MALX_STRR6
ID MALX_STRR6 Reviewed; 423 AA.
AC P59214; P29850;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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:0000305};
DE Flags: Precursor;
GN Name=malX; OrderedLocusNames=spr1918;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8478935; DOI=10.1006/jmbi.1993.1202;
RA Puyet A., Espinosa M.;
RT "Structure of the maltodextrin-uptake locus of Streptococcus pneumoniae.
RT Correlation to the Escherichia coli maltose regulon.";
RL J. Mol. Biol. 230:800-811(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6297760; DOI=10.1016/0092-8674(82)90126-x;
RA Lacks S.A., Dunn J.J., Greenberg B.;
RT "Identification of base mismatches recognized by the heteroduplex-DNA-
RT repair system of Streptococcus pneumoniae.";
RL Cell 31:327-336(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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:0000250|UniProtKB:P59213}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: By maltose.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26922.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L08611; AAA26925.1; -; Genomic_DNA.
DR EMBL; J01796; AAA26922.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE007317; AAL00720.1; -; Genomic_DNA.
DR PIR; C98111; C98111.
DR PIR; S32569; S32569.
DR RefSeq; NP_359509.1; NC_003098.1.
DR RefSeq; WP_000095484.1; NC_003098.1.
DR AlphaFoldDB; P59214; -.
DR SMR; P59214; -.
DR STRING; 171101.spr1918; -.
DR PRIDE; P59214; -.
DR EnsemblBacteria; AAL00720; AAL00720; spr1918.
DR GeneID; 60233886; -.
DR KEGG; spr:spr1918; -.
DR PATRIC; fig|171101.6.peg.2067; -.
DR eggNOG; COG2182; Bacteria.
DR HOGENOM; CLU_031285_17_2_9; -.
DR OMA; WAHDWIG; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:2001071; F:maltoheptaose binding; ISS:UniProtKB.
DR GO; GO:1901982; F:maltose binding; IBA:GO_Central.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015768; P:maltose transport; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW 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_0000031699"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 251..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P59213"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 45367 MW; 4555B07DA4E5BC5C CRC64;
MSSKFMKSTA VLGTVTLASL LLVACGSKTA DKPADSGSSE VKELTVYVDE GYKSYIEEVA
KAYEKEAGVK VTLKTGDALG GLDKLSLDNQ SGNVPDVMMA PYDRVGSLGS DGQLSEVKLS
DGAKTDDTTK SLVTAANGKV YGAPAVIESL VMYYNKDLVK DAPKTFADLE NLAKDSKYAF
AGEDGKTTAF LADWTNFYYT YGLLAGNGAY VFGQNGKDAK DIGLANDGSI AGINYAKSWY
EKWPKGMQDT EGAGNLIQTQ FQEGKTAAII DGPWKAQAFK DAKVNYGVAT IPTLPNGKEY
AAFGGGKAWV IPQAVKNLEA SQKFVDFLVA TEQQKVLYDK TNEIPANTEA RSYAEGKNDE
LTTAVIKQFK NTQPLPNISQ MSAVWDPAKN MLFDAVSGQK DAKTAANDAV TLIKETIKQK
FGE
