B is a potent inhibitor of the Mycobacterium tuberculosis
RT proteasome.";
RL Arch. Biochem. Biophys. 501:214-220(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-58 IN
RP COMPLEX WITH WILD-TYPE AND OPEN-GATE ALPHA SUBUNIT MUTANT, SUBUNIT, GATED
RP STRUCTURE, AND PROTEASOME ASSEMBLY PROCESS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20461058; DOI=10.1038/emboj.2010.95;
RA Li D., Li H., Wang T., Pan H., Lin G., Li H.;
RT "Structural basis for the assembly and gate closure mechanisms of the
RT Mycobacterium tuberculosis 20S proteasome.";
RL EMBO J. 29:2037-2047(2010).
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation. The
CC M.tuberculosis proteasome is able to cleave oligopeptides not only
CC after hydrophobic but also after basic, acidic and small neutral
CC residues (PubMed:16468985). In complex with the ATPase Mpa, degrades
CC protein targets conjugated to a prokaryotic ubiquitin-like protein
CC (Pup). Among the identified substrates of the M.tuberculosis proteasome
CC are the pupylated FabD, PanB and Mpa proteins (PubMed:17082771). One
CC function of the proteasome is to contribute to M.tuberculosis ability
CC to resist killing by host macrophages, since the core proteasome is
CC essential for persistence of the pathogen during the chronic phase of
CC infection in mice (PubMed:18059281). Likely functions to recycle amino
CC acids under nutrient starvation, thereby enabling the cell to maintain
CC basal metabolic activities (PubMed:20711362) (By similarity). The
CC mechanism of protection against bactericidal chemistries of the host's
CC immune response probably involves the degradation of proteins that are
CC irreversibly oxidized, nitrated, or nitrosated. A proteolysis-
CC independent activity of the proteasome core is required for optimal
CC growth of M.tuberculosis in mouse lungs and for RNI resistance; in
CC contrast, long-term survival of M.tuberculosis in stationary phase and
CC during starvation in vitro and in the chronic phase of mouse infection
CC required a proteolytically active proteasome (PubMed:20711362).
CC {ECO:0000250|UniProtKB:A0QZ47, ECO:0000255|HAMAP-Rule:MF_02113,
CC ECO:0000269|PubMed:16468985, ECO:0000269|PubMed:17082771,
CC ECO:0000269|PubMed:18059281, ECO:0000269|PubMed:20711362}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02113,
CC ECO:0000269|PubMed:16468985};
CC -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase ARC-20S
CC proteasome complex, likely via the docking of the C-termini of ARC into
CC the intersubunit pockets in the alpha-rings, may trigger opening of the
CC gate for substrate entry. Interconversion between the open-gate and
CC close-gate conformations leads to a dynamic regulation of the 20S
CC proteasome proteolysis activity. In vitro, chymotryptic and tryptic
CC activities of the proteasome are both completely inhibited by
CC epoxomicin and by the peptidyl boronate inhibitor MLN-273. Also
CC inhibited by Mg(2+), Ca(2+) and SDS. It was also shown that certain
CC oxathiazol-2-one compounds can act as selective suicide-substrate
CC inhibitors of the M.tuberculosis proteasome by irreversibly
CC cyclocarbonylating its active site threonine. Proteasome activity is
CC potently inhibited by fellutamide B (Ki=6.8 nM), a lipopeptide aldehyde
CC that forms a reversible bond with the beta-OH of the active site
CC threonine (PubMed:20558127). {ECO:0000255|HAMAP-Rule:MF_02113,
CC ECO:0000269|PubMed:16468985, ECO:0000269|PubMed:19759536,
CC ECO:0000269|PubMed:20558127}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56 uM for succinyl-LLVY-7-amino-4-methylcoumarin
CC {ECO:0000269|PubMed:16468985};
CC Vmax=0.24 nmol/min/mg enzyme with succinyl-LLVY-7-amino-4-
CC methylcoumarin as substrate {ECO:0000269|PubMed:16468985};
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02113}.
CC -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 beta
CC subunits that assemble into four stacked heptameric rings, resulting in
CC a barrel-shaped structure. The two inner rings, each composed of seven
CC catalytic beta subunits, are sandwiched by two outer rings, each
CC composed of seven alpha subunits. The catalytic chamber with the active
CC sites is on the inside of the barrel. Has a gated structure, the ends
CC of the cylinder being occluded by the N-termini of the alpha-subunits.
CC Is capped by the proteasome-associated ATPase, ARC (Mpa).
CC {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:16468985,
CC ECO:0000269|PubMed:16468986, ECO:0000269|PubMed:20085764,
CC ECO:0000269|PubMed:20461058}.
CC -!- INTERACTION:
CC P9WHT9; P9WHU1: prcA; NbExp=6; IntAct=EBI-7947958, EBI-7948002;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}.
CC -!- DOMAIN: In contrast to Rhodococus, the M.tuberculosis proteasome does
CC not require the propeptide of PrcB for correct folding and assembly.
CC {ECO:0000269|PubMed:16468985}.
CC -!- PTM: The unprocessed form of PrcB is phosphorylated by PknA. Processing
CC of PrcB is greatly retarded in the presence of H(2)O(2).
CC {ECO:0000269|PubMed:25224505}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking the core proteasome prcBA subunits
CC exhibit reduced growth and persistence in mice. They are also
CC attenuated in interferon-gamma-deficient mice. They also display
CC increased sensitivity to reactive nitrogen intermediates (RNI) and
CC increased resistance to oxidative stress. {ECO:0000269|PubMed:18059281,
CC ECO:0000269|PubMed:20711362}.
CC -!- BIOTECHNOLOGY: In the course of search for new antibiotics, a class of
CC oxathiazol-2-one compounds has been identified that selectively
CC inhibits the M.tuberculosis proteasome over the human proteasome and
CC that kills non-replicating M.tuberculosis.
CC {ECO:0000269|PubMed:19759536}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|HAMAP-
CC Rule:MF_02113}.
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DR EMBL; AL123456; CCP44885.1; -; Genomic_DNA.
DR PIR; A70512; A70512.
DR RefSeq; NP_216626.1; NC_000962.3.
DR RefSeq; WP_003411023.1; NZ_NVQJ01000058.1.
DR PDB; 2FHG; X-ray; 3.23 A; 2/C/E/G/H/J/L/N/P/R/T/V/X/Z=58-291.
DR PDB; 2FHH; X-ray; 2.99 A; 2/C/E/G/H/J/L/N/P/R/T/V/X/Z=58-291.
DR PDB; 2JAY; X-ray; 1.99 A; A=1-291.
DR PDB; 3H6F; X-ray; 2.51 A; 2/C/E/G/H/J/L/N/P/R/T/V/X/Z=59-291.
DR PDB; 3H6I; X-ray; 2.43 A; 2/C/E/G/H/J/L/N/P/R/T/V/X/Z=59-291.
DR PDB; 3HF9; X-ray; 2.88 A; 2/4/C/E/G/H/J/L/N/P/R/T/V/X/Z/c/e/g/h/j/l/n/p/r/t/v/x/z=59-291.
DR PDB; 3HFA; X-ray; 2.50 A; 2/C/E/G/H/J/L/N/P/R/T/V/X/Z=58-291.
DR PDB; 3KRD; X-ray; 2.50 A; 2/C/E/G/H/J/L/N/P/R/T/V/X/Z=58-291.
DR PDB; 3MFE; X-ray; 2.60 A; 2/C/E/H/J/L/N/P/R/T/X/Z=59-291, G/V=58-291.
DR PDB; 3MI0; X-ray; 2.20 A; 2/C/E/G/H/J/L/N/P/R/T/V/X/Z=58-291.
DR PDB; 3MKA; X-ray; 2.51 A; 2/C/E/G/H/J/L/N/P/R/T/V/X/Z=1-291.
DR PDB; 5LZP; EM; 3.45 A; A/C/E/F/G/I/K/L/N/O/P/R/T/U=59-291.
DR PDB; 5THO; X-ray; 3.00 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 5TRG; X-ray; 2.80 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 5TRR; X-ray; 3.10 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 5TRS; X-ray; 3.08 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 5TRY; X-ray; 3.00 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 5TS0; X-ray; 2.85 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 6BGL; EM; 3.40 A; P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c=58-291.
DR PDB; 6BGO; EM; 4.20 A; P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c=58-291.
DR PDB; 6OCW; X-ray; 2.60 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 6OCZ; X-ray; 2.65 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 6ODE; X-ray; 2.90 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=58-291.
DR PDB; 7PXC; EM; 3.84 A; H/J/L/M/N/P/R/S/U/V/W/Y/a/b=1-291.
DR PDBsum; 2FHG; -.
DR PDBsum; 2FHH; -.
DR PDBsum; 2JAY; -.
DR PDBsum; 3H6F; -.
DR PDBsum; 3H6I; -.
DR PDBsum; 3HF9; -.
DR PDBsum; 3HFA; -.
DR PDBsum; 3KRD; -.
DR PDBsum; 3MFE; -.
DR PDBsum; 3MI0; -.
DR PDBsum; 3MKA; -.
DR PDBsum; 5LZP; -.
DR PDBsum; 5THO; -.
DR PDBsum; 5TRG; -.
DR PDBsum; 5TRR; -.
DR PDBsum; 5TRS; -.
DR PDBsum; 5TRY; -.
DR PDBsum; 5TS0; -.
DR PDBsum; 6BGL; -.
DR PDBsum; 6BGO; -.
DR PDBsum; 6OCW; -.
DR PDBsum; 6OCZ; -.
DR PDBsum; 6ODE; -.
DR PDBsum; 7PXC; -.
DR AlphaFoldDB; P9WHT9; -.
DR SMR; P9WHT9; -.
DR IntAct; P9WHT9; 7.
DR MINT; P9WHT9; -.
DR STRING; 83332.Rv2110c; -.
DR DrugBank; DB04732; N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID.
DR PaxDb; P9WHT9; -.
DR DNASU; 887508; -.
DR GeneID; 887508; -.
DR KEGG; mtu:Rv2110c; -.
DR TubercuList; Rv2110c; -.
DR eggNOG; COG0638; Bacteria.
DR OMA; NLGMAMQ; -.
DR PhylomeDB; P9WHT9; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0035375; F:zymogen binding; IPI:CAFA.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IMP:UniProtKB.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:MTBBASE.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_02113_B; Proteasome_B_B; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR InterPro; IPR022483; PSB_actinobac.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03690; 20S_bact_beta; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Phosphoprotein; Protease; Proteasome; Reference proteome;
KW Threonine protease; Virulence; Zymogen.
FT PROPEP 1..57
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113,
FT ECO:0000269|PubMed:16468985"
FT /id="PRO_0000383485"
FT CHAIN 58..291
FT /note="Proteasome subunit beta"
FT /id="PRO_0000383486"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:20711362"
FT SITE 58
FT /note="Covalent link with the inhibitor MLN-273"
FT /evidence="ECO:0000269|PubMed:16468986"
FT MUTAGEN 58
FT /note="T->A: Loss of proteasome proteolytic activity. This
FT mutant enables optimal growth in vitro and in vivo, confers
FT RNI resistance but is not sufficient for persistence in
FT mice."
FT /evidence="ECO:0000269|PubMed:20711362"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:3MKA"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3MKA"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2JAY"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2JAY"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2JAY"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 106..127
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2JAY"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2JAY"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5LZP"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2JAY"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:2JAY"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2FHH"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:2JAY"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:2JAY"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:5LZP"
SQ SEQUENCE 291 AA; 30305 MW; 3FC3FCD81231E129 CRC64;
MTWPLPDRLS INSLSGTPAV DLSSFTDFLR RQAPELLPAS ISGGAPLAGG DAQLPHGTTI
VALKYPGGVV MAGDRRSTQG NMISGRDVRK VYITDDYTAT GIAGTAAVAV EFARLYAVEL
EHYEKLEGVP LTFAGKINRL AIMVRGNLAA AMQGLLALPL LAGYDIHASD PQSAGRIVSF
DAAGGWNIEE EGYQAVGSGS LFAKSSMKKL YSQVTDGDSG LRVAVEALYD AADDDSATGG
PDLVRGIFPT AVIIDADGAV DVPESRIAEL ARAIIESRSG ADTFGSDGGE K
