FUSA_STRPN
ID FUSA_STRPN Reviewed; 538 AA.
AC A0A0H2URD6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Fructooligosaccharide ABC transporter substrate-binding protein FusA {ECO:0000305};
DE Short=FOS ABC transporter SBP FusA {ECO:0000305};
DE Flags: Precursor;
GN Name=fusA {ECO:0000303|PubMed:23264576, ECO:0000303|PubMed:27939783};
GN OrderedLocusNames=SP_1796 {ECO:0000312|EMBL:AAK75869.1};
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187 {ECO:0000312|EMBL:AAK75869.1};
RN [1] {ECO:0000312|EMBL:AAK75869.1, ECO:0000312|Proteomes:UP000000585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4 {ECO:0000312|Proteomes:UP000000585};
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 FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC BAA-334 / TIGR4 {ECO:0000303|PubMed:23264576};
RX PubMed=23264576; DOI=10.1128/jb.01560-12;
RA Linke C.M., Woodiga S.A., Meyers D.J., Buckwalter C.M., Salhi H.E.,
RA King S.J.;
RT "The ABC transporter encoded at the pneumococcal fructooligosaccharide
RT utilization locus determines the ability to utilize long- and short-chain
RT fructooligosaccharides.";
RL J. Bacteriol. 195:1031-1041(2013).
RN [3] {ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60, ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62}
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 47-538 AND IN COMPLEXES WITH
RP KESTOSE; NYSTOSE AND CALCIUM AND MUTANT ALA-223/ALA-224 IN COMPLEX WITH
RP FRUCTOFURANOSYL-NYSTOSE, FUNCTION, DOMAIN, AND MUTAGENESIS OF GLU-167;
RP HIS-177; ASP-223; GLU-224; TRP-314; ASN-318; TRP-384; ARG-419 AND GLU-423.
RC STRAIN=ATCC BAA-334 / TIGR4 {ECO:0000303|PubMed:27939783};
RX PubMed=27939783; DOI=10.1016/j.str.2016.11.008;
RA Culurgioni S., Harris G., Singh A.K., King S.J., Walsh M.A.;
RT "Structural Basis for Regulation and Specificity of Fructooligosaccharide
RT Import in Streptococcus pneumoniae.";
RL Structure 25:79-93(2017).
CC -!- FUNCTION: Part of the ABC transporter complex FusABC-MsmK involved in
CC short- and long-chain fructooligosaccharide (FOS) import. Required for
CC the utilization of long-chain FOSs (PubMed:23264576). Binds kestose,
CC nystose, fructofuranosyl-nystose and inulin, but not sucrose. Has a
CC preference for long-chain FOSs (tetrasaccharides and larger)
CC (PubMed:27939783). {ECO:0000269|PubMed:27939783,
CC ECO:0000305|PubMed:23264576}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsmK),
CC two transmembrane proteins (FusB and FusC) and a solute-binding protein
CC (FusA). {ECO:0000305|PubMed:23264576}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- DOMAIN: The calcium-binding site is essential for the translocation of
CC fructooligosaccharide (FOS) substrates by the transporter.
CC {ECO:0000269|PubMed:27939783}.
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; AAK75869.1; -; Genomic_DNA.
DR RefSeq; WP_000669747.1; NZ_AKVY01000001.1.
DR PDB; 5G5Y; X-ray; 1.73 A; A/B=47-538.
DR PDB; 5G5Z; X-ray; 2.01 A; A/B/C/D=47-537.
DR PDB; 5G60; X-ray; 1.99 A; A/B/C/D=47-538.
DR PDB; 5G61; X-ray; 2.40 A; A/B/C/D=47-538.
DR PDB; 5G62; X-ray; 1.99 A; A/B=47-538.
DR PDBsum; 5G5Y; -.
DR PDBsum; 5G5Z; -.
DR PDBsum; 5G60; -.
DR PDBsum; 5G61; -.
DR PDBsum; 5G62; -.
DR AlphaFoldDB; A0A0H2URD6; -.
DR SMR; A0A0H2URD6; -.
DR STRING; 170187.SP_1796; -.
DR EnsemblBacteria; AAK75869; AAK75869; SP_1796.
DR KEGG; spn:SP_1796; -.
DR eggNOG; COG1653; Bacteria.
DR OMA; FVAMMQF; -.
DR PhylomeDB; A0A0H2URD6; -.
DR BioCyc; SPNE170187:G1FZB-1827-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015774; P:polysaccharide 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; Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Polysaccharide transport; Signal; Sugar transport; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..538
FT /note="Fructooligosaccharide ABC transporter substrate-
FT binding protein FusA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5002599567"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60,
FT ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60,
FT ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Y, ECO:0007744|PDB:5G5Z,
FT ECO:0007744|PDB:5G60"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60,
FT ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60,
FT ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60,
FT ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60,
FT ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60,
FT ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27939783,
FT ECO:0007744|PDB:5G5Z, ECO:0007744|PDB:5G60,
FT ECO:0007744|PDB:5G61, ECO:0007744|PDB:5G62"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 167
FT /note="E->A: Loss of fructooligosaccharide (FOS) binding.
FT No growth on nystose."
FT /evidence="ECO:0000269|PubMed:27939783"
FT MUTAGEN 177
FT /note="H->A: 2-fold decrease in fructooligosaccharide (FOS)
FT binding compared to the wild-type. Impaired growth on
FT nystose."
FT /evidence="ECO:0000269|PubMed:27939783"
FT MUTAGEN 223
FT /note="D->A: No effect in fructooligosaccharide (FOS)
FT binding, but no growth on nystose; when associated with A-
FT 224."
FT /evidence="ECO:0000269|PubMed:27939783"
FT MUTAGEN 224
FT /note="E->A: No effect in fructooligosaccharide (FOS)
FT binding, but no growth on nystose; when associated with A-
FT 223."
FT /evidence="ECO:0000269|PubMed:27939783"
FT MUTAGEN 314
FT /note="W->A: Loss of fructooligosaccharide (FOS) binding.
FT No growth on nystose."
FT /evidence="ECO:0000269|PubMed:27939783"
FT MUTAGEN 318
FT /note="N->A: Significant decrease in fructooligosaccharide
FT (FOS) binding. Impaired growth on nystose."
FT /evidence="ECO:0000269|PubMed:27939783"
FT MUTAGEN 384
FT /note="W->A: Significant decrease in fructooligosaccharide
FT (FOS) binding. Impaired growth on nystose."
FT /evidence="ECO:0000269|PubMed:27939783"
FT MUTAGEN 419
FT /note="R->A: Loss of fructooligosaccharide (FOS) binding.
FT No growth on nystose."
FT /evidence="ECO:0000269|PubMed:27939783"
FT MUTAGEN 423
FT /note="E->A: 10-fold decrease in fructooligosaccharide
FT (FOS) binding compared to the wild-type. Impaired growth on
FT nystose."
FT /evidence="ECO:0000269|PubMed:27939783"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:5G5Y"
FT TURN 289..293
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:5G5Y"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:5G5Y"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:5G5Y"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 443..455
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 473..499
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 503..516
FT /evidence="ECO:0007829|PDB:5G5Y"
FT HELIX 519..536
FT /evidence="ECO:0007829|PDB:5G5Y"
SQ SEQUENCE 538 AA; 60992 MW; 2BDF8A495C408F8B CRC64;
MKFKTFSKSA VLLTASLAVL AACGSKNTAS SPDYKLEGVT FPLQEKKTLK FMTASSPLSP
KDPNEKLILQ RLEKETGVHI DWTNYQSDFA EKRNLDISSG DLPDAIHNDG ASDVDLMNWA
KKGVIIPVED LIDKYMPNLK KILDEKPEYK ALMTAPDGHI YSFPWIEELG DGKESIHSVN
DMAWINKDWL KKLGLEMPKT TDDLIKVLEA FKNGDPNGNG EADEIPFSFI SGNGNEDFKF
LFAAFGIGDN DDHLVVGNDG KVDFTADNDN YKEGVKFIRQ LQEKGLIDKE AFEHDWNSYI
AKGHDQKFGV YFTWDKNNVT GSNESYDVLP VLAGPSGQKH VARTNGMGFA RDKMVITSVN
KNLELTAKWI DAQYAPLQSV QNNWGTYGDD KQQNIFELDQ ASNSLKHLPL NGTAPAELRQ
KTEVGGPLAI LDSYYGKVTT MPDDAKWRLD LIKEYYVPYM SNVNNYPRVF MTQEDLDKIA
HIEADMNDYI YRKRAEWIVN GNIDTEWDDY KKELEKYGLS DYLAIKQKYY DQYQANKN
