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 27-MAR-2024, entry version 148. DE RecName: Full=Small-conductance mechanosensitive channel; GN Name=mscS; Synonyms=yggB; OrderedLocusNames=b2924, JW2891; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7OO0; EM; 3.10 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 PDB; 7RAZ; EM; 3.40 A; A/B/C/D/E/F/G=1-286. DR PDB; 8DDJ; EM; 3.10 A; A/B/C/D/E/F/G=1-280. 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; 7OO0; -. DR PDBsum; 7OO6; -. DR PDBsum; 7RAZ; -. DR PDBsum; 8DDJ; -. DR AlphaFoldDB; P0C0S1; -. DR EMDB; EMD-12997; -. DR EMDB; EMD-13003; -. DR EMDB; EMD-13006; -. DR EMDB; EMD-20508; -. DR EMDB; EMD-20509; -. DR EMDB; EMD-20510; -. DR EMDB; EMD-20959; -. DR EMDB; EMD-21462; -. DR EMDB; EMD-21463; -. DR EMDB; EMD-21464; -. DR EMDB; EMD-24390; -. DR EMDB; EMD-27337; -. DR EMDB; EMD-4919; -. 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; 511145-b2924; -. DR EnsemblBacteria; AAC75961; AAC75961; b2924. DR GeneID; 75205238; -. 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; FTIRVWA; -. DR OrthoDB; 9809206at2; -. DR PhylomeDB; P0C0S1; -. DR BioCyc; EcoCyc:EG11160-MONOMER; -. DR BioCyc; MetaCyc:EG11160-MONOMER; -. DR EvolutionaryTrace; P0C0S1; -. DR PRO; PR:P0C0S1; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016020; C:membrane; IDA:EcoCyc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008381; F:mechanosensitive monoatomic ion channel activity; IDA:UniProtKB. DR GO; GO:0009992; P:intracellular water homeostasis; IMP:EcoCyc. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IDA:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR Gene3D; 1.10.287.1260; -; 1. DR Gene3D; 2.30.30.60; -; 1. DR Gene3D; 3.30.70.100; -; 1. DR InterPro; IPR010920; LSM_dom_sf. DR InterPro; IPR049142; MS_channel_1st. DR InterPro; IPR049278; MS_channel_C. DR InterPro; IPR008910; MSC_TM_helix. DR InterPro; IPR045275; MscS_archaea/bacteria_type. DR InterPro; IPR023408; MscS_beta-dom_sf. DR InterPro; IPR006685; MscS_channel_2nd. DR InterPro; IPR011066; MscS_channel_C_sf. DR InterPro; IPR006686; MscS_channel_CS. DR InterPro; IPR011014; MscS_channel_TM-2. DR PANTHER; PTHR30221; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1. DR PANTHER; PTHR30221:SF1; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1. DR Pfam; PF21088; MS_channel_1st; 1. DR Pfam; PF05552; MS_channel_1st_1; 1. DR Pfam; PF00924; MS_channel_2nd; 1. DR Pfam; PF21082; MS_channel_3rd; 1. DR SUPFAM; SSF82689; Mechanosensitive channel protein MscS (YggB), C-terminal domain; 1. DR SUPFAM; SSF82861; Mechanosensitive channel protein MscS (YggB), transmembrane region; 1. DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 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 FT cross-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 FT wild-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 //