ID   LETB_ECOLI              Reviewed;         877 AA.
AC   P76272; P97190; P97191;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   02-SEP-2026, entry version 157.
DE   RecName: Full=Lipophilic envelope-spanning tunnel protein B {ECO:0000303|PubMed:32359438};
DE   AltName: Full=Intermembrane transport protein LetB {ECO:0000305};
DE   AltName: Full=Lipid transporter YebT {ECO:0000303|PubMed:31870848};
GN   Name=letB {ECO:0000303|PubMed:32359438};
GN   Synonyms=yebT {ECO:0000303|PubMed:9278503};
GN   OrderedLocusNames=b1834, JW1823;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
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, SUBUNIT, AND DOMAIN.
RC   STRAIN=K12;
RX   PubMed=28388411; DOI=10.1016/j.cell.2017.03.019;
RA   Ekiert D.C., Bhabha G., Isom G.L., Greenan G., Ovchinnikov S.,
RA   Henderson I.R., Cox J.S., Vale R.D.;
RT   "Architectures of lipid transport systems for the bacterial outer
RT   membrane.";
RL   Cell 169:273-285(2017).
RN   [5]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND INDUCTION.
RX   PubMed=27795327; DOI=10.1128/jb.00606-16;
RA   Nakayama T., Zhang-Akiyama Q.M.;
RT   "pqiABC and yebST, putative mce operons of Escherichia coli, encode
RT   transport pathways and contribute to membrane integrity.";
RL   J. Bacteriol. 199:E00606-E00606(2017).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28819315; DOI=10.1038/s41598-017-09111-6;
RA   Isom G.L., Davies N.J., Chong Z.S., Bryant J.A., Jamshad M., Sharif M.,
RA   Cunningham A.F., Knowles T.J., Chng S.S., Cole J.A., Henderson I.R.;
RT   "MCE domain proteins: conserved inner membrane lipid-binding proteins
RT   required for outer membrane homeostasis.";
RL   Sci. Rep. 7:8608-8608(2017).
RN   [7] {ECO:0007744|PDB:6V0C, ECO:0007744|PDB:6V0D, ECO:0007744|PDB:6V0E, ECO:0007744|PDB:6V0F, ECO:0007744|PDB:6V0G, ECO:0007744|PDB:6V0H, ECO:0007744|PDB:6V0I, ECO:0007744|PDB:6V0J, ECO:0007744|PDB:6VCI}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.96 ANGSTROMS) OF 46-877 IN OPEN AND
RP   CLOSED STATES, X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 159-383, FUNCTION,
RP   NOMENCLATURE, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP   LEU-243; LEU-246; VAL-247; LEU-355; LEU-358 AND LEU-359.
RX   PubMed=32359438; DOI=10.1016/j.cell.2020.03.030;
RA   Isom G.L., Coudray N., MacRae M.R., McManus C.T., Ekiert D.C., Bhabha G.;
RT   "LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial
RT   Envelope.";
RL   Cell 181:653-664.e19(2020).
RN   [8] {ECO:0007744|PDB:6KZ3, ECO:0007744|PDB:6KZ4}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 46-509 AND 512-877,
RP   FUNCTION, SUBUNIT, AND DOMAIN.
RX   PubMed=31870848; DOI=10.1016/j.jmb.2019.12.008;
RA   Liu C., Ma J., Wang J., Wang H., Zhang L.;
RT   "Cryo-EM Structure of a Bacterial Lipid Transporter YebT.";
RL   J. Mol. Biol. 432:1008-1019(2020).
RN   [9] {ECO:0007744|PDB:7SEE, ECO:0007744|PDB:7SEF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 42-877 OF RING 6
RP   MUTANTS, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-123; LEU-126; VAL-127;
RP   LEU-243; LEU-246; VAL-247; LEU-355; LEU-358; LEU-359; ALA-473; TRP-476;
RP   ILE-477; LEU-595; ALA-598; LEU-599; PRO-701; ILE-703; ALA-705; ALA-706;
RP   GLY-707; VAL-708; LEU-711; ILE-714; LEU-715; PRO-717; PHE-830; PHE-833 AND
RP   ILE-834.
RX   PubMed=35077766; DOI=10.1016/j.jmb.2022.167463;
RA   Vieni C., Coudray N., Isom G.L., Bhabha G., Ekiert D.C.;
RT   "Role of Ring6 in the Function of the E. coli MCE Protein LetB.";
RL   J. Mol. Biol. 434:167463-167463(2022).
CC   -!- FUNCTION: Forms a tunnel that spans the entire periplasmic space
CC       (PubMed:28388411, PubMed:31870848, PubMed:32359438). Is probably
CC       involved in the transport of lipids between the inner membrane and the
CC       outer membrane through the tunnel (PubMed:28388411, PubMed:31870848,
CC       PubMed:32359438). Forms a dynamic tunnel sufficiently long to mediate
CC       lipid transport directly between the two membranes without the need for
CC       a shuttle protein (PubMed:32359438). Binds phospholipids
CC       (PubMed:28388411, PubMed:31870848, PubMed:32359438). Lipids bind inside
CC       the tunnel (PubMed:32359438). Required for outer membrane homeostasis
CC       (PubMed:28819315). Contributes to membrane integrity (PubMed:27795327).
CC       {ECO:0000269|PubMed:27795327, ECO:0000269|PubMed:28388411,
CC       ECO:0000269|PubMed:28819315, ECO:0000269|PubMed:31870848,
CC       ECO:0000269|PubMed:32359438}.
CC   -!- SUBUNIT: Homohexamer (PubMed:28388411, PubMed:31870848,
CC       PubMed:32359438, PubMed:35077766). May interact with LetA in the inner
CC       membrane (Probable). May also interact with partners in the outer
CC       membrane (Probable). {ECO:0000269|PubMed:28388411,
CC       ECO:0000269|PubMed:31870848, ECO:0000269|PubMed:32359438,
CC       ECO:0000269|PubMed:35077766, ECO:0000305|PubMed:27795327,
CC       ECO:0000305|PubMed:32359438}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:28819315}; Single-pass membrane protein
CC       {ECO:0000255}; Periplasmic side {ECO:0000269|PubMed:27795327,
CC       ECO:0000269|PubMed:32359438}.
CC   -!- INDUCTION: Induced by a defect in lipopolysaccharide molecules.
CC       {ECO:0000269|PubMed:27795327}.
CC   -!- DOMAIN: The seven MCE (Mammalian Cell Entry) domains of a single
CC       protomer of LetB resemble seven beads on a string (PubMed:32359438).
CC       Six copies of this linearly configured protomer associate laterally to
CC       form a homohexameric assembly (PubMed:32359438, PubMed:35077766). The
CC       LetB hexamers form an elongated tube consisting of seven stacked MCE
CC       rings, each formed from the association of six identical MCE domains,
CC       with a central tunnel (PubMed:28388411, PubMed:31870848,
CC       PubMed:32359438, PubMed:35077766). Rings 1, 5, 6 and 7 are dynamic and
CC       adopt open and closed states (PubMed:32359438). Studies with shorter
CC       mutant forms of LetB show that a five- or six-ring form of LetB is
CC       functional, but that the four-, three- and two-rings variants are
CC       stable and properly folded in vitro, but not functional
CC       (PubMed:32359438). Mutants lacking ring 1, ring 2, ring 5 or ring 7 are
CC       non functional (PubMed:35077766). Mutants lacking ring 6 or ring 3 are
CC       more resistant to lauryl sulfobetaine (LSB) and cholate
CC       (PubMed:35077766). {ECO:0000269|PubMed:28388411,
CC       ECO:0000269|PubMed:31870848, ECO:0000269|PubMed:32359438,
CC       ECO:0000269|PubMed:35077766}.
CC   -!- DISRUPTION PHENOTYPE: The letAB mutant is not sensitive to lauryl
CC       sulfobetaine (LSB), but the pqiAB-letAB double mutant is more sensitive
CC       to LSB than the pqiAB mutant (PubMed:28819315). Double mutation also
CC       increases sensitivity of the pqiAB mutant to caprylyl sulfobetaine
CC       (PubMed:28819315). {ECO:0000269|PubMed:28819315}.
CC   -!- SIMILARITY: Belongs to the PqiB 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; U00096; AAC74904.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15647.1; -; Genomic_DNA.
DR   PIR; B64945; B64945.
DR   RefSeq; NP_416348.2; NC_000913.3.
DR   RefSeq; WP_001326728.1; NZ_CP009789.1.
DR   PDB; 6KZ3; EM; 3.10 A; A/B/C/D/E/F=46-509.
DR   PDB; 6KZ4; EM; 3.00 A; A/B/C/D/E/F=512-877.
DR   PDB; 6V0C; EM; 3.46 A; A/B/C/D/E/F=46-877.
DR   PDB; 6V0D; EM; 3.49 A; A/B/C/D/E/F=46-877.
DR   PDB; 6V0E; EM; 3.06 A; A/B/C/D/E/F=46-877.
DR   PDB; 6V0F; EM; 2.96 A; A/B/C/D/E/F=46-877.
DR   PDB; 6V0G; EM; 3.03 A; A/B/C/D/E/F=46-877.
DR   PDB; 6V0H; EM; 3.60 A; A/B/C/D/E/F=46-877.
DR   PDB; 6V0I; EM; 3.43 A; A/B/C/D/E/F=46-877.
DR   PDB; 6V0J; EM; 3.78 A; A/B/C/D/E/F=46-877.
DR   PDB; 6VCI; X-ray; 2.15 A; A/C=159-383.
DR   PDB; 7SEE; EM; 3.20 A; A/B/C/D/E/F=43-877.
DR   PDB; 7SEF; EM; 3.55 A; A/B/C/D/E/F=43-877.
DR   PDB; 9N8W; EM; 3.50 A; B/C/D/E/F/G=1-877.
DR   PDB; 9N8X; EM; 3.50 A; B/C/D/E/F/G=1-877.
DR   AlphaFoldDB; P76272; -.
DR   EMDB; EMD-0784; -.
DR   EMDB; EMD-0785; -.
DR   EMDB; EMD-0786; -.
DR   EMDB; EMD-0787; -.
DR   EMDB; EMD-20993; -.
DR   EMDB; EMD-20994; -.
DR   EMDB; EMD-20995; -.
DR   EMDB; EMD-20996; -.
DR   EMDB; EMD-20997; -.
DR   EMDB; EMD-20998; -.
DR   EMDB; EMD-20999; -.
DR   EMDB; EMD-21000; -.
DR   EMDB; EMD-25066; -.
DR   EMDB; EMD-25067; -.
DR   EMDB; EMD-49148; -.
DR   EMDB; EMD-49152; -.
DR   SMR; P76272; -.
DR   BioGRID; 4259157; 14.
DR   BioGRID; 850709; 1.
DR   DIP; DIP-11815N; -.
DR   FunCoup; P76272; 113.
DR   IntAct; P76272; 6.
DR   STRING; 511145.b1834; -.
DR   TCDB; 9.A.69.1.2; the intermembrane phospholipid translocase (impl-t) family.
DR   jPOST; P76272; -.
DR   PaxDb; 511145-b1834; -.
DR   EnsemblBacteria; AAC74904; AAC74904; b1834.
DR   GeneID; 946352; -.
DR   KEGG; ecj:JW1823; -.
DR   KEGG; eco:b1834; -.
DR   KEGG; ecoc:C3026_10450; -.
DR   PATRIC; fig|511145.12.peg.1912; -.
DR   EchoBASE; EB3776; -.
DR   eggNOG; COG3008; Bacteria.
DR   HOGENOM; CLU_015836_0_0_6; -.
DR   InParanoid; P76272; -.
DR   OMA; RFWNISG; -.
DR   OrthoDB; 9806984at2; -.
DR   PhylomeDB; P76272; -.
DR   BioCyc; EcoCyc:G7007-MONOMER; -.
DR   PRO; PR:P76272; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0120009; P:intermembrane lipid transfer; IDA:EcoCyc.
DR   GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR   InterPro; IPR003399; Mce/MlaD.
DR   InterPro; IPR051800; PqiA-PqiB_transport.
DR   PANTHER; PTHR30462; INTERMEMBRANE TRANSPORT PROTEIN PQIB-RELATED; 1.
DR   PANTHER; PTHR30462:SF0; INTERMEMBRANE TRANSPORT PROTEIN YEBT; 1.
DR   Pfam; PF02470; MlaD; 6.
DR   PDBsum; 6KZ3; -.
DR   PDBsum; 6KZ4; -.
DR   PDBsum; 6V0C; -.
DR   PDBsum; 6V0D; -.
DR   PDBsum; 6V0E; -.
DR   PDBsum; 6V0F; -.
DR   PDBsum; 6V0G; -.
DR   PDBsum; 6V0H; -.
DR   PDBsum; 6V0I; -.
DR   PDBsum; 6V0J; -.
DR   PDBsum; 6VCI; -.
DR   PDBsum; 7SEE; -.
DR   PDBsum; 7SEF; -.
DR   PDBsum; 9N8W; -.
DR   PDBsum; 9N8X; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Lipid transport;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..877
FT                   /note="Lipophilic envelope-spanning tunnel protein B"
FT                   /id="PRO_0000169055"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:27795327"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..877
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:27795327"
FT   REGION          46..149
FT                   /note="MCE/MlaD 1"
FT                   /evidence="ECO:0000305|PubMed:32359438"
FT   REGION          160..272
FT                   /note="MCE/MlaD 2"
FT                   /evidence="ECO:0000305|PubMed:32359438"
FT   REGION          279..382
FT                   /note="MCE/MlaD 3"
FT                   /evidence="ECO:0000305|PubMed:32359438"
FT   REGION          391..499
FT                   /note="MCE/MlaD 4"
FT                   /evidence="ECO:0000305|PubMed:32359438"
FT   REGION          515..625
FT                   /note="MCE/MlaD 5"
FT                   /evidence="ECO:0000305|PubMed:32359438"
FT   REGION          634..737
FT                   /note="MCE/MlaD 6"
FT                   /evidence="ECO:0000305|PubMed:32359438"
FT   REGION          746..862
FT                   /note="MCE/MlaD 7"
FT                   /evidence="ECO:0000305|PubMed:32359438"
FT   MUTAGEN         123
FT                   /note="L->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         126
FT                   /note="L->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         127
FT                   /note="V->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         243
FT                   /note="L->N: Well folded and assembled into a hexameric
FT                   structure, but loses its function."
FT                   /evidence="ECO:0000269|PubMed:32359438,
FT                   ECO:0000269|PubMed:35077766"
FT   MUTAGEN         246
FT                   /note="L->N: Well folded and assembled into a hexameric
FT                   structure, but loses its function."
FT                   /evidence="ECO:0000269|PubMed:32359438,
FT                   ECO:0000269|PubMed:35077766"
FT   MUTAGEN         247
FT                   /note="V->N: Well folded and assembled into a hexameric
FT                   structure, but loses its function."
FT                   /evidence="ECO:0000269|PubMed:32359438,
FT                   ECO:0000269|PubMed:35077766"
FT   MUTAGEN         355
FT                   /note="L->N: Well folded and assembled into a hexameric
FT                   structure, but loses its function."
FT                   /evidence="ECO:0000269|PubMed:32359438,
FT                   ECO:0000269|PubMed:35077766"
FT   MUTAGEN         358
FT                   /note="L->N: Well folded and assembled into a hexameric
FT                   structure, but loses its function."
FT                   /evidence="ECO:0000269|PubMed:32359438,
FT                   ECO:0000269|PubMed:35077766"
FT   MUTAGEN         359
FT                   /note="L->N: Well folded and assembled into a hexameric
FT                   structure, but loses its function."
FT                   /evidence="ECO:0000269|PubMed:32359438,
FT                   ECO:0000269|PubMed:35077766"
FT   MUTAGEN         473
FT                   /note="A->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         476
FT                   /note="W->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         477
FT                   /note="I->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         595
FT                   /note="L->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         598
FT                   /note="A->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         599
FT                   /note="L->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         701
FT                   /note="P->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         703
FT                   /note="I->N: Does not affect function."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         705
FT                   /note="A->N: Does not affect function."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         706
FT                   /note="A->N: Does not affect function."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         707
FT                   /note="G->N: Partially affects function."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         708
FT                   /note="V->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         711
FT                   /note="L->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         714
FT                   /note="I->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         715
FT                   /note="L->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         717
FT                   /note="P->N: Does not affect function."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         830
FT                   /note="F->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         833
FT                   /note="F->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   MUTAGEN         834
FT                   /note="I->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:35077766"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:9N8W"
FT   HELIX           26..45
FT                   /evidence="ECO:0007829|PDB:9N8W"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          71..82
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          87..94
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   HELIX           96..101
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   HELIX           117..121
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          131..135
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          143..146
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          161..168
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          184..194
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          196..207
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   HELIX           209..211
FT                   /evidence="ECO:0007829|PDB:6KZ3"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          221..227
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          237..240
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          247..253
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:6KZ3"
FT   STRAND          267..273
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   HELIX           274..277
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          281..288
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   TURN            295..297
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          298..302
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          305..315
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   TURN            317..319
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          321..327
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   HELIX           329..334
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          340..344
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   HELIX           347..349
FT                   /evidence="ECO:0007829|PDB:6V0G"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   HELIX           357..360
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          363..367
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          371..373
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   STRAND          375..381
FT                   /evidence="ECO:0007829|PDB:6VCI"
FT   HELIX           382..385
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   TURN            386..388
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          389..391
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          393..401
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          410..413
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          416..426
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          431..437
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   HELIX           439..444
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          449..453
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          458..460
FT                   /evidence="ECO:0007829|PDB:7SEE"
FT   STRAND          467..470
FT                   /evidence="ECO:0007829|PDB:7SEE"
FT   HELIX           473..478
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          481..485
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          493..496
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   STRAND          498..500
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   HELIX           501..505
FT                   /evidence="ECO:0007829|PDB:6V0F"
FT   HELIX           506..508
FT                   /evidence="ECO:0007829|PDB:6KZ3"
FT   STRAND          510..512
FT                   /evidence="ECO:0007829|PDB:7SEE"
FT   HELIX           513..515
FT                   /evidence="ECO:0007829|PDB:6V0D"
FT   STRAND          516..523
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          525..527
FT                   /evidence="ECO:0007829|PDB:6V0D"
FT   STRAND          532..548
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          550..559
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   HELIX           561..566
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          569..575
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          580..582
FT                   /evidence="ECO:0007829|PDB:7SEE"
FT   STRAND          588..590
FT                   /evidence="ECO:0007829|PDB:7SEE"
FT   HELIX           597..600
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          602..607
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          612..619
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          623..626
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   HELIX           627..631
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          634..642
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          652..655
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          658..663
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          667..669
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   TURN            670..673
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          674..681
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   TURN            683..688
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          689..691
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          695..699
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          702..704
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          707..709
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   HELIX           711..714
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          718..722
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          731..736
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   HELIX           742..744
FT                   /evidence="ECO:0007829|PDB:6V0E"
FT   STRAND          745..747
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          749..755
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          765..768
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          771..780
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          783..786
FT                   /evidence="ECO:0007829|PDB:6V0E"
FT   STRAND          787..794
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   HELIX           799..801
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          803..805
FT                   /evidence="ECO:0007829|PDB:6V0E"
FT   STRAND          808..811
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          816..818
FT                   /evidence="ECO:0007829|PDB:9N8W"
FT   STRAND          820..822
FT                   /evidence="ECO:0007829|PDB:6V0D"
FT   STRAND          823..825
FT                   /evidence="ECO:0007829|PDB:9N8W"
FT   HELIX           831..833
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          837..839
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   HELIX           842..844
FT                   /evidence="ECO:0007829|PDB:6V0D"
FT   HELIX           848..850
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   STRAND          857..860
FT                   /evidence="ECO:0007829|PDB:6KZ4"
FT   HELIX           868..870
FT                   /evidence="ECO:0007829|PDB:6V0E"
SQ   SEQUENCE   877 AA;  94970 MW;  3F4585F094D2D05A CRC64;
     MSQETPASTT EAQIKNKRRI SPFWLLPFIA LMIASWLIWD SYQDRGNTVT IDFMSADGIV
     PGRTPVRYQG VEVGTVQDIS LSDDLRKIEV KVSIKSDMKD ALREETQFWL VTPKASLAGV
     SGLDALVGGN YIGMMPGKGK EQDHFVALDT QPKYRLDNGD LMIHLQAPDL GSLNSGSLVY
     FRKIPVGKVY DYAINPNKQG VVIDVLIERR FTDLVKKGSR FWNVSGVDAN VSISGAKVKL
     ESLAALVNGA IAFDSPEESK PAEAEDTFGL YEDLAHSQRG VIIKLELPSG AGLTADSTPL
     MYQGLEVGQL TKLDLNPGGK VTGEMTVDPS VVTLLRENTR IELRNPKLSL SDANLSALLT
     GKTFELVPGD GEPRKEFVVV PGEKALLHEP DVLTLTLTAP ESYGIDAGQP LILHGVQVGQ
     VIDRKLTSKG VTFTVAIEPQ HRELVKGDSK FVVNSRVDVK VGLDGVEFLG ASASEWINGG
     IRILPGDKGE MKASYPLYAN LEKALENSLS DLPTTTVSLS AETLPDVQAG SVVLYRKFEV
     GEVITVRPRA NAFDIDLHIK PEYRNLLTSN SVFWAEGGAK VQLNGSGLTV QASPLSRALK
     GAISFDNLSG ASASQRKGDK RILYASETAA RAVGGQITLH AFDAGKLAVG MPIRYLGIDI
     GQIQTLDLIT ARNEVQAKAV LYPEYVQTFA RGGTRFSVVT PQISAAGVEH LDTILQPYIN
     VEPGRGNPRR DFELQEATIT DSRYLDGLSI IVEAPEAGSL GIGTPVLFRG LEVGTVTGMT
     LGTLSDRVMI AMRISKRYQH LVRNNSVFWL ASGYSLDFGL TGGVVKTGTF NQFIRGGIAF
     ATPPGTPLAP KAQEGKHFLL QESEPKEWRE WGTALPK
//