DCTP_RUEPO
ID DCTP_RUEPO Reviewed; 327 AA.
AC Q5LSJ5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Solute-binding protein SPO1773 {ECO:0000305};
DE Flags: Precursor;
GN Name=dctP {ECO:0000305};
GN OrderedLocusNames=SPO1773 {ECO:0000312|EMBL:AAV95052.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000312|EMBL:AAV95052.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
RN [3] {ECO:0007744|PDB:4PAF, ECO:0007744|PDB:4PAI, ECO:0007744|PDB:4PBH}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH
RP 3,4-DIHYDROXYBENZOATE AND 3-HYDROXYBENZOATE, 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 3,4-dihydroxybenzoate and
CC 3-hydroxybenzoate (in vitro) (PubMed:25540822). Probably part of a
CC tripartite ATP-independent periplasmic (TRAP) transport system that
CC 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; CP000031; AAV95052.1; -; Genomic_DNA.
DR RefSeq; WP_011047506.1; NC_003911.12.
DR PDB; 4PAF; X-ray; 1.60 A; A=1-327.
DR PDB; 4PAI; X-ray; 1.40 A; A=1-327.
DR PDB; 4PBH; X-ray; 1.20 A; A=1-327.
DR PDBsum; 4PAF; -.
DR PDBsum; 4PAI; -.
DR PDBsum; 4PBH; -.
DR AlphaFoldDB; Q5LSJ5; -.
DR SMR; Q5LSJ5; -.
DR STRING; 246200.SPO1773; -.
DR EnsemblBacteria; AAV95052; AAV95052; SPO1773.
DR KEGG; sil:SPO1773; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_4_0_5; -.
DR OMA; IPTPQVF; -.
DR OrthoDB; 752834at2; -.
DR Proteomes; UP000001023; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; TAS:TIGR.
DR GO; GO:0015740; P:C4-dicarboxylate transport; TAS:TIGR.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..327
FT /note="Solute-binding protein SPO1773"
FT /id="PRO_5004259607"
FT BINDING 39..41
FT /ligand="3-hydroxybenzoate"
FT /ligand_id="ChEBI:CHEBI:16193"
FT /evidence="ECO:0007744|PDB:4PAF, ECO:0007744|PDB:4PAI"
FT BINDING 150
FT /ligand="3-hydroxybenzoate"
FT /ligand_id="ChEBI:CHEBI:16193"
FT /evidence="ECO:0007744|PDB:4PAF, ECO:0007744|PDB:4PAI"
FT BINDING 170..172
FT /ligand="3-hydroxybenzoate"
FT /ligand_id="ChEBI:CHEBI:16193"
FT /evidence="ECO:0007744|PDB:4PAF, ECO:0007744|PDB:4PAI"
FT BINDING 211
FT /ligand="3-hydroxybenzoate"
FT /ligand_id="ChEBI:CHEBI:16193"
FT /evidence="ECO:0007744|PDB:4PAF, ECO:0007744|PDB:4PAI"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:4PBH"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:4PBH"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 251..282
FT /evidence="ECO:0007829|PDB:4PBH"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:4PBH"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:4PBH"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:4PBH"
SQ SEQUENCE 327 AA; 34905 MW; 8C7E4BAC39D543C9 CRC64;
MTISFKGLAR GVACAALVLA ALPAAAKEFR LGLITPPPHT WTKAAEAFGA ELSEKSGGAH
SVSVFPARQL GNEAQMLQQL QTGALDMAFM TVAEVSNRVP NMGAFYAPYL AGDINHAAAI
LRSDTARGML AVLPQEAGVV GVGFGSAGMR QILSRGAVNS AADLSGLKLR ITPFDPILDF
YNALGAAPTP MPLPAVYDAL ANGQVDAIDM DVELINVLKY HEHADTILIS NHMMFPMVGL
ISARVYAGMS DADKAMISEL MAKHVDSTLD VYMVKEPEWT DALTKVGKTF KRVDQSFFGD
AIAQWETIWA DKAPSLPELR KTAADLQ