DCTP_BURCM
ID DCTP_BURCM Reviewed; 328 AA.
AC Q0B2F6;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Solute-binding protein Bamb_6123 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=Bamb_6123 {ECO:0000312|EMBL:ABI91667.1};
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670 {ECO:0000312|EMBL:ABI91667.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4LN5, ECO:0007744|PDB:4N15, ECO:0007744|PDB:4N17}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH
RP BETA-D-GALACTURONATE AND BETA-D-GLUCURONATE, AND FUNCTION.
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; CP000442; ABI91667.1; -; Genomic_DNA.
DR RefSeq; WP_011660998.1; NZ_CP009800.1.
DR PDB; 4LN5; X-ray; 2.10 A; A=1-328.
DR PDB; 4N15; X-ray; 1.65 A; A=1-328.
DR PDB; 4N17; X-ray; 1.50 A; A=1-328.
DR PDBsum; 4LN5; -.
DR PDBsum; 4N15; -.
DR PDBsum; 4N17; -.
DR AlphaFoldDB; Q0B2F6; -.
DR SMR; Q0B2F6; -.
DR STRING; 339670.Bamb_6123; -.
DR EnsemblBacteria; ABI91667; ABI91667; Bamb_6123.
DR GeneID; 44696662; -.
DR KEGG; bam:Bamb_6123; -.
DR PATRIC; fig|339670.21.peg.7098; -.
DR eggNOG; COG1638; Bacteria.
DR OMA; MPMGEVY; -.
DR Proteomes; UP000000662; Chromosome 3.
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; Periplasm; Signal; Sugar transport; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..328
FT /note="Solute-binding protein Bamb_6123"
FT /id="PRO_5004168636"
FT BINDING 35
FT /ligand="beta-D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:85312"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N17"
FT BINDING 35
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N15"
FT BINDING 73
FT /ligand="beta-D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:85312"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N17"
FT BINDING 73
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N15"
FT BINDING 89
FT /ligand="beta-D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:85312"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N17"
FT BINDING 89
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N15"
FT BINDING 149
FT /ligand="beta-D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:85312"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N17"
FT BINDING 149
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N15"
FT BINDING 209
FT /ligand="beta-D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:85312"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N17"
FT BINDING 209
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N15"
FT BINDING 236
FT /ligand="beta-D-galacturonate"
FT /ligand_id="ChEBI:CHEBI:85312"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N17"
FT BINDING 236
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4N15"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:4N17"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:4N17"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:4N17"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 250..284
FT /evidence="ECO:0007829|PDB:4N17"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:4N17"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:4N17"
SQ SEQUENCE 328 AA; 35995 MW; A75EF5C9E5B35C02 CRC64;
MTHRFPRSRT ALAVALMAGF AMSAQARVFR SADVHGDSFP TNMAVKFMGD ELSKLTGGKD
SIKVFGNSAL GSEKDTVDQV RIGAIDMARV NGASFNEIVP ESLIPSFPFL FRDVDHFRKA
MYGPAGQKIL DAFAAKGMIA LTFYESGARS IYAKRPVRTP ADMKGLKVRV QPSDLMVDEI
RAMGGTPTPM PFAEVYTGLK TGLVDAAENN LPSYEETKHF EVAPDYSETQ HAMTPEVLVF
SKKIWDTLSP QEQAAIRKAA ADSVPYYQKL WTAREASAQQ AVTKGGANIL PAAQVDRAAF
VKAMQPLWTK YEKTPQMKQI VDEIEATK
