ID   DCTP_VEREI              Reviewed;         335 AA.
AC   A1WPV4;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Solute-binding protein Veis_3954 {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=Veis_3954 {ECO:0000312|EMBL:ABM59661.1};
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735 {ECO:0000312|EMBL:ABM59661.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007744|PDB:4P9K, ECO:0007744|PDB:4PAK}
RP   X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 33-335 IN COMPLEX WITH
RP   ERYTHRONATE AND PANTOATE, 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 (R)-pantoate and D-
CC       erythronate (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}.
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; CP000542; ABM59661.1; -; Genomic_DNA.
DR   RefSeq; WP_011811648.1; NC_008786.1.
DR   PDB; 4P9K; X-ray; 1.40 A; A=33-335.
DR   PDB; 4PAK; X-ray; 1.20 A; A=33-335.
DR   PDBsum; 4P9K; -.
DR   PDBsum; 4PAK; -.
DR   AlphaFoldDB; A1WPV4; -.
DR   SMR; A1WPV4; -.
DR   STRING; 391735.Veis_3954; -.
DR   EnsemblBacteria; ABM59661; ABM59661; Veis_3954.
DR   KEGG; vei:Veis_3954; -.
DR   eggNOG; COG1638; Bacteria.
DR   HOGENOM; CLU_036176_1_3_4; -.
DR   OMA; RTMENPV; -.
DR   OrthoDB; 752834at2; -.
DR   Proteomes; UP000000374; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071702; P:organic substance transport; IEA:UniProt.
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; Reference proteome; Signal; Transport.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..335
FT                   /note="Solute-binding protein Veis_3954"
FT                   /id="PRO_5002640020"
FT   BINDING         50
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0007744|PDB:4PAK"
FT   BINDING         82
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0007744|PDB:4PAK"
FT   BINDING         155..158
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0007744|PDB:4PAK"
FT   BINDING         179
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0007744|PDB:4PAK"
FT   BINDING         219
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0007744|PDB:4PAK"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           49..64
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          68..74
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   TURN            76..79
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           82..91
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          93..101
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           109..115
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           123..131
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           133..140
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           141..145
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          147..164
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           184..192
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          196..199
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           202..204
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           205..211
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          213..219
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           221..226
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          234..251
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           252..257
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           260..294
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   STRAND          298..300
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           305..311
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           313..323
FT                   /evidence="ECO:0007829|PDB:4PAK"
FT   HELIX           325..332
FT                   /evidence="ECO:0007829|PDB:4PAK"
SQ   SEQUENCE   335 AA;  36407 MW;  B8A09DCD0BFAFD7B CRC64;
     MPSTRPLPRP SSRSLRRLAL GLGLAFGLGA TAAAQTTMRI NISTAQNSHQ GVAIDTFAKE
     VEKRTGGRYK VQTFYNAALG AERESVEAVQ LGTHELTFSS SGPIPNFVPE TKILDVPFLF
     RDKAHARAVL DGPIGQELLT RFDGKGFKAL AWAENGFRHM SNSKRAVKEP GDLKGLKMRT
     MENPVHIAAY KGFGIVTTPM AFSEVFTALQ QGTVDGQENP LSVIISAKFD QVQKHLTLTG
     HVYSPALFLM NKALFDKLPA ADQQAFIDAA RQGAKLNRAR VDEDDAKGVA DLRAKGMTVI
     DNIDKARFVA ALAPVNAQFE KQFGKAALEQ IRSAQ