DCTP_ROSDO
ID DCTP_ROSDO Reviewed; 325 AA.
AC Q16BC9;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Solute-binding protein RD1_1052 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=RD1_1052 {ECO:0000312|EMBL:ABG30714.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000312|EMBL:ABG30714.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114;
RX PubMed=17098896; DOI=10.1128/jb.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
RN [2] {ECO:0007744|PDB:4PC9, ECO:0007744|PDB:4PCD}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 27-325 IN COMPLEXES WITH
RP L-GALACTONATE AND D-MANNONATE, 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 L-galactonate and D-
CC mannonate (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; CP000362; ABG30714.1; -; Genomic_DNA.
DR RefSeq; WP_011567336.1; NZ_FOOO01000009.1.
DR PDB; 4PC9; X-ray; 1.30 A; A=27-325.
DR PDB; 4PCD; X-ray; 1.70 A; A=27-325.
DR PDBsum; 4PC9; -.
DR PDBsum; 4PCD; -.
DR AlphaFoldDB; Q16BC9; -.
DR SMR; Q16BC9; -.
DR STRING; 375451.RD1_1052; -.
DR EnsemblBacteria; ABG30714; ABG30714; RD1_1052.
DR KEGG; rde:RD1_1052; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_1_3_5; -.
DR OMA; RSWIYLT; -.
DR OrthoDB; 752834at2; -.
DR Proteomes; UP000007029; 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; Periplasm; Reference proteome; Signal; Sugar transport;
KW Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..325
FT /note="Solute-binding protein RD1_1052"
FT /evidence="ECO:0000255"
FT /id="PRO_5004184503"
FT BINDING 75
FT /ligand="D-mannonate"
FT /ligand_id="ChEBI:CHEBI:17767"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PC9"
FT BINDING 75
FT /ligand="L-galactonate"
FT /ligand_id="ChEBI:CHEBI:53071"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PCD"
FT BINDING 93..95
FT /ligand="D-mannonate"
FT /ligand_id="ChEBI:CHEBI:17767"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PC9"
FT BINDING 93..95
FT /ligand="L-galactonate"
FT /ligand_id="ChEBI:CHEBI:53071"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PCD"
FT BINDING 148..151
FT /ligand="D-mannonate"
FT /ligand_id="ChEBI:CHEBI:17767"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PC9"
FT BINDING 148..151
FT /ligand="L-galactonate"
FT /ligand_id="ChEBI:CHEBI:53071"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PCD"
FT BINDING 171
FT /ligand="D-mannonate"
FT /ligand_id="ChEBI:CHEBI:17767"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PC9"
FT BINDING 171
FT /ligand="L-galactonate"
FT /ligand_id="ChEBI:CHEBI:53071"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PCD"
FT BINDING 211
FT /ligand="D-mannonate"
FT /ligand_id="ChEBI:CHEBI:17767"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PC9"
FT BINDING 211
FT /ligand="L-galactonate"
FT /ligand_id="ChEBI:CHEBI:53071"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4PCD"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:4PC9"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:4PC9"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4PCD"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 252..286
FT /evidence="ECO:0007829|PDB:4PC9"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:4PC9"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:4PC9"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:4PC9"
SQ SEQUENCE 325 AA; 35383 MW; 5DE35D2A25B100EE CRC64;
MRLFTKIKGL AAVTCVAALA SSAAFAQEMT LKLGHLANEQ NAWHLAAVKF GEELSTLTDG
RIAVEVFPNE SLGKEIDLIN GMQLGTVDMT ITGESLQNWA PMAALLAVPY AYKSLEHMDE
VASGEIGEQI KQQIIEKAQV RPIAFFARGP RNLTSQRPIT SPADLDGMKM RVPNVPLFVD
VWSALGASPT PMAFSEVFTS LQNGVIDGQE NPLALIRSAN FNEVQGYVNQ TEHVRSWIYL
TIAESTWAKL SEDDQNAVMQ AAATAQEYER GLLLESLAED RGYLESKGMT FVEVDGAAFQ
AAAKDAVLAN VSEEIRPIVE SLFSE
