FIEF_ECOLI
ID FIEF_ECOLI Reviewed; 300 AA.
AC P69380; P32159; Q2M8L1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cation-efflux pump FieF {ECO:0000255|HAMAP-Rule:MF_01425, ECO:0000305};
DE AltName: Full=Ferrous-iron efflux pump FieF;
GN Name=fieF {ECO:0000255|HAMAP-Rule:MF_01425, ECO:0000303|PubMed:15549269};
GN Synonyms=yiiP; OrderedLocusNames=b3915, JW3886;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [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 METAL BINDING.
RX PubMed=14960568; DOI=10.1074/jbc.m400208200;
RA Chao Y., Fu D.;
RT "Thermodynamic studies of the mechanism of metal binding to the Escherichia
RT coli zinc transporter YiiP.";
RL J. Biol. Chem. 279:17173-17180(2004).
RN [5]
RP SUBUNIT.
RX PubMed=15258151; DOI=10.1074/jbc.m407044200;
RA Wei Y., Li H., Fu D.;
RT "Oligomeric state of the Escherichia coli metal transporter YiiP.";
RL J. Biol. Chem. 279:39251-39259(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15549269; DOI=10.1007/s00203-004-0739-4;
RA Grass G., Otto M., Fricke B., Haney C.J., Rensing C., Nies D.H.,
RA Munkelt D.;
RT "FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation
RT of iron and relieves iron stress.";
RL Arch. Microbiol. 183:9-18(2005).
RN [7]
RP FUNCTION, METAL BINDING, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF
RP ASP-157.
RX PubMed=16049012; DOI=10.1074/jbc.m506107200;
RA Wei Y., Fu D.;
RT "Selective metal binding to a membrane-embedded aspartate in the
RT Escherichia coli metal transporter YiiP (FieF).";
RL J. Biol. Chem. 280:33716-33724(2005).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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 [9]
RP FUNCTION, METAL BINDING, AND MUTAGENESIS OF ASP-49.
RX PubMed=16790427; DOI=10.1074/jbc.m602254200;
RA Wei Y., Fu D.;
RT "Binding and transport of metal ions at the dimer interface of the
RT Escherichia coli metal transporter YiiP.";
RL J. Biol. Chem. 281:23492-23502(2006).
RN [10] {ECO:0007744|PDB:2QFI}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) IN COMPLEX WITH ZINC, SUBUNIT, AND
RP DOMAIN.
RX PubMed=17717154; DOI=10.1126/science.1143748;
RA Lu M., Fu D.;
RT "Structure of the zinc transporter YiiP.";
RL Science 317:1746-1748(2007).
RN [11] {ECO:0007744|PDB:3H90}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 8-290 IN COMPLEX WITH ZINC,
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY,
RP DOMAIN, AND MUTAGENESIS OF LYS-77 AND HIS-232.
RX PubMed=19749753; DOI=10.1038/nsmb.1662;
RA Lu M., Chai J., Fu D.;
RT "Structural basis for autoregulation of the zinc transporter YiiP.";
RL Nat. Struct. Mol. Biol. 16:1063-1067(2009).
CC -!- FUNCTION: Divalent metal cation transporter which exports Zn(2+),
CC Cd(2+) and possibly Fe(2+) (PubMed:14960568, PubMed:15549269,
CC PubMed:16049012, PubMed:16790427, PubMed:19749753). May be involved in
CC zinc and iron detoxification by efflux (PubMed:15549269,
CC PubMed:19749753). In vitro, can also bind, but probably not transport,
CC Hg(2+), Co(2+), Ni(2+), Mn(2+), Ca(2+) and Mg(2+) (PubMed:14960568,
CC PubMed:16049012, PubMed:16790427). {ECO:0000269|PubMed:14960568,
CC ECO:0000269|PubMed:15549269, ECO:0000269|PubMed:16049012,
CC ECO:0000269|PubMed:16790427, ECO:0000269|PubMed:19749753}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + Zn(2+)(in) = H(+)(in) + Zn(2+)(out);
CC Xref=Rhea:RHEA:28839, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01425,
CC ECO:0000269|PubMed:15549269, ECO:0000305|PubMed:16049012};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cd(2+)(in) + H(+)(out) = Cd(2+)(out) + H(+)(in);
CC Xref=Rhea:RHEA:28739, ChEBI:CHEBI:15378, ChEBI:CHEBI:48775;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01425,
CC ECO:0000305|PubMed:16049012, ECO:0000305|PubMed:16790427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(2+)(in) + H(+)(out) = Fe(2+)(out) + H(+)(in);
CC Xref=Rhea:RHEA:29439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01425,
CC ECO:0000269|PubMed:15549269};
CC -!- ACTIVITY REGULATION: Cytoplasmic zinc binding may trigger movements of
CC two electrically repulsive cytoplasmic domains and reorient
CC transmembrane helices, thereby modulating coordination geometry of the
CC active site for zinc transport. It may modulate activity in response to
CC cytoplasmic metal fluctuations. {ECO:0000269|PubMed:19749753}.
CC -!- SUBUNIT: Homodimer (PubMed:15258151, PubMed:17717154, PubMed:19749753).
CC The subunits are held together in a parallel orientation through zinc
CC binding at the interface of the cytoplasmic domains (PubMed:17717154,
CC PubMed:19749753). {ECO:0000269|PubMed:15258151,
CC ECO:0000269|PubMed:17717154, ECO:0000269|PubMed:19749753}.
CC -!- INTERACTION:
CC P69380; P69380: fieF; NbExp=2; IntAct=EBI-15802920, EBI-15802920;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01425, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:16049012, ECO:0000269|PubMed:19749753}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_01425,
CC ECO:0000269|PubMed:16049012, ECO:0000269|PubMed:19749753}.
CC -!- INDUCTION: Induced by iron and zinc. {ECO:0000269|PubMed:15549269}.
CC -!- DOMAIN: The two transmembrane domains of the dimer swing out to yield a
CC Y-shaped structure (PubMed:17717154, PubMed:19749753). In each
CC protomer, the cytoplasmic domain adopts a metallochaperone-like protein
CC fold (PubMed:17717154, PubMed:19749753). Each protomer contains three
CC zinc-binding sites: a tetrahedral active Zn(2+) binding site for zinc
CC transport, which is located toward the center of the transmembrane
CC domain, and two cytoplasmic Zn(2+) binding sites that may serve as zinc
CC sensors and regulate activity (PubMed:17717154, PubMed:19749753).
CC {ECO:0000269|PubMed:17717154, ECO:0000269|PubMed:19749753}.
CC -!- MISCELLANEOUS: Asp-49 and Asp-157 are required for both metal binding
CC and transport process (PubMed:16049012, PubMed:16790427). Asp-49 is a
CC selective binding residue for Zn(2+), Cd(2+) and Fe(2+)
CC (PubMed:16790427). Asp-157 is a highly specific coordination residue
CC for Zn(2+) and Cd(2+), but not for Hg(2+) and Fe(2+) (PubMed:16049012).
CC {ECO:0000269|PubMed:16049012, ECO:0000269|PubMed:16790427}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. FieF subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01425, ECO:0000305}.
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DR EMBL; L19201; AAB03047.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76897.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77395.1; -; Genomic_DNA.
DR PIR; S40858; S40858.
DR RefSeq; NP_418350.1; NC_000913.3.
DR RefSeq; WP_001076742.1; NZ_SSZK01000014.1.
DR PDB; 2QFI; X-ray; 3.80 A; A/B=1-300.
DR PDB; 3H90; X-ray; 2.90 A; A/B/C/D=8-290.
DR PDBsum; 2QFI; -.
DR PDBsum; 3H90; -.
DR AlphaFoldDB; P69380; -.
DR SMR; P69380; -.
DR BioGRID; 4261076; 7.
DR DIP; DIP-48564N; -.
DR STRING; 511145.b3915; -.
DR TCDB; 2.A.4.7.1; the cation diffusion facilitator (cdf) family.
DR PaxDb; P69380; -.
DR PRIDE; P69380; -.
DR EnsemblBacteria; AAC76897; AAC76897; b3915.
DR EnsemblBacteria; BAE77395; BAE77395; BAE77395.
DR GeneID; 66672177; -.
DR GeneID; 948413; -.
DR KEGG; ecj:JW3886; -.
DR KEGG; eco:b3915; -.
DR PATRIC; fig|1411691.4.peg.2790; -.
DR EchoBASE; EB1819; -.
DR eggNOG; COG0053; Bacteria.
DR HOGENOM; CLU_013430_3_0_6; -.
DR InParanoid; P69380; -.
DR OMA; IEMHLIV; -.
DR PhylomeDB; P69380; -.
DR BioCyc; EcoCyc:YIIP-MON; -.
DR BioCyc; MetaCyc:YIIP-MON; -.
DR EvolutionaryTrace; P69380; -.
DR PRO; PR:P69380; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015341; F:zinc efflux active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015691; P:cadmium ion transport; IDA:EcoCyc.
DR GO; GO:0006876; P:cellular cadmium ion homeostasis; IDA:EcoCyc.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:EcoCyc.
DR GO; GO:0006826; P:iron ion transport; IDA:EcoCyc.
DR GO; GO:0006829; P:zinc ion transport; IDA:EcoCyc.
DR Gene3D; 1.20.1510.10; -; 1.
DR Gene3D; 3.30.70.1350; -; 1.
DR HAMAP; MF_01425; Cation_efflux_FieF; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027470; Cation_efflux_CTD.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR023783; Cation_efflux_FieF.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR Pfam; PF16916; ZT_dimer; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Iron;
KW Iron transport; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..300
FT /note="Cation-efflux pump FieF"
FT /id="PRO_0000206124"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16049012,
FT ECO:0000269|PubMed:19749753"
FT TRANSMEM 17..30
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19749753"
FT TOPO_DOM 31..41
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16049012,
FT ECO:0000269|PubMed:19749753"
FT TRANSMEM 42..58
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19749753"
FT TOPO_DOM 59..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16049012,
FT ECO:0000269|PubMed:19749753"
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19749753"
FT TOPO_DOM 104..117
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16049012,
FT ECO:0000269|PubMed:19749753"
FT TRANSMEM 118..136
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19749753"
FT TOPO_DOM 137..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16049012,
FT ECO:0000269|PubMed:19749753"
FT TRANSMEM 148..158
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19749753"
FT TOPO_DOM 159..178
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16049012,
FT ECO:0000269|PubMed:19749753"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19749753"
FT TOPO_DOM 199..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:16049012, ECO:0000269|PubMed:19749753"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="transported zinc"
FT /evidence="ECO:0000269|PubMed:17717154,
FT ECO:0000269|PubMed:19749753, ECO:0000305|PubMed:16790427,
FT ECO:0007744|PDB:2QFI, ECO:0007744|PDB:3H90"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="transported zinc"
FT /evidence="ECO:0000269|PubMed:17717154,
FT ECO:0000269|PubMed:19749753, ECO:0000305|PubMed:16790427,
FT ECO:0007744|PDB:2QFI, ECO:0007744|PDB:3H90"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:17717154,
FT ECO:0000269|PubMed:19749753, ECO:0007744|PDB:2QFI,
FT ECO:0007744|PDB:3H90"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:19749753,
FT ECO:0007744|PDB:3H90"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:17717154,
FT ECO:0000269|PubMed:19749753, ECO:0007744|PDB:2QFI,
FT ECO:0007744|PDB:3H90"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="transported zinc"
FT /evidence="ECO:0000269|PubMed:17717154,
FT ECO:0000269|PubMed:19749753, ECO:0000305|PubMed:16790427,
FT ECO:0007744|PDB:2QFI, ECO:0007744|PDB:3H90"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="transported zinc"
FT /evidence="ECO:0000269|PubMed:17717154,
FT ECO:0000269|PubMed:19749753, ECO:0000305|PubMed:16049012,
FT ECO:0007744|PDB:2QFI, ECO:0007744|PDB:3H90"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:19749753,
FT ECO:0007744|PDB:3H90"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:19749753,
FT ECO:0007744|PDB:3H90"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:19749753,
FT ECO:0007744|PDB:3H90"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:19749753,
FT ECO:0007744|PDB:3H90"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:19749753,
FT ECO:0007744|PDB:3H90"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="regulatory"
FT /evidence="ECO:0000269|PubMed:19749753,
FT ECO:0007744|PDB:3H90"
FT MUTAGEN 49
FT /note="D->A: Disrupts one Cd(2+)/Zn(2+)-binding site and
FT abolishes Cd(2+)/Zn(2+) transport."
FT /evidence="ECO:0000269|PubMed:16790427"
FT MUTAGEN 49
FT /note="D->C: Does not affect binding and transport of
FT Cd(2+) and Zn(2+). Can form a Cys-49-Hg(2+)-Cys-49
FT biscysteinate complex across the dimer interface."
FT /evidence="ECO:0000269|PubMed:16790427"
FT MUTAGEN 77
FT /note="K->D: Abolishes Zn(2+) transport activity."
FT /evidence="ECO:0000269|PubMed:19749753"
FT MUTAGEN 157
FT /note="D->A: Disrupts one Cd(2+)/Zn(2+)-binding site and
FT abolishes Cd(2+)/Zn(2+) transport. Does not alter binding
FT of Fe(2+) or Hg(2+)."
FT /evidence="ECO:0000269|PubMed:16049012"
FT MUTAGEN 157
FT /note="D->C: Does not affect binding and transport of
FT Cd(2+) and Zn(2+)."
FT /evidence="ECO:0000269|PubMed:16049012"
FT MUTAGEN 232
FT /note="H->A: Shows reduced Zn(2+) transport kinetics."
FT /evidence="ECO:0000269|PubMed:19749753"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:3H90"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:3H90"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3H90"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3H90"
FT HELIX 45..63
FT /evidence="ECO:0007829|PDB:3H90"
FT HELIX 78..103
FT /evidence="ECO:0007829|PDB:3H90"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3H90"
FT HELIX 119..141
FT /evidence="ECO:0007829|PDB:3H90"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:3H90"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3H90"
FT HELIX 180..205
FT /evidence="ECO:0007829|PDB:3H90"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:3H90"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3H90"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:3H90"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:3H90"
FT HELIX 257..274
FT /evidence="ECO:0007829|PDB:3H90"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3H90"
SQ SEQUENCE 300 AA; 32927 MW; A9ECC4D6ED9A750F CRC64;
MNQSYGRLVS RAAIAATAMA SLLLLIKIFA WWYTGSVSIL AALVDSLVDI GASLTNLLVV
RYSLQPADDN HSFGHGKAES LAALAQSMFI SGSALFLFLT GIQHLISPTP MTDPGVGVIV
TIVALICTII LVSFQRWVVR RTQSQAVRAD MLHYQSDVMM NGAILLALGL SWYGWHRADA
LFALGIGIYI LYSALRMGYE AVQSLLDRAL PDEERQEIID IVTSWPGVSG AHDLRTRQSG
PTRFIQIHLE MEDSLPLVQA HMVADQVEQA ILRRFPGSDV IIHQDPCSVV PREGKRSMLS
