DCTP_ALBFT
ID DCTP_ALBFT Reviewed; 338 AA.
AC Q21XD7;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Solute-binding protein Rfer_1840 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=Rfer_1840 {ECO:0000312|EMBL:ABD69566.1};
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969 {ECO:0000312|EMBL:ABD69566.1};
RN [1] {ECO:0000312|Proteomes:UP000008332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118 {ECO:0000312|Proteomes:UP000008332};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH MALONATE, AND
RP 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 malonate (in vitro)
CC (PubMed:25540822). Probably part of a tripartite ATP-independent
CC periplasmic (TRAP) transport system that mediates solute transport into
CC the cytoplasm. {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}.
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DR EMBL; CP000267; ABD69566.1; -; Genomic_DNA.
DR RefSeq; WP_011464134.1; NC_007908.1.
DR PDB; 4MCO; X-ray; 1.60 A; A/B/C=1-338.
DR PDB; 4MEV; X-ray; 1.80 A; A=1-338.
DR PDBsum; 4MCO; -.
DR PDBsum; 4MEV; -.
DR AlphaFoldDB; Q21XD7; -.
DR SMR; Q21XD7; -.
DR STRING; 338969.Rfer_1840; -.
DR EnsemblBacteria; ABD69566; ABD69566; Rfer_1840.
DR KEGG; rfr:Rfer_1840; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_1_3_4; -.
DR OMA; HQFPGGT; -.
DR OrthoDB; 752834at2; -.
DR Proteomes; UP000008332; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..338
FT /note="Solute-binding protein Rfer_1840"
FT /evidence="ECO:0000255"
FT /id="PRO_5004200133"
FT BINDING 47
FT /ligand="malonate"
FT /ligand_id="ChEBI:CHEBI:15792"
FT /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT BINDING 100
FT /ligand="malonate"
FT /ligand_id="ChEBI:CHEBI:15792"
FT /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT BINDING 175
FT /ligand="malonate"
FT /ligand_id="ChEBI:CHEBI:15792"
FT /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT BINDING 197
FT /ligand="malonate"
FT /ligand_id="ChEBI:CHEBI:15792"
FT /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT BINDING 214..218
FT /ligand="malonate"
FT /ligand_id="ChEBI:CHEBI:15792"
FT /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT BINDING 244
FT /ligand="malonate"
FT /ligand_id="ChEBI:CHEBI:15792"
FT /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:4MCO"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 151..161
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 258..292
FT /evidence="ECO:0007829|PDB:4MCO"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:4MCO"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:4MCO"
SQ SEQUENCE 338 AA; 36911 MW; 5FBCDB16858DE50C CRC64;
MQRRQLLQSM GGLAASTMPF SLAFAQTSAL KISHQFPGGT IKEGDFRDRL VRNFAAEVEK
RSKGAMKFEI YPGSSLMKTN AQFSSMRKGA LDMALIPLSY AGGEVPELNI GLMPGLVVSY
EQAYSWKTKP VGIELTRVLQ EKGIVLISWI WQAGGVASRG KPVVEPEDAK GMKIRGGSRE
MDMILKDAGA AVVSLPSNEI YAAMQTGAMD AAMTSSTSFI SFRLEEVAKA LTTGRTGAYW
FMFEPLMMSK AIFDKLPKDQ RDMLMTVGAE MEKFALEAAK KDDIDVAAVY QKAGAKVVDL
SDGTIKKWQD IARKTAWKDY GAKNEGCAKL LALAQQTL