SBP92_STRPN
ID SBP92_STRPN Reviewed; 491 AA.
AC A0A0H2UMY0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Carbohydrate ABC transporter substrate-binding protein {ECO:0000305};
DE AltName: Full=Carbohydrate substrate-binding protein SP0092 {ECO:0000303|PubMed:28045395, ECO:0000303|PubMed:28994793};
DE Short=Carbohydrate SBP SP0092 {ECO:0000303|PubMed:28045395};
GN OrderedLocusNames=SP_0092 {ECO:0000312|EMBL:AAK74279.1};
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:AAK74279.1};
RN [1] {ECO:0000312|EMBL:AAK74279.1, ECO:0000312|Proteomes:UP000000585}
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 CRYSTALLIZATION, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP BIOTECHNOLOGY.
RX PubMed=28994793; DOI=10.3791/56294;
RA Culurgioni S., Tang M., Hall D.R., Walsh M.A.;
RT "Biochemical and Structural Characterization of the Carbohydrate Transport
RT Substrate-binding-protein SP0092.";
RL J. Vis. Exp. 128:E56294-E56294(2017).
RN [3] {ECO:0007744|PDB:5MLT}
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 39-491 IN COMPLEX WITH ZINC,
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC BAA-334 / TIGR4 {ECO:0000303|PubMed:28045395};
RX PubMed=28045395; DOI=10.1107/s2053230x16020252;
RA Culurgioni S., Tang M., Walsh M.A.;
RT "Structural characterization of the Streptococcus pneumoniae carbohydrate
RT substrate-binding protein SP0092.";
RL Acta Crystallogr. F 73:54-61(2017).
CC -!- FUNCTION: Probably part of an ABC transporter complex involved in
CC carbohydrate transport. {ECO:0000305|PubMed:28045395,
CC ECO:0000305|PubMed:28994793}.
CC -!- SUBUNIT: Exists as a monomer, homodimer, homotrimer and homotetramer;
CC oligomerization increases with higher protein concentration.
CC {ECO:0000269|PubMed:28045395, ECO:0000269|PubMed:28994793}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305|PubMed:28994793}.
CC -!- BIOTECHNOLOGY: This protein has potential use in the development of
CC vaccines and antimicrobials against pneumococcus, because of its
CC extracellular localization and the essentiality of carbohydrate import
CC for the pneumococcal metabolism. The characterization protocol
CC developed for this protein can be helpful in structure-based design of
CC inhibitors for the carbohydrate-binding proteins in general.
CC {ECO:0000305|PubMed:28994793}.
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; AAK74279.1; -; Genomic_DNA.
DR RefSeq; WP_000800407.1; NZ_AKVY01000001.1.
DR PDB; 5MLT; X-ray; 1.61 A; A=39-491.
DR PDBsum; 5MLT; -.
DR AlphaFoldDB; A0A0H2UMY0; -.
DR SMR; A0A0H2UMY0; -.
DR STRING; 170187.SP_0092; -.
DR EnsemblBacteria; AAK74279; AAK74279; SP_0092.
DR GeneID; 60233537; -.
DR GeneID; 66805296; -.
DR KEGG; spn:SP_0092; -.
DR eggNOG; COG1653; Bacteria.
DR OMA; TKLMPKY; -.
DR PhylomeDB; A0A0H2UMY0; -.
DR BioCyc; SPNE170187:G1FZB-96-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:UniProtKB.
DR GO; GO:0010339; C:external side of cell wall; NAS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0098704; P:carbohydrate import across plasma membrane; NAS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR InterPro; IPR022627; DUF3502.
DR Pfam; PF12010; DUF3502; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Sugar transport; Transport; Zinc.
FT CHAIN 1..491
FT /note="Carbohydrate ABC transporter substrate-binding
FT protein"
FT /id="PRO_5002599486"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28045395,
FT ECO:0007744|PDB:5MLT"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28045395,
FT ECO:0007744|PDB:5MLT"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28045395,
FT ECO:0007744|PDB:5MLT"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28045395,
FT ECO:0007744|PDB:5MLT"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 55..70
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5MLT"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:5MLT"
FT TURN 262..266
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5MLT"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:5MLT"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:5MLT"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:5MLT"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 431..449
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:5MLT"
FT HELIX 471..487
FT /evidence="ECO:0007829|PDB:5MLT"
SQ SEQUENCE 491 AA; 54486 MW; F5C0CCB158E7EAB6 CRC64;
MKNWKKYAFA SASVVALAAG LAACGNLTGN SKKAADSGDK PVIKMYQIGD KPDNLDELLA
NANKIIEEKV GAKLDIQYLG WGDYGKKMSV ITSSGENYDI AFADNYIVNA QKGAYADLTE
LYKKEGKDLY KALDPAYIKG NTVNGKIYAV PVAANVASSQ NFAFNGTLLA KYGIDISGVT
SYETLEPVLK QIKEKAPDVV PFAIGKVFIP SDNFDYPVAN GLPFVIDLEG DTTKVVNRYE
VPRFKEHLKT LHKFYEAGYI PKDVATSDTS FDLQQDTWFV REETVGPADY GNSLLSRVAN
KDIQIKPITN FIKKNQTTQV ANFVISNNSK NKEKSMEILN LLNTNPELLN GLVYGPEGKN
WEKIEGKENR VRVLDGYKGN THMGGWNTGN NWILYINENV TDQQIENSKK ELAEAKESPA
LGFIFNTDNV KSEISAIANT MQQFDTAINT GTVDPDKAIP ELMEKLKSEG AYEKVLNEMQ
KQYDEFLKNK K
