MALE_THELN
ID MALE_THELN Reviewed; 450 AA.
AC Q7LYW7; H3ZP67;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Trehalose/maltose-binding protein MalE;
DE Short=TMBP;
DE Flags: Precursor;
GN Name=malE; ORFNames=OCC_03562;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=9457875; DOI=10.1128/jb.180.3.680-689.1998;
RA Horlacher R., Xavier K.B., Santos H., DiRuggiero J., Kossmann M., Boos W.;
RT "Archaeal binding protein-dependent ABC transporter: molecular and
RT biochemical analysis of the trehalose/maltose transport system of the
RT hyperthermophilic archaeon Thermococcus litoralis.";
RL J. Bacteriol. 180:680-689(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=11115105; DOI=10.1046/j.1365-2958.2000.02161.x;
RA Diruggiero J., Dunn D., Maeder D.L., Holley-Shanks R., Chatard J.,
RA Horlacher R., Robb F.T., Boos W., Weiss R.B.;
RT "Evidence of recent lateral gene transfer among hyperthermophilic
RT archaea.";
RL Mol. Microbiol. 38:684-693(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=8759837; DOI=10.1128/jb.178.16.4773-4777.1996;
RA Xavier K.B., Martins L.O., Peist R., Kossmann M., Boos W., Santos H.;
RT "High-affinity maltose/trehalose transport system in the hyperthermophilic
RT archaeon Thermococcus litoralis.";
RL J. Bacteriol. 178:4773-4777(1996).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=11453995; DOI=10.1046/j.1432-1327.2001.02313.x;
RA Greller G., Riek R., Boos W.;
RT "Purification and characterization of the heterologously expressed
RT trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon
RT Thermococcus litoralis.";
RL Eur. J. Biochem. 268:4011-4018(2001).
RN [6]
RP FUNCTION.
RX PubMed=16532450; DOI=10.1002/prot.20952;
RA Herman P., Staiano M., Marabotti A., Varriale A., Scire A., Tanfani F.,
RA Vecer J., Rossi M., D'Auria S.;
RT "D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon
RT Thermococcus litoralis: the binding of trehalose and maltose results in
RT different protein conformational states.";
RL Proteins 63:754-767(2006).
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC trehalose/maltose import. Binds maltose and trehalose.
CC {ECO:0000269|PubMed:11453995, ECO:0000269|PubMed:16532450,
CC ECO:0000269|PubMed:8759837, ECO:0000269|PubMed:9457875}.
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). {ECO:0000269|PubMed:11453995}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11453995,
CC ECO:0000305|PubMed:9457875}; Lipid-anchor {ECO:0000305|PubMed:11453995,
CC ECO:0000305|PubMed:9457875}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11453995}.
CC -!- MISCELLANEOUS: The protein assumes different conformations with
CC different physical properties depending whether maltose or trehalose is
CC bound to the protein. {ECO:0000305|PubMed:16532450}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AF012836; AAC38136.1; -; Genomic_DNA.
DR EMBL; AF307053; AAG45388.1; -; Genomic_DNA.
DR EMBL; CP006670; EHR78234.1; -; Genomic_DNA.
DR RefSeq; WP_004068724.1; NC_022084.1.
DR PDB; 1EU8; X-ray; 1.90 A; A=45-450.
DR PDBsum; 1EU8; -.
DR AlphaFoldDB; Q7LYW7; -.
DR SMR; Q7LYW7; -.
DR STRING; 523849.OCC_03562; -.
DR EnsemblBacteria; EHR78234; EHR78234; OCC_03562.
DR GeneID; 16548949; -.
DR KEGG; tlt:OCC_03562; -.
DR HOGENOM; CLU_031285_9_1_2; -.
DR OMA; PFWANTQ; -.
DR OrthoDB; 14861at2157; -.
DR Proteomes; UP000015502; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR006059; SBP.
DR Pfam; PF01547; SBP_bac_1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; Lipoprotein; Membrane; Signal;
KW Sugar transport; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 25..450
FT /note="Trehalose/maltose-binding protein MalE"
FT /id="PRO_0000421288"
FT CONFLICT 219
FT /note="S -> G (in Ref. 1; AAC38136 and 2; AAG45388)"
FT /evidence="ECO:0000305"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1EU8"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1EU8"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:1EU8"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:1EU8"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1EU8"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:1EU8"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:1EU8"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 382..387
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 395..399
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 410..425
FT /evidence="ECO:0007829|PDB:1EU8"
FT HELIX 431..446
FT /evidence="ECO:0007829|PDB:1EU8"
SQ SEQUENCE 450 AA; 50421 MW; 48386C9DC402075B CRC64;
MNVKKVLLGL FLVGVLGIAV VASGCIGGQQ TSTVTSTPTE TSLQGKIVFA VGGAPNEIEY
WKGVIAEFEK KYPGVTVELK RQATDTEQRR LDLVNALRGK SSDPDVFLMD VAWLGQFIAS
GWLEPLDDYV QKDNYDLSVF FQSVINLADK QGGKLYALPV YIDAGLLYYR KDLLEKYGYS
KPPETWQELV EMAQKIQSGE RETNPNFWGF VWQGKQYESL VCDFVEYVYS NGGSLGEFKD
GKWVPTLNKP ENVEALQFMV DLIHKYKISP PNTYTEMTEE PVRLMFQQGN AAFERNWPYA
WGLHNADDSP VKGKVGVAPL PHFPGHKSAA TLGGWHIGIS KYSDNKALAW EFVKFVESYS
VQKGFAMNLG WNPGRVDVYD DPAVVSKSPH LKELRAVFEN AVPRPIVPYY PQLSEIIQKY
VNSALAGKIS PQEALDKAQK EAEELVKQYS
