ID   DCTP2_OLEA2             Reviewed;         340 AA.
AC   Q315G1;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Solute-binding protein Dde_0634 {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=Dde_0634 {ECO:0000312|EMBL:ABB37435.1};
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559 {ECO:0000312|EMBL:ABB37435.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
RN   [2] {ECO:0007744|PDB:4NAP, ECO:0007744|PDB:4PGN, ECO:0007744|PDB:4PGP}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 30-340 IN COMPLEXES WITH
RP   INDOLE-3-PYRUVATE; D-TRYPTOPHAN AND INDOLE-3-ACETATE, 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 indole-3-pyruvate and
CC       indole-3-acetate (in vitro). Can also bind D-tryptophan (in vitro), but
CC       that is probably not a physiological ligand (PubMed:25540822). Probably
CC       part of a tripartite ATP-independent periplasmic (TRAP) transport
CC       system that mediates solute transport into the cytoplasm.
CC       {ECO:0000269|PubMed:25540822, 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; CP000112; ABB37435.1; -; Genomic_DNA.
DR   RefSeq; WP_011366730.1; NC_007519.1.
DR   PDB; 4NAP; X-ray; 2.30 A; A/B/C/D=30-340.
DR   PDB; 4PGN; X-ray; 1.80 A; A/B/C/D=30-340.
DR   PDB; 4PGP; X-ray; 2.25 A; A/B/C/D=30-340.
DR   PDBsum; 4NAP; -.
DR   PDBsum; 4PGN; -.
DR   PDBsum; 4PGP; -.
DR   AlphaFoldDB; Q315G1; -.
DR   SMR; Q315G1; -.
DR   STRING; 207559.Dde_0634; -.
DR   EnsemblBacteria; ABB37435; ABB37435; Dde_0634.
DR   KEGG; dde:Dde_0634; -.
DR   eggNOG; COG1638; Bacteria.
DR   HOGENOM; CLU_036176_2_1_7; -.
DR   OMA; LPANDMY; -.
DR   OrthoDB; 752834at2; -.
DR   Proteomes; UP000002710; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; IPR038404; TRAP_DctP_sf.
DR   PANTHER; PTHR33376; PTHR33376; 1.
DR   Pfam; PF03480; DctP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..340
FT                   /note="Solute-binding protein Dde_0634"
FT                   /id="PRO_5004220063"
FT   BINDING         99
FT                   /ligand="(indol-3-yl)acetate"
FT                   /ligand_id="ChEBI:CHEBI:30854"
FT                   /evidence="ECO:0007744|PDB:4PGP"
FT   BINDING         172
FT                   /ligand="(indol-3-yl)acetate"
FT                   /ligand_id="ChEBI:CHEBI:30854"
FT                   /evidence="ECO:0007744|PDB:4PGP"
FT   BINDING         210..213
FT                   /ligand="(indol-3-yl)acetate"
FT                   /ligand_id="ChEBI:CHEBI:30854"
FT                   /evidence="ECO:0007744|PDB:4PGP"
FT   BINDING         235
FT                   /ligand="(indol-3-yl)acetate"
FT                   /ligand_id="ChEBI:CHEBI:30854"
FT                   /evidence="ECO:0007744|PDB:4PGP"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           45..60
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          64..70
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           81..86
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           107..111
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           119..133
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          152..158
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           163..166
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           175..184
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           196..201
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          226..232
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          236..241
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           243..247
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           251..258
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           261..287
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   STRAND          290..292
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           296..306
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           308..319
FT                   /evidence="ECO:0007829|PDB:4PGN"
FT   HELIX           324..337
FT                   /evidence="ECO:0007829|PDB:4PGN"
SQ   SEQUENCE   340 AA;  36923 MW;  EBDD2DE9E752DA8D CRC64;
     MKSTFAALLI MVGCLVSGAL LTGSEAAAAQ PVTLNYANFP PASTFPCIQM EQWAHEVRTR
     TRGKVDVLTY PGGTLLGARN MLRGVMSGQA DIGCISLAYH PGVFPVMSVF ELPLGFTSAE
     AASSVLWELY SGLRPAELER VKVLTMFTSA PSHFMTVTPV RSLRDLQGME IRGAGTLSAI
     LEKLGATPVS MPMPEVPEAV QKGIIKGLFT SLDVMKDMNF AEMTGHVTRA DQAVYPFAVI
     MNREAWERLS PDVQQVLDGL AAEHAAWTGR YLDAHVQDSM RWAEEKHGVQ VHTLPEEDIA
     AMRRSVQPLF DAWAQRAADK GADPDAVMRT VDALKAQYGG