DCTP1_POLSJ
ID DCTP1_POLSJ Reviewed; 330 AA.
AC Q128M1;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Solute-binding protein Bpro_3107 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=Bpro_3107 {ECO:0000312|EMBL:ABE45021.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000312|EMBL:ABE45021.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
RN [2] {ECO:0007744|PDB:4MHF, ECO:0007744|PDB:4MIJ}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEXES WITH D-GALACTURONATE
RP AND D-GLUCURONATE, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=25540822; DOI=10.1021/bi501388y;
RA Vetting M.W., Al-Obaidi N., Zhao S., San Francisco B., Kim J.,
RA Wichelecki D.J., Bouvier J.T., Solbiati J.O., Vu H., Zhang X.,
RA Rodionov D.A., Love J.D., Hillerich B.S., Seidel R.D., Quinn R.J.,
RA Osterman A.L., Cronan J.E., Jacobson M.P., Gerlt J.A., Almo S.C.;
RT "Experimental strategies for functional annotation and metabolism
RT discovery: targeted screening of solute binding proteins and unbiased
RT panning of metabolomes.";
RL Biochemistry 54:909-931(2015).
CC -!- FUNCTION: Solute-binding protein that binds D-galacturonate and D-
CC glucuronate (in vitro) (PubMed:25540822). Probably part of a tripartite
CC ATP-independent periplasmic (TRAP) transport system that mediates
CC solute transport into the cytoplasm. {ECO:0000269|PubMed:25540822,
CC ECO:0000305}.
CC -!- SUBUNIT: The complex is comprised of an extracytoplasmic solute-binding
CC protein and a heteromeric permease formed by two transmembrane
CC proteins. {ECO:0000250|UniProtKB:P37735}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P37735}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC {ECO:0000305}.
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DR EMBL; CP000316; ABE45021.1; -; Genomic_DNA.
DR RefSeq; WP_011484016.1; NC_007948.1.
DR PDB; 4MHF; X-ray; 1.46 A; A=1-330.
DR PDB; 4MIJ; X-ray; 1.10 A; A=1-330.
DR PDBsum; 4MHF; -.
DR PDBsum; 4MIJ; -.
DR AlphaFoldDB; Q128M1; -.
DR SMR; Q128M1; -.
DR STRING; 296591.Bpro_3107; -.
DR EnsemblBacteria; ABE45021; ABE45021; Bpro_3107.
DR KEGG; pol:Bpro_3107; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_4_0_4; -.
DR OMA; MPMGEVY; -.
DR OrthoDB; 752834at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.40.190.170; -; 1.
DR InterPro; IPR018389; DctP_fam.
DR InterPro; IPR004682; TRAP_DctP.
DR InterPro; IPR038404; TRAP_DctP_sf.
DR PANTHER; PTHR33376; PTHR33376; 1.
DR Pfam; PF03480; DctP; 1.
DR PIRSF; PIRSF006470; DctB; 1.
DR TIGRFAMs; TIGR00787; dctP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Periplasm; Reference proteome; Signal;
KW Sugar transport; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..330
FT /note="Solute-binding protein Bpro_3107"
FT /id="PRO_5004181211"
FT BINDING 39
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 39
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT BINDING 78
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 78
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT BINDING 94
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 94
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT BINDING 154
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 154
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT BINDING 174..176
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 174..176
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT BINDING 197
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 197
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT BINDING 214
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 214
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT BINDING 218
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 218
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT BINDING 241
FT /ligand="D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:75525"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MIJ"
FT BINDING 241
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4MHF"
FT DISULFID 104..138
FT /evidence="ECO:0007744|PDB:4MHF, ECO:0007744|PDB:4MIJ"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:4MIJ"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4MIJ"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4MIJ"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:4MIJ"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 255..289
FT /evidence="ECO:0007829|PDB:4MIJ"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:4MIJ"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:4MIJ"
SQ SEQUENCE 330 AA; 35807 MW; EA7B608AFB25E83E CRC64;
MTNRTPRISA IRSAALAALL AGLGMGAAQA TEFRSADTHN ADDYPTVAAV KYMGELLEKK
SGGKHKIKVF NKQALGSEKE TIDQVKIGAL DFTRVNVGPM NAICPLTQVP TMPFLFSSIA
HMRKSLDGPV GDEILKSCES AGFIGLAFYD SGARSIYAKK PIRTVADAKG LKIRVQQSDL
WVALVSAMGA NATPMPYGEV YTGLKTGLID AAENNIPSFD TAKHVEAVKV YSKTEHSMAP
EILVMSKIIY DKLPKAEQDM IRAAAKESVA FERQKWDEQE AKSLANVKAA GAEIVEVDKK
SFQAVMGPVY DKFMTTPDMK RLVKAVQDTK
