MALE_PYRFU
ID MALE_PYRFU Reviewed; 434 AA.
AC P58300;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Maltotriose-binding protein;
DE AltName: Full=MMBP;
DE AltName: Full=Maltodextrin-binding protein;
DE Flags: Precursor;
GN Name=malE; OrderedLocusNames=PF1938;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 59-434.
RX PubMed=11162100; DOI=10.1006/jmbi.2000.4202;
RA Evdokimov A.G., Anderson D.E., Routzahn K.M., Waugh D.S.;
RT "Structural basis for oligosaccharide recognition by Pyrococcus furiosus
RT maltodextrin-binding protein.";
RL J. Mol. Biol. 305:891-904(2001).
CC -!- FUNCTION: Involved in an abc transport system for maltotriose. Binds
CC maltotriose much more tightly than maltose.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AE009950; AAL82062.1; -; Genomic_DNA.
DR RefSeq; WP_011013078.1; NZ_CP023154.1.
DR PDB; 1ELJ; X-ray; 1.85 A; A=59-434.
DR PDBsum; 1ELJ; -.
DR AlphaFoldDB; P58300; -.
DR SMR; P58300; -.
DR STRING; 186497.PF1938; -.
DR TCDB; 3.A.1.1.16; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAL82062; AAL82062; PF1938.
DR GeneID; 41713758; -.
DR KEGG; pfu:PF1938; -.
DR PATRIC; fig|186497.12.peg.2010; -.
DR eggNOG; arCOG00154; Archaea.
DR HOGENOM; CLU_031285_17_1_2; -.
DR OMA; WAHDWIG; -.
DR OrthoDB; 74127at2157; -.
DR PhylomeDB; P58300; -.
DR EvolutionaryTrace; P58300; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR006060; Maltose/Cyclodextrin-bd.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR006061; SBP_1_CS.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PRINTS; PR00181; MALTOSEBP.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Signal; Sugar transport; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..434
FT /note="Maltotriose-binding protein"
FT /id="PRO_0000031701"
FT REGION 28..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 69..85
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:1ELJ"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:1ELJ"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1ELJ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:1ELJ"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1ELJ"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1ELJ"
FT STRAND 315..324
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 394..409
FT /evidence="ECO:0007829|PDB:1ELJ"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:1ELJ"
FT HELIX 417..431
FT /evidence="ECO:0007829|PDB:1ELJ"
SQ SEQUENCE 434 AA; 48244 MW; EBC9E260636A9565 CRC64;
MRRATYAFAL LAILVLGVVA SGCIGGGTTT PTQTSPATQP TTTQTPTQTE TQAVECGSGK
VVIWHAMQPN ELEVFQSLAE EYMALCPEVE IVFEQKPNLE DALKAAIPTG QGPDLFIWAH
DWIGKFAEAG LLEPIDEYVT EDLLNEFAPM AQDAMQYKGH YYALPFAAET VAIIYNKEMV
SEPPKTFDEM KAIMEKYYDP ANEKYGIAWP INAYFISAIA QAFGGYYFDD KTEQPGLDKP
ETIEGFKFFF TEIWPYMAPT GDYNTQQSIF LEGRAPMMVN GPWSINDVKK AGINFGVVPL
PPIIKDGKEY WPRPYGGVKL IYFAAGIKNK DAAWKFAKWL TTSEESIKTL ALELGYIPVL
TKVLDDPEIK NDPVIYGFGQ AVQHAYLMPK SPKMSAVWGG VDGAINEILQ DPQNADIEGI
LKKYQQEILN NMQG
