CAIT_ECOLI
ID CAIT_ECOLI Reviewed; 504 AA.
AC P31553; P75624; Q6IU45;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000303|PubMed:12163501};
GN Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000303|PubMed:7815937};
GN Synonyms=yaaP; OrderedLocusNames=b0040, JW0039;
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=O44:K74;
RX PubMed=7815937; DOI=10.1111/j.1365-2958.1994.tb00470.x;
RA Eichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.;
RT "Molecular characterization of the cai operon necessary for carnitine
RT metabolism in Escherichia coli.";
RL Mol. Microbiol. 13:775-786(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 203.
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 [5]
RP PROTEIN SEQUENCE OF 1-12, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=12163501; DOI=10.1074/jbc.m206319200;
RA Jung H., Buchholz M., Clausen J., Nietschke M., Revermann A., Schmid R.,
RA Jung K.;
RT "CaiT of Escherichia coli, a new transporter catalyzing L-carnitine/gamma-
RT butyrobetaine exchange.";
RL J. Biol. Chem. 277:39251-39258(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-428.
RC STRAIN=B;
RX PubMed=12664169; DOI=10.1007/s00239-002-2423-0;
RA Lenski R.E., Winkworth C.L., Riley M.A.;
RT "Rates of DNA sequence evolution in experimental populations of Escherichia
RT coli during 20,000 generations.";
RL J. Mol. Evol. 56:498-508(2003).
RN [7]
RP 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 [8]
RP SUBUNIT.
RX PubMed=16365043; DOI=10.1074/jbc.m508993200;
RA Vinothkumar K.R., Raunser S., Jung H., Kuehlbrandt W.;
RT "Oligomeric structure of the carnitine transporter CaiT from Escherichia
RT coli.";
RL J. Biol. Chem. 281:4795-4801(2006).
RN [9]
RP DOMAIN, AND MOLECULAR DYNAMICS SIMULATIONS.
RX PubMed=22843728; DOI=10.1074/jbc.m112.397364;
RA Zomot E., Bahar I.;
RT "A conformational switch in a partially unwound helix selectively
RT determines the pathway for substrate release from the carnitine/gamma-
RT butyrobetaine antiporter CaiT.";
RL J. Biol. Chem. 287:31823-31832(2012).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF ASP-288; MET-295; ARG-299 AND THR-304.
RX PubMed=30846799; DOI=10.1038/s41598-019-40516-7;
RA Bracher S., Hilger D., Guerin K., Polyhach Y., Jeschke G., Krafczyk R.,
RA Giacomelli G., Jung H.;
RT "Comparison of the functional properties of trimeric and monomeric CaiT of
RT Escherichia coli.";
RL Sci. Rep. 9:3787-3787(2019).
RN [11] {ECO:0007744|PDB:2WSX}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH GAMMA-BUTYROBETAINE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RX PubMed=20829798; DOI=10.1038/nature09310;
RA Schulze S., Koster S., Geldmacher U., Terwisscha van Scheltinga A.C.,
RA Kuhlbrandt W.;
RT "Structural basis of Na(+)-independent and cooperative substrate/product
RT antiport in CaiT.";
RL Nature 467:233-236(2010).
RN [12] {ECO:0007744|PDB:3HFX}
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH CARNITINE, SUBUNIT,
RP SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF TYR-114;
RP TRP-316; TRP-323; TRP-324; TYR-327 AND GLN-330.
RX PubMed=20357772; DOI=10.1038/nsmb.1788;
RA Tang L., Bai L., Wang W.H., Jiang T.;
RT "Crystal structure of the carnitine transporter and insights into the
RT antiport mechanism.";
RL Nat. Struct. Mol. Biol. 17:492-496(2010).
CC -!- FUNCTION: Catalyzes the exchange of L-carnitine for gamma-butyrobetaine
CC (PubMed:12163501, PubMed:20829798, PubMed:30846799). Can also transport
CC D-carnitine and, with lower efficiency, acetyl-L-carnitine and glycine
CC betaine (PubMed:12163501). {ECO:0000269|PubMed:12163501,
CC ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:30846799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + 4-(trimethylamino)butanoate(in) = (R)-
CC carnitine(in) + 4-(trimethylamino)butanoate(out);
CC Xref=Rhea:RHEA:29427, ChEBI:CHEBI:16244, ChEBI:CHEBI:16347;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01049,
CC ECO:0000269|PubMed:12163501, ECO:0000269|PubMed:20829798,
CC ECO:0000269|PubMed:30846799};
CC -!- ACTIVITY REGULATION: Inhibited by the sulfhydryl reagent N-
CC ethylmaleimide, but not by the ionophore carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:12163501}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=105 uM for L-carnitine {ECO:0000269|PubMed:12163501};
CC KM=81.1 uM for L-carnitine {ECO:0000269|PubMed:20829798};
CC KM=45.3 uM for L-carnitine {ECO:0000269|PubMed:30846799};
CC Vmax=6058 nmol/min/mg enzyme {ECO:0000269|PubMed:12163501};
CC Vmax=4921 nmol/min/mg enzyme {ECO:0000269|PubMed:20829798};
CC Vmax=2.13 umol/min/mg enzyme {ECO:0000269|PubMed:30846799};
CC Note=kcat is 279 min(-1) with L-carnitine as substrate.
CC {ECO:0000269|PubMed:20829798};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000305|PubMed:12163501,
CC ECO:0000305|PubMed:7815937}.
CC -!- SUBUNIT: Homotrimer (PubMed:16365043, PubMed:20357772, PubMed:20829798,
CC PubMed:30846799). The monomer is stable in the membrane and is fully
CC functional, but physical contact between the protomers of a trimer may
CC facilitate conformational alterations associated with substrate binding
CC (PubMed:30846799). {ECO:0000269|PubMed:16365043,
CC ECO:0000269|PubMed:20357772, ECO:0000269|PubMed:20829798,
CC ECO:0000269|PubMed:30846799}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01049, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:20357772, ECO:0000269|PubMed:20829798}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_01049,
CC ECO:0000269|PubMed:20357772, ECO:0000269|PubMed:20829798}.
CC -!- DOMAIN: Contains two carnitine binding sites, a primary binding site at
CC the center of the protein and a secondary binding site at the bottom of
CC the intracellular vestibule (PubMed:20357772). Contains two gamma-
CC butyrobetaine binding sites, one in the central transport site, the
CC other in an extracellular binding pocket (PubMed:20829798). Binding of
CC both butyrobetaine molecules is cooperative, indicating that the
CC extracellular site is regulatory (PubMed:20829798). The occupied
CC regulatory site may increase the binding affinity of the transport site
CC and initiates substrate translocation (PubMed:20829798). Both L-
CC carnitine and gamma-butyrobetaine are able to dissociate completely
CC from their primary site into the cytoplasm (PubMed:22843728). Substrate
CC molecules initially located at the secondary sites dissociate even
CC faster into the extra- or intracellular regions (PubMed:22843728).
CC {ECO:0000269|PubMed:20357772, ECO:0000269|PubMed:20829798,
CC ECO:0000269|PubMed:22843728}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:12163501}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family. CaiT
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000305}.
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DR EMBL; X73904; CAA52110.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73151.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96609.2; -; Genomic_DNA.
DR EMBL; AY625104; AAT42458.1; -; Genomic_DNA.
DR PIR; H64724; H64724.
DR RefSeq; NP_414582.1; NC_000913.3.
DR RefSeq; WP_000787103.1; NZ_STEB01000010.1.
DR PDB; 2WSX; X-ray; 3.50 A; A/B/C=1-504.
DR PDB; 3HFX; X-ray; 3.15 A; A=1-504.
DR PDBsum; 2WSX; -.
DR PDBsum; 3HFX; -.
DR AlphaFoldDB; P31553; -.
DR SMR; P31553; -.
DR BioGRID; 4260766; 345.
DR DIP; DIP-9247N; -.
DR STRING; 511145.b0040; -.
DR TCDB; 2.A.15.2.1; the betaine/carnitine/choline transporter (bcct) family.
DR PaxDb; P31553; -.
DR PRIDE; P31553; -.
DR EnsemblBacteria; AAC73151; AAC73151; b0040.
DR EnsemblBacteria; BAB96609; BAB96609; BAB96609.
DR GeneID; 944765; -.
DR KEGG; ecj:JW0039; -.
DR KEGG; eco:b0040; -.
DR PATRIC; fig|1411691.4.peg.2243; -.
DR EchoBASE; EB1522; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_6_0_6; -.
DR InParanoid; P31553; -.
DR OMA; AWAPFTG; -.
DR PhylomeDB; P31553; -.
DR BioCyc; EcoCyc:CAIT-MON; -.
DR BioCyc; MetaCyc:CAIT-MON; -.
DR UniPathway; UPA00117; -.
DR EvolutionaryTrace; P31553; -.
DR PRO; PR:P31553; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0044667; F:(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity; IEA:InterPro.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1900751; P:4-(trimethylammonio)butanoate transport; IEA:InterPro.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015879; P:carnitine transport; IDA:EcoCyc.
DR HAMAP; MF_01049; CaiT; 1.
DR InterPro; IPR018093; BCCT_CS.
DR InterPro; IPR000060; BCCT_transptr.
DR InterPro; IPR023449; BCCT_transptr_CaiT.
DR PANTHER; PTHR30047; PTHR30047; 1.
DR Pfam; PF02028; BCCT; 1.
DR TIGRFAMs; TIGR00842; bcct; 1.
DR PROSITE; PS01303; BCCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiport; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..504
FT /note="L-carnitine/gamma-butyrobetaine antiporter"
FT /id="PRO_0000201486"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 13..30
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 31..51
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 52..67
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 68..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 91..98
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 99..131
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 132..151
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 152..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 187..219
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 220..230
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 231..248
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 249..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 254..277
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 278..311
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 312..335
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 336..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 350..372
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 373..403
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 404..431
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 432..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 447..466
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 467..468
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TRANSMEM 469..490
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT TOPO_DOM 491..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT BINDING 114
FT /ligand="4-(trimethylamino)butanoate"
FT /ligand_id="ChEBI:CHEBI:16244"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20829798,
FT ECO:0007744|PDB:2WSX"
FT BINDING 142
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT BINDING 315..316
FT /ligand="4-(trimethylamino)butanoate"
FT /ligand_id="ChEBI:CHEBI:16244"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20829798,
FT ECO:0007744|PDB:2WSX"
FT BINDING 323..324
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT BINDING 323
FT /ligand="4-(trimethylamino)butanoate"
FT /ligand_id="ChEBI:CHEBI:16244"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20829798,
FT ECO:0007744|PDB:2WSX"
FT BINDING 327..330
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20357772,
FT ECO:0007744|PDB:3HFX"
FT BINDING 331
FT /ligand="4-(trimethylamino)butanoate"
FT /ligand_id="ChEBI:CHEBI:16244"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20829798,
FT ECO:0007744|PDB:2WSX"
FT VARIANT 353
FT /note="L -> M (in strain: O44:K74)"
FT VARIANT 374
FT /note="I -> M (in strain: B)"
FT MUTAGEN 114
FT /note="Y->L: Small decrease in transport activity."
FT /evidence="ECO:0000269|PubMed:20357772"
FT MUTAGEN 288
FT /note="D->A: Retains 70% of transport activity. Forms
FT mostly monomers."
FT /evidence="ECO:0000269|PubMed:30846799"
FT MUTAGEN 288
FT /note="D->R: Abolishes transport activity. Forms mostly
FT monomers."
FT /evidence="ECO:0000269|PubMed:30846799"
FT MUTAGEN 288
FT /note="D->W: Retains 4% of transport activity. Forms mostly
FT monomers."
FT /evidence="ECO:0000269|PubMed:30846799"
FT MUTAGEN 295
FT /note="M->E: Does not affect transport activity. Forms
FT mostly monomers. Can also form small amounts of homodimers
FT and homotrimers."
FT /evidence="ECO:0000269|PubMed:30846799"
FT MUTAGEN 299
FT /note="R->A: Does not affect transport activity. Forms
FT mostly monomers. Can also form small amounts of homodimers
FT and homotrimers. Shows a high tendency to aggregate."
FT /evidence="ECO:0000269|PubMed:30846799"
FT MUTAGEN 304
FT /note="T->A: Does not affect transport activity. Forms
FT mostly monomers. Shows a high tendency to aggregate."
FT /evidence="ECO:0000269|PubMed:30846799"
FT MUTAGEN 316
FT /note="W->L: Decrease in transport activity."
FT /evidence="ECO:0000269|PubMed:20357772"
FT MUTAGEN 323
FT /note="W->L: Abolishes transport activity."
FT /evidence="ECO:0000269|PubMed:20357772"
FT MUTAGEN 324
FT /note="W->L: Abolishes transport activity."
FT /evidence="ECO:0000269|PubMed:20357772"
FT MUTAGEN 327
FT /note="Y->L: Strong decrease in transport activity."
FT /evidence="ECO:0000269|PubMed:20357772"
FT MUTAGEN 330
FT /note="Q->L: Decrease in transport activity."
FT /evidence="ECO:0000269|PubMed:20357772"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:3HFX"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 33..71
FT /evidence="ECO:0007829|PDB:3HFX"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3HFX"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:3HFX"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2WSX"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 144..162
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:3HFX"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 188..219
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 229..247
FT /evidence="ECO:0007829|PDB:3HFX"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:2WSX"
FT HELIX 255..301
FT /evidence="ECO:0007829|PDB:3HFX"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:2WSX"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:3HFX"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:2WSX"
FT HELIX 344..375
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:3HFX"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 406..432
FT /evidence="ECO:0007829|PDB:3HFX"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 447..466
FT /evidence="ECO:0007829|PDB:3HFX"
FT HELIX 470..500
FT /evidence="ECO:0007829|PDB:3HFX"
SQ SEQUENCE 504 AA; 56587 MW; A852310DBEA22D82 CRC64;
MKNEKRKTGI EPKVFFPPLI IVGILCWLTV RDLDAANVVI NAVFSYVTNV WGWAFEWYMV
VMLFGWFWLV FGPYAKKRLG NEPPEFSTAS WIFMMFASCT SAAVLFWGSI EIYYYISTPP
FGLEPNSTGA KELGLAYSLF HWGPLPWATY SFLSVAFAYF FFVRKMEVIR PSSTLVPLVG
EKHAKGLFGT IVDNFYLVAL IFAMGTSLGL ATPLVTECMQ WLFGIPHTLQ LDAIIITCWI
ILNAICVACG LQKGVRIASD VRSYLSFLML GWVFIVSGAS FIMNYFTDSV GMLLMYLPRM
LFYTDPIAKG GFPQGWTVFY WAWWVIYAIQ MSIFLARISR GRTVRELCFG MVLGLTASTW
ILWTVLGSNT LLLIDKNIIN IPNLIEQYGV ARAIIETWAA LPLSTATMWG FFILCFIATV
TLVNACSYTL AMSTCREVRD GEEPPLLVRI GWSILVGIIG IVLLALGGLK PIQTAIIAGG
CPLFFVNIMV TLSFIKDAKQ NWKD
