MSCS_ECOLI
ID MSCS_ECOLI Reviewed; 286 AA.
AC P0C0S1; P11666; Q2M9R8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Small-conductance mechanosensitive channel;
GN Name=mscS; Synonyms=yggB; OrderedLocusNames=b2924, JW2891;
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 / CS520;
RX PubMed=2546007; DOI=10.1111/j.1365-2958.1989.tb00221.x;
RA Alefounder P.R., Perham R.N.;
RT "Identification, molecular cloning and sequence analysis of a gene cluster
RT encoding the class II fructose 1,6-bisphosphate aldolase, 3-
RT phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate
RT dehydrogenase of Escherichia coli.";
RL Mol. Microbiol. 3:723-732(1989).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / AW405;
RX PubMed=2436228; DOI=10.1073/pnas.84.8.2297;
RA Martinac B., Buechner M., Delcour A.H., Adler J., Kung C.;
RT "Pressure-sensitive ion channel in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2297-2301(1987).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND SENSITIVITY TO OSMOTIC AND VOLTAGE
RP DIFFERENCES ACROSS THE CYTOPLASMIC MEMBRANE.
RC STRAIN=K12;
RX PubMed=7595939; DOI=10.1007/bf00238414;
RA Cui C., Smith D.O., Adler J.;
RT "Characterization of mechanosensitive channels in Escherichia coli
RT cytoplasmic membrane by whole-cell patch clamp recording.";
RL J. Membr. Biol. 144:31-42(1995).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHYSIOLOGICAL ROLE.
RC STRAIN=K12 / MJF379;
RX PubMed=10202137; DOI=10.1093/emboj/18.7.1730;
RA Levina N., Toetemeyer S., Stokes N.R., Louis P., Jones M.A., Booth I.R.;
RT "Protection of Escherichia coli cells against extreme turgor by activation
RT of MscS and MscL mechanosensitive channels: identification of genes
RT required for MscS activity.";
RL EMBO J. 18:1730-1737(1999).
RN [7]
RP LIPOSOME RECONSTITUTION, AND FUNCTION.
RC STRAIN=K12 / AW405;
RX PubMed=12080120; DOI=10.1016/s0006-3495(02)75169-2;
RA Sukharev S.;
RT "Purification of the small mechanosensitive channel of Escherichia coli
RT (MscS): the subunit structure, conduction, and gating characteristics in
RT liposomes.";
RL Biophys. J. 83:290-298(2002).
RN [8]
RP LIPOSOME RECONSTITUTION, FUNCTION, AND MUTAGENESIS OF VAL-40.
RC STRAIN=K12 / MJF379;
RX PubMed=12015316; DOI=10.1074/jbc.m202497200;
RA Okada K., Moe P.C., Blount P.;
RT "Functional design of bacterial mechanosensitive channels. Comparisons and
RT contrasts illuminated by random mutagenesis.";
RL J. Biol. Chem. 277:27682-27688(2002).
RN [9]
RP CROSS-LINKING OF THE C-TERMINI INHIBITS CHANNEL OPENING, DOMAIN, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MJF379;
RX PubMed=12551944; DOI=10.1074/jbc.m212073200;
RA Koprowski P., Kubalski A.;
RT "C termini of the Escherichia coli mechanosensitive ion channel (MscS) move
RT apart upon the channel opening.";
RL J. Biol. Chem. 278:11237-11245(2003).
RN [10]
RP SUBUNIT IN THE CLOSED STATE, MUTAGENESIS OF SER-58 AND SER-267, AND DOMAIN.
RX PubMed=12767977; DOI=10.1074/jbc.m303188200;
RA Miller S., Edwards M.D., Ozdemir C., Booth I.R.;
RT "The closed structure of the MscS mechanosensitive channel. Cross-linking
RT of single cysteine mutants.";
RL J. Biol. Chem. 278:32246-32250(2003).
RN [11]
RP C-TERMINAL DELETIONS.
RX PubMed=15304354; DOI=10.1016/j.febslet.2004.07.045;
RA Schumann U., Edwards M.D., Li C., Booth I.R.;
RT "The conserved carboxy-terminus of the MscS mechanosensitive channel is not
RT essential but increases stability and activity.";
RL FEBS Lett. 572:233-237(2004).
RN [12]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [13]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [14]
RP 3D-STRUCTURE MODELING, MUTAGENESIS OF CONSERVED GLY AND ALA RESIDUES IN
RP TM3, AND PRESENTATION OF MODELS OF THE CLOSED STATE CHANNEL AND CLOSED TO
RP OPEN STATE TRANSITIONS.
RC STRAIN=K12 / MJF431;
RX PubMed=15665866; DOI=10.1038/nsmb895;
RA Edwards M.D., Li Y., Kim S., Miller S., Bartlett W., Black S., Dennison S.,
RA Iscla I., Blount P., Bowie J.U., Booth I.R.;
RT "Pivotal role of the glycine-rich TM3 helix in gating the MscS
RT mechanosensitive channel.";
RL Nat. Struct. Mol. Biol. 12:113-119(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 27-280 PROBABLY IN THE OPEN STATE,
RP SUBUNIT, FUNCTION, TOPOLOGY, AND DOMAIN.
RC STRAIN=K12;
RX PubMed=12446901; DOI=10.1126/science.1077945;
RA Bass R.B., Strop P., Barclay M., Rees D.C.;
RT "Crystal structure of Escherichia coli MscS, a voltage-modulated and
RT mechanosensitive channel.";
RL Science 298:1582-1587(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RX PubMed=23012406; DOI=10.1073/pnas.1202286109;
RA Pliotas C., Ward R., Branigan E., Rasmussen A., Hagelueken G., Huang H.,
RA Black S.S., Booth I.R., Schiemann O., Naismith J.H.;
RT "Conformational state of the MscS mechanosensitive channel in solution
RT revealed by pulsed electron-electron double resonance (PELDOR)
RT spectroscopy.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E2675-E2682(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 272-286, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ALA-158.
RX PubMed=23074248; DOI=10.1073/pnas.1207977109;
RA Zhang X., Wang J., Feng Y., Ge J., Li W., Sun W., Iscla I., Yu J.,
RA Blount P., Li Y., Yang M.;
RT "Structure and molecular mechanism of an anion-selective mechanosensitive
RT channel of small conductance.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18180-18185(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (4.37 ANGSTROMS), SUBUNIT, AND TOPOLOGY.
RX PubMed=23339071; DOI=10.1002/pro.2222;
RA Lai J.Y., Poon Y.S., Kaiser J.T., Rees D.C.;
RT "Open and shut: crystal structures of the dodecylmaltoside solubilized
RT mechanosensitive channel of small conductance from Escherichia coli and
RT Helicobacter pylori at 4.4 A and 4.1 A resolutions.";
RL Protein Sci. 22:502-509(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS), FUNCTION, SUBUNIT, TOPOLOGY, AND
RP DOMAIN.
RX PubMed=26551077; DOI=10.1038/nsmb.3120;
RA Pliotas C., Dahl A.C., Rasmussen T., Mahendran K.R., Smith T.K., Marius P.,
RA Gault J., Banda T., Rasmussen A., Miller S., Robinson C.V., Bayley H.,
RA Sansom M.S., Booth I.R., Naismith J.H.;
RT "The role of lipids in mechanosensation.";
RL Nat. Struct. Mol. Biol. 22:991-998(2015).
CC -!- FUNCTION: Mechanosensitive channel that participates in the regulation
CC of osmotic pressure changes within the cell, opening in response to
CC stretch forces in the membrane lipid bilayer, without the need for
CC other proteins. Contributes to normal resistance to hypoosmotic shock.
CC Forms an ion channel of 1.0 nanosiemens conductance with a slight
CC preference for anions. The channel is sensitive to voltage; as the
CC membrane is depolarized, less tension is required to open the channel
CC and vice versa. The channel is characterized by short bursts of
CC activity that last for a few seconds. {ECO:0000269|PubMed:10202137,
CC ECO:0000269|PubMed:12015316, ECO:0000269|PubMed:12080120,
CC ECO:0000269|PubMed:12446901, ECO:0000269|PubMed:12551944,
CC ECO:0000269|PubMed:12767977, ECO:0000269|PubMed:23012406,
CC ECO:0000269|PubMed:23074248, ECO:0000269|PubMed:2436228,
CC ECO:0000269|PubMed:26551077, ECO:0000269|PubMed:7595939}.
CC -!- SUBUNIT: Homoheptamer. {ECO:0000269|PubMed:12446901,
CC ECO:0000269|PubMed:12767977, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:23012406, ECO:0000269|PubMed:23074248,
CC ECO:0000269|PubMed:23339071, ECO:0000269|PubMed:26551077}.
CC -!- INTERACTION:
CC P0C0S1; P0C0S1: mscS; NbExp=7; IntAct=EBI-554616, EBI-554616;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10202137,
CC ECO:0000269|PubMed:12551944, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:23012406, ECO:0000269|PubMed:23074248,
CC ECO:0000269|PubMed:2436228, ECO:0000269|PubMed:7595939}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12446901,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:23012406,
CC ECO:0000269|PubMed:23339071, ECO:0000269|PubMed:26551077}.
CC -!- DOMAIN: The channel pore is formed by TM3 and the loop between TM2 and
CC TM3. After a sharp turn at Gly-113, an alpha-helix (residues 114-127)
CC is oriented nearly parallel to the plane of the putative lipid bilayer.
CC On the intracellular side of the channel, the permeation pathway of
CC MscS does not connect directly to the cytoplasm but instead opens to a
CC large chamber that is connected to the cytoplasm. This chamber
CC resembles a molecular filter that could serve to prescreen large
CC molecules before they are allowed passage to the transmembrane pore.
CC The TM1 and TM2 helices appear to be likely candidates for mediating
CC the tension and voltage sensitivities of MscS. Gating requires large
CC rearrangements of at least the C-terminus, and is probably influenced
CC by freely exchangeable membrane lipids that bind in grooves and pockets
CC between the transmembrane helices and enhance the stability of the
CC closed channel conformation. In a hypoosmotic environment the membrane
CC is stretched, and lipids may be pulled into the lipid bilayer and away
CC from the protein, which is predicted to destabilize the closed
CC conformation and promote channel gating. {ECO:0000269|PubMed:12446901,
CC ECO:0000269|PubMed:12551944, ECO:0000269|PubMed:12767977,
CC ECO:0000269|PubMed:23074248, ECO:0000269|PubMed:26551077}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR EMBL; X14436; CAA32606.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69091.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75961.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76988.1; -; Genomic_DNA.
DR PIR; S04735; QQEC4A.
DR RefSeq; NP_417399.1; NC_000913.3.
DR RefSeq; WP_000389818.1; NZ_STEB01000001.1.
DR PDB; 2OAU; X-ray; 3.70 A; A/B/C/D/E/F/G=1-286.
DR PDB; 2VV5; X-ray; 3.45 A; A/B/C/D/E/F/G=1-286.
DR PDB; 3UDC; X-ray; 3.36 A; A/B/C/D/E/F/G=272-286.
DR PDB; 4AGE; X-ray; 4.84 A; A/B/C/D/E/F/G=1-286.
DR PDB; 4AGF; X-ray; 4.70 A; A/B/C/D/E/F/G=1-286.
DR PDB; 4HWA; X-ray; 4.37 A; A/B/C/D/E/F/G=1-286.
DR PDB; 5AJI; X-ray; 2.99 A; A/B/C/D/E/F/G=1-286.
DR PDB; 6PWN; EM; 3.10 A; A/B/C/D/E/F/G=1-286.
DR PDB; 6PWO; EM; 3.40 A; A/B/C/D/E/F/G=1-286.
DR PDB; 6PWP; EM; 4.10 A; A/B/C/D/E/F/G=1-286.
DR PDB; 6RLD; EM; 2.93 A; A/B/C/D/E/F/G=1-286.
DR PDB; 6UZH; EM; 3.30 A; A/B/C/D/E/F/G=1-286.
DR PDB; 6VYK; EM; 3.20 A; A/B/C/D/E/F/G=1-286.
DR PDB; 6VYL; EM; 3.40 A; A/B/C/D/E/F/G=1-286.
DR PDB; 6VYM; EM; 3.70 A; A/B/C/D/E/F/G=1-286.
DR PDB; 7ONL; EM; 3.90 A; A/B/C/D/E/F/G=1-286.
DR PDB; 7OO6; EM; 3.10 A; A/B/C/D/E/F/G=1-286.
DR PDBsum; 2OAU; -.
DR PDBsum; 2VV5; -.
DR PDBsum; 3UDC; -.
DR PDBsum; 4AGE; -.
DR PDBsum; 4AGF; -.
DR PDBsum; 4HWA; -.
DR PDBsum; 5AJI; -.
DR PDBsum; 6PWN; -.
DR PDBsum; 6PWO; -.
DR PDBsum; 6PWP; -.
DR PDBsum; 6RLD; -.
DR PDBsum; 6UZH; -.
DR PDBsum; 6VYK; -.
DR PDBsum; 6VYL; -.
DR PDBsum; 6VYM; -.
DR PDBsum; 7ONL; -.
DR PDBsum; 7OO6; -.
DR AlphaFoldDB; P0C0S1; -.
DR SMR; P0C0S1; -.
DR BioGRID; 4259238; 255.
DR DIP; DIP-36192N; -.
DR IntAct; P0C0S1; 2.
DR STRING; 511145.b2924; -.
DR TCDB; 1.A.23.2.1; the small conductance mechanosensitive ion channel (mscs) family.
DR jPOST; P0C0S1; -.
DR PaxDb; P0C0S1; -.
DR PRIDE; P0C0S1; -.
DR EnsemblBacteria; AAC75961; AAC75961; b2924.
DR EnsemblBacteria; BAE76988; BAE76988; BAE76988.
DR GeneID; 66673199; -.
DR GeneID; 947416; -.
DR KEGG; ecj:JW2891; -.
DR KEGG; eco:b2924; -.
DR PATRIC; fig|1411691.4.peg.3808; -.
DR EchoBASE; EB1149; -.
DR eggNOG; COG0668; Bacteria.
DR HOGENOM; CLU_037945_1_1_6; -.
DR InParanoid; P0C0S1; -.
DR OMA; GMQDTLT; -.
DR PhylomeDB; P0C0S1; -.
DR BioCyc; EcoCyc:EG11160-MON; -.
DR EvolutionaryTrace; P0C0S1; -.
DR PRO; PR:P0C0S1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; IMP:EcoCyc.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR Gene3D; 2.30.30.60; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR045275; MscS_archaea/bacteria_type.
DR InterPro; IPR006685; MscS_channel.
DR InterPro; IPR011066; MscS_channel_C.
DR InterPro; IPR006686; MscS_channel_CS.
DR InterPro; IPR011014; MscS_channel_TM-2.
DR InterPro; IPR023408; MscS_dom_sf.
DR InterPro; IPR008910; TM_helix.
DR PANTHER; PTHR30221; PTHR30221; 1.
DR Pfam; PF00924; MS_channel; 1.
DR Pfam; PF05552; TM_helix; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR SUPFAM; SSF82689; SSF82689; 1.
DR SUPFAM; SSF82861; SSF82861; 1.
DR PROSITE; PS01246; UPF0003; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..286
FT /note="Small-conductance mechanosensitive channel"
FT /id="PRO_0000110238"
FT TOPO_DOM 1..30
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:12446901,
FT ECO:0000269|PubMed:26551077"
FT TOPO_DOM 53..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:12446901,
FT ECO:0000269|PubMed:26551077"
FT TOPO_DOM 89..90
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:12446901,
FT ECO:0000269|PubMed:26551077"
FT TOPO_DOM 112..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT MUTAGEN 40
FT /note="V->C,G,N: No detectable phenotype."
FT /evidence="ECO:0000269|PubMed:12015316"
FT MUTAGEN 40
FT /note="V->D,K: Normal growth stops, without cell death, due
FT to increased membrane permeability to potassium ions and
FT protons (permeability tested only for D substitutions)."
FT /evidence="ECO:0000269|PubMed:12015316"
FT MUTAGEN 58
FT /note="S->C: Readily forms disulfide bonds with cross-
FT linkers, suggesting that individual S-58 are only 3
FT Angstroms apart in the closed state, versus 33 Angstroms
FT apart in the open state crystal structure."
FT /evidence="ECO:0000269|PubMed:12767977"
FT MUTAGEN 158
FT /note="A->F: Decreased conductance, due to decreased
FT diameter of the channel portal."
FT /evidence="ECO:0000269|PubMed:23074248"
FT MUTAGEN 266..286
FT /note="ISFPYPQMDVNFKRVKEDKAA->HHHHHHLE: Normal levels of
FT channels are expressed; they recover more slowly than wild-
FT type cells after desensitization."
FT /evidence="ECO:0000269|PubMed:15665866"
FT MUTAGEN 266..286
FT /note="ISFPYPQMDVNFKRVKEDKAA->LE: Fewer channels present in
FT the membrane, they require slightly more pressure to open
FT and do not recover after desensitization."
FT /evidence="ECO:0000269|PubMed:15665866"
FT MUTAGEN 267
FT /note="S->C: Provides biochemical evidence for heptameric
FT structure upon cross-linking."
FT /evidence="ECO:0000269|PubMed:12767977"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:6PWN"
FT TURN 16..20
FT /evidence="ECO:0007829|PDB:6PWN"
FT HELIX 23..57
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6PWN"
FT HELIX 63..89
FT /evidence="ECO:0007829|PDB:6RLD"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:6RLD"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6RLD"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 175..192
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6PWO"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6PWN"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 230..242
FT /evidence="ECO:0007829|PDB:6RLD"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:5AJI"
FT HELIX 246..263
FT /evidence="ECO:0007829|PDB:6RLD"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:6RLD"
SQ SEQUENCE 286 AA; 30896 MW; FF00AD64F795E9FE CRC64;
MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IVAALAIIIV GLIIARMISN AVNRLMISRK
IDATVADFLS ALVRYGIIAF TLIAALGRVG VQTASVIAVL GAAGLAVGLA LQGSLSNLAA
GVLLVMFRPF RAGEYVDLGG VAGTVLSVQI FSTTMRTADG KIIVIPNGKI IAGNIINFSR
EPVRRNEFII GVAYDSDIDQ VKQILTNIIQ SEDRILKDRE MTVRLNELGA SSINFVVRVW
SNSGDLQNVY WDVLERIKRE FDAAGISFPY PQMDVNFKRV KEDKAA
