DCTP2_POLSJ
ID DCTP2_POLSJ Reviewed; 325 AA.
AC Q122C7;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Solute-binding protein Bpro_4736 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=Bpro_4736 {ECO:0000312|EMBL:ABE46615.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000312|EMBL:ABE46615.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
RN [2] {ECO:0007744|PDB:4MNC, ECO:0007744|PDB:4MNI}
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH PHENYLGLYOXYLATE,
RP 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 phenylglyoxylate (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; CP000316; ABE46615.1; -; Genomic_DNA.
DR RefSeq; WP_011485600.1; NC_007948.1.
DR PDB; 4MNC; X-ray; 1.05 A; A=1-325.
DR PDB; 4MNI; X-ray; 1.90 A; A=1-325.
DR PDBsum; 4MNC; -.
DR PDBsum; 4MNI; -.
DR AlphaFoldDB; Q122C7; -.
DR SMR; Q122C7; -.
DR STRING; 296591.Bpro_4736; -.
DR EnsemblBacteria; ABE46615; ABE46615; Bpro_4736.
DR KEGG; pol:Bpro_4736; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_068413_0_0_4; -.
DR OMA; VDGYGWP; -.
DR OrthoDB; 1251304at2; -.
DR Proteomes; UP000001983; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..325
FT /note="Solute-binding protein Bpro_4736"
FT /evidence="ECO:0000255"
FT /id="PRO_5004180668"
FT BINDING 168..173
FT /ligand="phenylglyoxylate"
FT /ligand_id="ChEBI:CHEBI:36656"
FT /evidence="ECO:0007744|PDB:4MNC, ECO:0007744|PDB:4MNI"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:4MNC"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:4MNC"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4MNC"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:4MNC"
FT TURN 211..215
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 266..280
FT /evidence="ECO:0007829|PDB:4MNC"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 290..311
FT /evidence="ECO:0007829|PDB:4MNC"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:4MNC"
SQ SEQUENCE 325 AA; 36236 MW; AB0CF09823071CD8 CRC64;
MKTRTLKVLK PTLALLLAAS FSAGALAQEV TLRLVSAFPE NGIYVQRLLP WIAKVNAEGK
GVLQINFLGG PKAIPTFEAG NAVKTGVVDM AMNTGAFYTN VMPEADFLKL TQIPVAEQRK
NGAFDAINKV WNEKGNTQYL ARMVENQPFH IYTNKKIDKP DLSGQKIRIS PVYRDFFQAL
NANVVTTPPG EVYTALERGV VDGYGWPIGG IFDLNWQEKT KFRVDPGFYD AEVSLTMNLP
AYKKLTDAQR NYLQKQLLVL EAENTFWTRY GNVETARQET AGIQTIKFDA ATSKAFREKA
YEVGWAGAMK QSPEVAARFK TLFSK
