ID MALX_STRPN Reviewed; 423 AA.
AC P59213; P29850;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Maltooligosaccharide ABC transporter solute-binding lipoprotein {ECO:0000305};
DE AltName: Full=Maltodextrin-binding protein {ECO:0000305};
DE AltName: Full=Solute-binding protein MalX {ECO:0000303|PubMed:20497336};
DE Flags: Precursor;
GN Name=malX {ECO:0000303|PubMed:2684766, ECO:0000312|EMBL:AAK76167.1};
GN OrderedLocusNames=SP_2108 {ECO:0000312|EMBL:AAK76167.1};
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R6 / R800;
RX PubMed=2684766; DOI=10.1016/0378-1119(89)90287-4;
RA Martin B., Alloing G., Boucraut C., Claverys J.-P.;
RT "The difficulty of cloning Streptococcus pneumoniae mal and ami loci in
RT Escherichia coli: toxicity of malX and amiA gene products.";
RL Gene 80:227-238(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-423 AND IN COMPLEX WITH
RP MALTOHEPTAOSE, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20497336; DOI=10.1111/j.1365-2958.2010.07199.x;
RA Abbott D.W., Higgins M.A., Hyrnuik S., Pluvinage B.,
RA Lammerts van Bueren A., Boraston A.B.;
RT "The molecular basis of glycogen breakdown and transport in Streptococcus
RT pneumoniae.";
RL Mol. Microbiol. 77:183-199(2010).
CC -!- FUNCTION: Part of an ABC transporter complex involved in the uptake of
CC maltodextrins. Binds glycogen-derived linear maltooligosaccharides
CC increasing in size from maltotriose to maltooctaose with the highest
CC affinity for maltotriose. Has a very weak affinity for maltose. Has
CC also a very low affinity for maltotetraitol, indicating that the
CC binding is selective for maltooligosaccharides with an intact reducing
CC end. {ECO:0000269|PubMed:20497336}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: By maltose.
CC -!- DISRUPTION PHENOTYPE: Grows readily on glucose and maltotriose, but is
CC not able to grow on glycogen. Deletion mutant is still able to
CC depolymerize glycogen to some extent resulting in alpha-
CC glucooligosaccharides increasing in size from maltotetraose to
CC maltooctaose and larger oligosaccharides. In contrast to the wild-type
CC cells, which almost completely deplete alpha-glucooligosaccharides up
CC to eight glucose units in length, only partially deplete
CC oligosaccharides of 9-11 glucose units in length and which have little
CC to no ability to deplete oligosaccharides longer than 11 glucose units
CC in length, the most abundant alpha-glucooligosaccharides produced by
CC the deletion mutant are maltopentaose, maltohexaose, and maltoheptaose.
CC {ECO:0000269|PubMed:20497336}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005672; AAK76167.1; -; Genomic_DNA.
DR PIR; F95246; F95246.
DR RefSeq; WP_000095467.1; NZ_CP089948.1.
DR PDB; 2XD2; X-ray; 2.90 A; A/B=31-423.
DR PDB; 2XD3; X-ray; 2.00 A; A=31-423.
DR PDBsum; 2XD2; -.
DR PDBsum; 2XD3; -.
DR AlphaFoldDB; P59213; -.
DR SMR; P59213; -.
DR PaxDb; 170187-SP_2108; -.
DR EnsemblBacteria; AAK76167; AAK76167; SP_2108.
DR GeneID; 66807187; -.
DR KEGG; spn:SP_2108; -.
DR eggNOG; COG2182; Bacteria.
DR PhylomeDB; P59213; -.
DR BioCyc; SPNE170187:G1FZB-2196-MONOMER; -.
DR EvolutionaryTrace; P59213; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:UniProtKB.
DR GO; GO:0042958; F:maltodextrin transmembrane transporter activity; IC:UniProtKB.
DR GO; GO:2001071; F:maltoheptaose binding; IDA:UniProtKB.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IMP:UniProtKB.
DR CDD; cd13658; PBP2_CMBP; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR006060; Maltose/Cyclodextrin-bd.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR006061; SBP_1_CS.
DR PANTHER; PTHR30061; MALTOSE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30061:SF50; MALTOSE_MALTODEXTRIN-BINDING PERIPLASMIC PROTEIN; 1.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PRINTS; PR00181; MALTOSEBP.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Sugar transport; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000305"
FT CHAIN 25..423
FT /note="Maltooligosaccharide ABC transporter solute-binding
FT lipoprotein"
FT /id="PRO_0000031698"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 251..254
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20497336,
FT ECO:0007744|PDB:2XD3"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:2XD3"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2XD2"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:2XD3"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 385..396
FT /evidence="ECO:0007829|PDB:2XD3"
FT HELIX 402..416
FT /evidence="ECO:0007829|PDB:2XD3"
SQ SEQUENCE 423 AA; 45337 MW; 3FFE39EB2E78FE66 CRC64;
MSSKFMKSAA VLGTATLASL LLVACGSKTA DKPADSGSSE VKELTVYVDE GYKSYIEEVA
KAYEKEAGVK VTLKTGDALG GLDKLSLDNQ SGNVPDVMMA PYDRVGSLGS DGQLSEVKLS
DGAKTDDTTK SLVTAANGKV YGAPAVIESL VMYYNKDLVK DAPKTFADLE NLAKDSKYAF
AGEDGKTTAF LADWTNFYYT YGLLAGNGAY VFGQNGKDAK DIGLANDGSI VGINYAKSWY
EKWPKGMQDT EGAGNLIQTQ FQEGKTAAII DGPWKAQAFK DAKVNYGVAT IPTLPNGKEY
AAFGGGKAWV IPQAVKNLEA SQKFVDFLVA TEQQKVLYDK TNEIPANTEA RSYAEGKNDE
LTTAVIKQFK NTQPLPNISQ MSAVWDPAKN MLFDAVSGQK DAKTAANDAV TLIKETIKQK
FGE
//
