GADC_ECOLI
ID GADC_ECOLI Reviewed; 511 AA.
AC P63235; P39183; P76131; P77384; Q54152;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glutamate/gamma-aminobutyrate antiporter {ECO:0000305};
DE Short=Glu/GABA antiporter {ECO:0000303|PubMed:23589309};
DE AltName: Full=Extreme acid sensitivity protein;
GN Name=gadC {ECO:0000303|PubMed:8682809};
GN Synonyms=acsA, xasA {ECO:0000303|PubMed:8682809};
GN OrderedLocusNames=b1492, JW1487;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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], AND SEQUENCE REVISION.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-490, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8682809; DOI=10.1128/jb.178.13.3978-3981.1996;
RA Hersh B.M., Farooq F.T., Barstad D.N., Blankenhorn D.L., Slonczewski J.L.;
RT "A glutamate-dependent acid resistance gene in Escherichia coli.";
RL J. Bacteriol. 178:3978-3981(1996).
RN [5]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 11246;
RX PubMed=10383761; DOI=10.1046/j.1365-2958.1999.01430.x;
RA De Biase D., Tramonti A., Bossa F., Visca P.;
RT "The response to stationary-phase stress conditions in Escherichia coli:
RT role and regulation of the glutamic acid decarboxylase system.";
RL Mol. Microbiol. 32:1198-1211(1999).
RN [6]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 11246;
RX PubMed=11976288; DOI=10.1128/jb.184.10.2603-2613.2002;
RA Tramonti A., Visca P., De Canio M., Falconi M., De Biase D.;
RT "Functional characterization and regulation of gadX, a gene encoding an
RT AraC/XylS-like transcriptional activator of the Escherichia coli glutamic
RT acid decarboxylase system.";
RL J. Bacteriol. 184:2603-2613(2002).
RN [7]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12399493; DOI=10.1128/jb.184.22.6225-6234.2002;
RA Masuda N., Church G.M.;
RT "Escherichia coli gene expression responsive to levels of the response
RT regulator EvgA.";
RL J. Bacteriol. 184:6225-6234(2002).
RN [8]
RP ACTIVITY REGULATION, AND INHIBITION BY L-PDC.
RC STRAIN=K12;
RX PubMed=12855178; DOI=10.1016/s0378-1097(03)00427-0;
RA Waterman S.R., Small P.L.C.;
RT "The glutamate-dependent acid resistance system of Escherichia coli and
RT Shigella flexneri is inhibited in vitro by L-trans-pyrrolidine-2,4-
RT dicarboxylic acid.";
RL FEMS Microbiol. Lett. 224:119-125(2003).
RN [9]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=12867478; DOI=10.1128/jb.185.15.4644-4647.2003;
RA Waterman S.R., Small P.L.C.;
RT "Transcriptional expression of Escherichia coli glutamate-dependent acid
RT resistance genes gadA and gadBC in an hns rpoS mutant.";
RL J. Bacteriol. 185:4644-4647(2003).
RN [10]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12694615; DOI=10.1046/j.1365-2958.2003.03477.x;
RA Masuda N., Church G.M.;
RT "Regulatory network of acid resistance genes in Escherichia coli.";
RL Mol. Microbiol. 48:699-712(2003).
RN [11]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12;
RX PubMed=12940989; DOI=10.1046/j.1365-2958.2003.03633.x;
RA Ma Z., Gong S., Richard H., Tucker D.L., Conway T., Foster J.W.;
RT "GadE (YhiE) activates glutamate decarboxylase-dependent acid resistance in
RT Escherichia coli K-12.";
RL Mol. Microbiol. 49:1309-1320(2003).
RN [12]
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 [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, AND MUTAGENESIS
RP OF 471-GLY--HIS-511.
RX PubMed=23589309; DOI=10.1074/jbc.m113.474502;
RA Ma D., Lu P., Shi Y.;
RT "Substrate selectivity of the acid-activated glutamate/gamma-aminobutyric
RT acid (GABA) antiporter GadC from Escherichia coli.";
RL J. Biol. Chem. 288:15148-15153(2013).
RN [14]
RP FUNCTION.
RX PubMed=30498489; DOI=10.3389/fmicb.2018.02869;
RA Pennacchietti E., D'Alonzo C., Freddi L., Occhialini A., De Biase D.;
RT "The glutaminase-dependent acid resistance system: qualitative and
RT quantitative assays and analysis of its distribution in enteric bacteria.";
RL Front. Microbiol. 9:2869-2869(2018).
RN [15] {ECO:0007744|PDB:4DJI, ECO:0007744|PDB:4DJK}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF MET-25; TYR-30; LEU-212;
RP GLU-218; GLU-304; TRP-308; TYR-378; TYR-382; 471-GLY--HIS-511; HIS-491;
RP ARG-497; ARG-499; HIS-502 AND TYR-503.
RX PubMed=22407317; DOI=10.1038/nature10917;
RA Ma D., Lu P., Yan C., Fan C., Yin P., Wang J., Shi Y.;
RT "Structure and mechanism of a glutamate-GABA antiporter.";
RL Nature 483:632-636(2012).
CC -!- FUNCTION: Involved in glutaminase-dependent acid resistance
CC (PubMed:8682809, PubMed:30498489). Exchanges extracellular glutamate
CC (Glu) for intracellular gamma-aminobutyric acid (GABA) under acidic
CC conditions (PubMed:22407317, PubMed:23589309). The protonation states
CC of substrates are crucial for transport. Selectively transports Glu
CC with no net charge and GABA with a positive charge (PubMed:23589309).
CC Also efficiently transports glutamine and, to a smaller extent,
CC methionine and leucine (PubMed:22407317). When the extracellular pH
CC drops below 2.5, can import L-glutamine and export either glutamate or
CC GABA (PubMed:30498489). The ability to survive the extremely acidic
CC conditions of the stomach is essential for successful colonization of
CC the host by commensal and pathogenic bacteria (PubMed:8682809,
CC PubMed:30498489). {ECO:0000269|PubMed:22407317,
CC ECO:0000269|PubMed:23589309, ECO:0000269|PubMed:30498489,
CC ECO:0000269|PubMed:8682809, ECO:0000305|PubMed:30498489,
CC ECO:0000305|PubMed:8682809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(in) + L-glutamate(out) = 4-
CC aminobutanoate(out) + L-glutamate(in); Xref=Rhea:RHEA:28919,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888;
CC Evidence={ECO:0000269|PubMed:22407317, ECO:0000269|PubMed:23589309};
CC -!- ACTIVITY REGULATION: Shows pH-dependent activity (PubMed:22407317,
CC PubMed:23589309). The Glu/GABA transport activity is robust at pH 4.5
CC and rapidly decreases with increasing pH, with no detectable activity
CC at pH 6.5 or above (PubMed:22407317, PubMed:23589309). The Glu analog
CC L-trans-pyrrolidine-2,4-dicarboxylic acid (L-PDC) blocks the uptake of
CC glutamate by selective inhibition (PubMed:12855178).
CC {ECO:0000269|PubMed:12855178, ECO:0000269|PubMed:22407317,
CC ECO:0000269|PubMed:23589309}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=146.6 uM for L-glutamate (at pH 5) {ECO:0000269|PubMed:22407317};
CC KM=85.3 uM for L-glutamate (at pH 5.5) {ECO:0000269|PubMed:22407317};
CC KM=92 uM for L-glutamate (at pH 6) {ECO:0000269|PubMed:22407317};
CC KM=203.3 uM for L-glutamine (at pH 5.5)
CC {ECO:0000269|PubMed:22407317};
CC KM=202.4 uM for GABA (at pH 5.5) {ECO:0000269|PubMed:22407317};
CC Vmax=666 nmol/min/mg enzyme with L-glutamate as substrate (at pH 5)
CC {ECO:0000269|PubMed:22407317};
CC Vmax=112 nmol/min/mg enzyme with L-glutamate as substrate (at pH 5.5)
CC {ECO:0000269|PubMed:22407317};
CC Vmax=14.8 nmol/min/mg enzyme with L-glutamate as substrate (at pH 6)
CC {ECO:0000269|PubMed:22407317};
CC Vmax=280 nmol/min/mg enzyme with L-glutamine as substrate (at pH 5.5)
CC {ECO:0000269|PubMed:22407317};
CC Vmax=88.4 nmol/min/mg enzyme with GABA as substrate (at pH 5.5)
CC {ECO:0000269|PubMed:22407317};
CC pH dependence:
CC Inactive at pH 6.5 or above. {ECO:0000269|PubMed:22407317};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22407317}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:22407317}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22407317}.
CC -!- INDUCTION: By acidic conditions. Expression is regulated by a complex
CC system involving RpoS, cAMP, CRP, EvgAS, H-NS, GadE, GadW and GadX. The
CC level of involvement for each regulator varies depending upon the
CC growth phase and the medium. {ECO:0000269|PubMed:10383761,
CC ECO:0000269|PubMed:11976288, ECO:0000269|PubMed:12399493,
CC ECO:0000269|PubMed:12694615, ECO:0000269|PubMed:12867478,
CC ECO:0000269|PubMed:12940989}.
CC -!- DOMAIN: Contains a unique C-terminal C-plug that plays an important
CC role in substrate transport. The C-plug forms a folded domain and
CC completely blocks the path to the putative substrate-binding site.
CC Under neutral or basic pH, the C-plug probably remains closed and
CC prevents substrate transport (PubMed:22407317, PubMed:23589309). At
CC acidic pH, the C-plug may be displaced, allowing influx of Glu and
CC efflux of GABA (PubMed:23589309). {ECO:0000269|PubMed:22407317,
CC ECO:0000269|PubMed:23589309}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows a 10-fold decrease in resistance
CC with glutamate. {ECO:0000269|PubMed:8682809}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Glutamate:GABA antiporter (GGA) (TC 2.A.3.7) family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74565.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15156.2; -; Genomic_DNA.
DR EMBL; U13204; AAB17694.1; -; Genomic_DNA.
DR PIR; G64902; G64902.
DR RefSeq; NP_416009.1; NC_000913.3.
DR RefSeq; WP_000246019.1; NZ_STEB01000054.1.
DR PDB; 4DJI; X-ray; 3.19 A; A/B=1-511.
DR PDB; 4DJK; X-ray; 3.10 A; A/B=1-511.
DR PDBsum; 4DJI; -.
DR PDBsum; 4DJK; -.
DR AlphaFoldDB; P63235; -.
DR SMR; P63235; -.
DR BioGRID; 4260789; 37.
DR DIP; DIP-48121N; -.
DR STRING; 511145.b1492; -.
DR jPOST; P63235; -.
DR PaxDb; P63235; -.
DR PRIDE; P63235; -.
DR EnsemblBacteria; AAC74565; AAC74565; b1492.
DR EnsemblBacteria; BAA15156; BAA15156; BAA15156.
DR GeneID; 66674656; -.
DR GeneID; 946057; -.
DR KEGG; ecj:JW1487; -.
DR KEGG; eco:b1492; -.
DR PATRIC; fig|1411691.4.peg.775; -.
DR EchoBASE; EB2350; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_020854_4_0_6; -.
DR InParanoid; P63235; -.
DR OMA; RIEPSRW; -.
DR PhylomeDB; P63235; -.
DR BioCyc; EcoCyc:XASA-MON; -.
DR BioCyc; MetaCyc:XASA-MON; -.
DR PRO; PR:P63235; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015297; F:antiporter activity; ISS:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0051454; P:intracellular pH elevation; IMP:EcoCyc.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004759; Glu_antiport.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00910; 2A0307_GadC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Antiport; Cell inner membrane;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..511
FT /note="Glutamate/gamma-aminobutyrate antiporter"
FT /id="PRO_0000213040"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 14..36
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 37..40
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 41..64
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 65..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 86..112
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 113..126
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 148..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 152..180
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 181..201
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 202..225
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 226..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 230..259
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 260..288
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 289..322
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 323..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 360..362
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 363..396
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 397..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 431..443
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TRANSMEM 444..467
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:22407317"
FT TOPO_DOM 468..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:22407317"
FT MUTAGEN 25
FT /note="M->A: 25% decrease in substrate transport."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 30
FT /note="Y->A: At least 90% decrease in substrate transport."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 212
FT /note="L->A: 70% decrease in substrate transport."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 218
FT /note="E->A: At least 90% decrease in substrate transport."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 304
FT /note="E->A: At least 90% decrease in substrate transport."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 308
FT /note="W->A: At least 90% decrease in substrate transport."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 378
FT /note="Y->A: At least 90% decrease in substrate transport."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 382
FT /note="Y->A: At least 90% decrease in substrate transport."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 471..511
FT /note="Missing: Shifts the pH-dependent substrate transport
FT towards higher pH values. Transports Gln, but not Glu, at
FT pH 7.0 or higher."
FT /evidence="ECO:0000269|PubMed:22407317,
FT ECO:0000269|PubMed:23589309"
FT MUTAGEN 491
FT /note="H->A: Allows substrate transport at pH 6.5."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 497
FT /note="R->A: Allows substrate transport at pH 6.5."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 499
FT /note="R->A: Allows substrate transport at pH 6.5."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 502
FT /note="H->A: Allows substrate transport at pH 6.5."
FT /evidence="ECO:0000269|PubMed:22407317"
FT MUTAGEN 503
FT /note="Y->A: Allows substrate transport at pH 6.5."
FT /evidence="ECO:0000269|PubMed:22407317"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:4DJK"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4DJI"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 85..102
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:4DJK"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 129..146
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:4DJK"
FT TURN 201..206
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4DJK"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 234..257
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4DJI"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:4DJI"
FT HELIX 289..308
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 340..357
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4DJK"
FT HELIX 362..395
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4DJI"
FT HELIX 410..429
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:4DJI"
FT HELIX 445..465
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:4DJI"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:4DJI"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:4DJK"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:4DJI"
SQ SEQUENCE 511 AA; 55077 MW; 85DF72B82816CE33 CRC64;
MATSVQTGKA KQLTLLGFFA ITASMVMAVY EYPTFATSGF SLVFFLLLGG ILWFIPVGLC
AAEMATVDGW EEGGVFAWVS NTLGPRWGFA AISFGYLQIA IGFIPMLYFV LGALSYILKW
PALNEDPITK TIAALIILWA LALTQFGGTK YTARIAKVGF FAGILLPAFI LIALAAIYLH
SGAPVAIEMD SKTFFPDFSK VGTLVVFVAF ILSYMGVEAS ATHVNEMSNP GRDYPLAMLL
LMVAAICLSS VGGLSIAMVI PGNEINLSAG VMQTFTVLMS HVAPEIEWTV RVISALLLLG
VLAEIASWIV GPSRGMYVTA QKNLLPAAFA KMNKNGVPVT LVISQLVITS IALIILTNTG
GGNNMSFLIA LALTVVIYLC AYFMLFIGYI VLVLKHPDLK RTFNIPGGKG VKLVVAIVGL
LTSIMAFIVS FLPPDNIQGD STDMYVELLV VSFLVVLALP FILYAVHDRK GKANTGVTLE
PINSQNAPKG HFFLHPRARS PHYIVMNDKK H
