MALK_ECOLI
ID MALK_ECOLI Reviewed; 371 AA.
AC P68187; P02914; Q2M6R9; Q47348;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Maltose/maltodextrin import ATP-binding protein MalK {ECO:0000255|HAMAP-Rule:MF_01709};
DE EC=7.5.2.1 {ECO:0000255|HAMAP-Rule:MF_01709, ECO:0000269|PubMed:2026607, ECO:0000269|PubMed:2155217};
GN Name=malK {ECO:0000255|HAMAP-Rule:MF_01709, ECO:0000303|PubMed:6296778};
GN OrderedLocusNames=b4035, JW3995;
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=K12;
RX PubMed=6296778; DOI=10.1093/nar/10.22.7449;
RA Gilson E., Nikaido H., Hofnung M.;
RT "Sequence of the malK gene in E.coli K12.";
RL Nucleic Acids Res. 10:7449-7458(1982).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=2674653; DOI=10.1007/bf00331269;
RA Dahl M.K., Francoz E., Saurin W., Boos W., Manson M.D., Hofnung M.;
RT "Comparison of sequences from the malB regions of Salmonella typhimurium
RT and Enterobacter aerogenes with Escherichia coli K12: a potential new
RT regulatory site in the interoperonic region.";
RL Mol. Gen. Genet. 218:199-207(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX PubMed=6283312; DOI=10.1007/bf00333794;
RA Bedouelle H., Hofnung M.;
RT "A DNA sequence containing the control regions of the malEFG and malK-lamB
RT operons in Escherichia coli K12.";
RL Mol. Gen. Genet. 185:82-87(1982).
RN [7]
RP CHARACTERIZATION OF MALTOSE TRANSPORT AND ATP HYDROLYSIS ACTIVITIES,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=2155217; DOI=10.1016/s0021-9258(19)39555-9;
RA Davidson A.L., Nikaido H.;
RT "Overproduction, solubilization, and reconstitution of the maltose
RT transport system from Escherichia coli.";
RL J. Biol. Chem. 265:4254-4260(1990).
RN [8]
RP REGULATION, AND MUTAGENESIS OF ALA-124; PHE-241; GLY-278 AND GLY-284.
RX PubMed=2250006; DOI=10.1016/s0021-9258(17)45318-x;
RA Dean D.A., Reizer J., Nikaido H., Saier M.H. Jr.;
RT "Regulation of the maltose transport system of Escherichia coli by the
RT glucose-specific enzyme III of the phosphoenolpyruvate-sugar
RT phosphotransferase system. Characterization of inducer exclusion-resistant
RT mutants and reconstitution of inducer exclusion in proteoliposomes.";
RL J. Biol. Chem. 265:21005-21010(1990).
RN [9]
RP PURIFICATION OF THE MALK-MALF-MALG COMPLEX AND ITS ATPASE ACTIVITY,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=2026607; DOI=10.1016/s0021-9258(18)31535-7;
RA Davidson A.L., Nikaido H.;
RT "Purification and characterization of the membrane-associated components of
RT the maltose transport system from Escherichia coli.";
RL J. Biol. Chem. 266:8946-8951(1991).
RN [10]
RP REGULATION, AND MUTAGENESIS OF GLU-119; GLY-137; ASP-158; ARG-228; TRP-267;
RP SER-282; GLY-302; SER-322 AND GLY-346.
RX PubMed=2007546; DOI=10.1128/jb.173.7.2180-2186.1991;
RA Kuehnau S., Reyes M., Sievertsen A., Shuman H.A., Boos W.;
RT "The activities of the Escherichia coli MalK protein in maltose transport,
RT regulation, and inducer exclusion can be separated by mutations.";
RL J. Bacteriol. 173:2180-2186(1991).
RN [11]
RP INTERACTION BETWEEN MALK AND MALT.
RX PubMed=9822819; DOI=10.1046/j.1365-2958.1998.01084.x;
RA Panagiotidis C.H., Boos W., Shuman H.A.;
RT "The ATP-binding cassette subunit of the maltose transporter MalK
RT antagonizes MalT, the activator of the Escherichia coli mal regulon.";
RL Mol. Microbiol. 30:535-546(1998).
RN [12]
RP MUTAGENESIS OF ALA-85 AND VAL-117.
RX PubMed=9214624; DOI=10.1093/emboj/16.11.3066;
RA Mourez M., Hofnung M., Dassa E.;
RT "Subunit interactions in ABC transporters: a conserved sequence in
RT hydrophobic membrane proteins of periplasmic permeases defines an important
RT site of interaction with the ATPase subunits.";
RL EMBO J. 16:3066-3077(1997).
RN [13]
RP MUTAGENESIS OF LYS-106 AND VAL-114.
RX PubMed=10809785; DOI=10.1074/jbc.275.20.15526;
RA Hunke S., Mourez M., Jehanno M., Dassa E., Schneider E.;
RT "ATP modulates subunit-subunit interactions in an ATP-binding cassette
RT transporter (MalFGK2) determined by site-directed chemical cross-linking.";
RL J. Biol. Chem. 275:15526-15534(2000).
RN [14]
RP MUTAGENESIS OF GLU-308; GLY-340 AND PHE-355, AND MODELING.
RX PubMed=11709552; DOI=10.1074/jbc.m107905200;
RA Boehm A., Diez J., Diederichs K., Welte W., Boos W.;
RT "Structural model of MalK, the ABC subunit of the maltose transporter of
RT Escherichia coli: implications for mal gene regulation, inducer exclusion,
RT and subunit assembly.";
RL J. Biol. Chem. 277:3708-3717(2002).
RN [15]
RP 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 [16]
RP SUBUNIT, SUBCELLULAR LOCATION, AND REQUIREMENT FOR YIDC FOR PROTEIN AND
RP COMPLEX FORMATION.
RX PubMed=18456666; DOI=10.1074/jbc.m801481200;
RA Wagner S., Pop O.I., Haan G.J., Baars L., Koningstein G., Klepsch M.M.,
RA Genevaux P., Luirink J., de Gier J.W.;
RT "Biogenesis of MalF and the MalFGK(2) maltose transport complex in
RT Escherichia coli requires YidC.";
RL J. Biol. Chem. 283:17881-17890(2008).
RN [17]
RP REVIEW.
RX PubMed=9529892; DOI=10.1128/mmbr.62.1.204-229.1998;
RA Boos W., Shuman H.;
RT "Maltose/maltodextrin system of Escherichia coli: transport, metabolism,
RT and regulation.";
RL Microbiol. Mol. Biol. Rev. 62:204-229(1998).
RN [18]
RP REVIEW.
RA Schneider E.;
RT "Import of solutes by ABC transporters - The maltose and other systems.";
RL (In) Holland I.B., Cole S.P.C., Kuchler K., Higgins C.F. (eds.);
RL ABC proteins from bacteria to man, pp.157-185, Academic Press, San Diego.
RL (2003).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=14527411; DOI=10.1016/j.molcel.2003.08.004;
RA Chen J., Lu G., Lin J., Davidson A.L., Quiocho F.A.;
RT "A tweezers-like motion of the ATP-binding cassette dimer in an ABC
RT transport cycle.";
RL Mol. Cell 12:651-661(2003).
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC maltose/maltodextrin import. Responsible for energy coupling to the
CC transport system. {ECO:0000269|PubMed:2026607,
CC ECO:0000269|PubMed:2155217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-maltose(out) + H2O = ADP + D-maltose(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:22132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17306, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.5.2.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01709,
CC ECO:0000269|PubMed:2026607, ECO:0000269|PubMed:2155217};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MalK),
CC two transmembrane proteins (MalG and MalF) and a solute-binding protein
CC (MalE). Protein stability and stable complex formation require YidC.
CC {ECO:0000269|PubMed:18456666, ECO:0000269|PubMed:2026607,
CC ECO:0000269|PubMed:2155217}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01709, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:18456666}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01709, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:18456666}.
CC -!- MISCELLANEOUS: Target for inducer exclusion, mediated by the
CC unphosphorylated enzyme III of the phosphotransferase system for
CC glucose and resulting in the inhibition of maltose transport.
CC {ECO:0000269|PubMed:2250006}.
CC -!- MISCELLANEOUS: Acts as a repressor of mal genes. In absence of maltose,
CC the C-terminus of MalK interacts with MalT, then MalT becomes inactive
CC and the mal genes are not activated. In presence of maltose, MalK is
CC tightly associated with the MalFG complex and has no affinity for MalT.
CC {ECO:0000269|PubMed:9822819}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC Maltooligosaccharide importer (TC 3.A.1.1.1) family.
CC {ECO:0000255|HAMAP-Rule:MF_01709}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23582.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J01648; AAB59057.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43129.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77005.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78037.1; -; Genomic_DNA.
DR EMBL; V00303; CAA23582.1; ALT_INIT; Genomic_DNA.
DR PIR; B65211; MMECMK.
DR RefSeq; NP_418459.1; NC_000913.3.
DR RefSeq; WP_000179165.1; NZ_STEB01000022.1.
DR PDB; 1Q12; X-ray; 2.60 A; A/B/C/D=1-371.
DR PDB; 1Q1B; X-ray; 2.80 A; A/B/C/D=1-371.
DR PDB; 1Q1E; X-ray; 2.90 A; A/B=1-371.
DR PDB; 2AWN; X-ray; 2.30 A; A/B/C/D=1-371.
DR PDB; 2AWO; X-ray; 2.80 A; A/B/C/D=1-371.
DR PDB; 2R6G; X-ray; 2.80 A; A/B=1-371.
DR PDB; 3FH6; X-ray; 4.50 A; A/B/C/D=1-371.
DR PDB; 3GD7; X-ray; 2.70 A; A/B/C/D=219-371.
DR PDB; 3PUV; X-ray; 2.40 A; A/B=1-371.
DR PDB; 3PUW; X-ray; 2.30 A; A/B=1-371.
DR PDB; 3PUX; X-ray; 2.30 A; A/B=1-371.
DR PDB; 3PUY; X-ray; 3.10 A; A/B=1-371.
DR PDB; 3PUZ; X-ray; 2.90 A; A/B=1-371.
DR PDB; 3PV0; X-ray; 3.10 A; A/B=1-371.
DR PDB; 3RLF; X-ray; 2.20 A; A/B=1-371.
DR PDB; 4JBW; X-ray; 3.91 A; A/B/C/D=1-371.
DR PDB; 4KI0; X-ray; 2.38 A; A/B=1-371.
DR PDBsum; 1Q12; -.
DR PDBsum; 1Q1B; -.
DR PDBsum; 1Q1E; -.
DR PDBsum; 2AWN; -.
DR PDBsum; 2AWO; -.
DR PDBsum; 2R6G; -.
DR PDBsum; 3FH6; -.
DR PDBsum; 3GD7; -.
DR PDBsum; 3PUV; -.
DR PDBsum; 3PUW; -.
DR PDBsum; 3PUX; -.
DR PDBsum; 3PUY; -.
DR PDBsum; 3PUZ; -.
DR PDBsum; 3PV0; -.
DR PDBsum; 3RLF; -.
DR PDBsum; 4JBW; -.
DR PDBsum; 4KI0; -.
DR AlphaFoldDB; P68187; -.
DR SMR; P68187; -.
DR BioGRID; 4262662; 20.
DR ComplexPortal; CPX-1932; Maltose ABC transporter complex.
DR ComplexPortal; CPX-1978; Enzyme IIA-maltose transport inhibitory complex.
DR DIP; DIP-47850N; -.
DR IntAct; P68187; 8.
DR STRING; 511145.b4035; -.
DR MoonProt; P68187; -.
DR TCDB; 3.A.1.1.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P68187; -.
DR PaxDb; P68187; -.
DR PRIDE; P68187; -.
DR EnsemblBacteria; AAC77005; AAC77005; b4035.
DR EnsemblBacteria; BAE78037; BAE78037; BAE78037.
DR GeneID; 66672050; -.
DR GeneID; 948537; -.
DR KEGG; ecj:JW3995; -.
DR KEGG; eco:b4035; -.
DR PATRIC; fig|511145.12.peg.4150; -.
DR EchoBASE; EB0553; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_6; -.
DR InParanoid; P68187; -.
DR OMA; SPKAFLM; -.
DR PhylomeDB; P68187; -.
DR BioCyc; EcoCyc:MALK-MON; -.
DR BioCyc; MetaCyc:MALK-MON; -.
DR BRENDA; 7.5.2.1; 2026.
DR EvolutionaryTrace; P68187; -.
DR PRO; PR:P68187; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR GO; GO:1990154; C:enzyme IIA-maltose transporter complex; IPI:ComplexPortal.
DR GO; GO:1990060; C:maltose transport complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0015768; P:maltose transport; IDA:EcoCyc.
DR GO; GO:1902344; P:negative regulation of maltose transport; IC:ComplexPortal.
DR GO; GO:0034763; P:negative regulation of transmembrane transport; IC:ComplexPortal.
DR CDD; cd03301; ABC_MalK_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015855; ABC_transpr_MalK-like.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR040582; OB_MalK.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17912; OB_MalK; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51245; MALK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Sugar transport; Translocase;
KW Transport.
FT CHAIN 1..371
FT /note="Maltose/maltodextrin import ATP-binding protein
FT MalK"
FT /id="PRO_0000092475"
FT DOMAIN 4..234
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01709"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01709"
FT MUTAGEN 85
FT /note="A->M: Suppressor of EAA loop mutations in MalFG."
FT /evidence="ECO:0000269|PubMed:9214624"
FT MUTAGEN 106
FT /note="K->C: Suppressor of EAA loop mutations in MalFG."
FT /evidence="ECO:0000269|PubMed:10809785"
FT MUTAGEN 114
FT /note="V->C: Suppressor of EAA loop mutations in MalFG."
FT /evidence="ECO:0000269|PubMed:10809785"
FT MUTAGEN 117
FT /note="V->M: Suppressor of EAA loop mutations in MalFG."
FT /evidence="ECO:0000269|PubMed:9214624"
FT MUTAGEN 119
FT /note="E->K: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 124
FT /note="A->T: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2250006"
FT MUTAGEN 137
FT /note="G->A: Loss of maltose transport. Has greater ability
FT to decrease mal gene expression than wild-type MalK."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 158
FT /note="D->N: Loss of maltose transport but retains ability
FT to repress mal genes."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 228
FT /note="R->C: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 241
FT /note="F->I: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2250006"
FT MUTAGEN 267
FT /note="W->G: Normal maltose transport but constitutive mal
FT gene expression."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 278
FT /note="G->P: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2250006"
FT MUTAGEN 282
FT /note="S->L: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 284
FT /note="G->S: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2250006"
FT MUTAGEN 302
FT /note="G->D: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 308
FT /note="E->Q: Maltose transport is affected but retains
FT ability to interact with MalT."
FT /evidence="ECO:0000269|PubMed:11709552"
FT MUTAGEN 322
FT /note="S->F: Resistant to inhibitory effects of alpha-
FT methylglucoside but retains transport capacity."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 340
FT /note="G->A: Maltose transport is affected but retains
FT ability to interact with MalT."
FT /evidence="ECO:0000269|PubMed:11709552"
FT MUTAGEN 346
FT /note="G->S: Normal maltose transport but constitutive mal
FT gene expression."
FT /evidence="ECO:0000269|PubMed:2007546"
FT MUTAGEN 355
FT /note="F->Y: Maltose transport is affected but retains
FT ability to interact with MalT."
FT /evidence="ECO:0000269|PubMed:11709552"
FT CONFLICT 220..241
FT /note="ELYHYPADRFVAGFIGSPKMNF -> AVPLSGRPFCRRIYRFAKDEL (in
FT Ref. 1; AAB59057)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 16..26
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1Q12"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:3PV0"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1Q1E"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 166..183
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:1Q1B"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 297..309
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2AWN"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:3RLF"
SQ SEQUENCE 371 AA; 40990 MW; 240D58F59450F30E CRC64;
MASVQLQNVT KAWGEVVVSK DINLDIHEGE FVVFVGPSGC GKSTLLRMIA GLETITSGDL
FIGEKRMNDT PPAERGVGMV FQSYALYPHL SVAENMSFGL KLAGAKKEVI NQRVNQVAEV
LQLAHLLDRK PKALSGGQRQ RVAIGRTLVA EPSVFLLDEP LSNLDAALRV QMRIEISRLH
KRLGRTMIYV THDQVEAMTL ADKIVVLDAG RVAQVGKPLE LYHYPADRFV AGFIGSPKMN
FLPVKVTATA IDQVQVELPM PNRQQVWLPV ESRDVQVGAN MSLGIRPEHL LPSDIADVIL
EGEVQVVEQL GNETQIHIQI PSIRQNLVYR QNDVVLVEEG ATFAIGLPPE RCHLFREDGT
ACRRLHKEPG V
