DCTP_SHELP
ID DCTP_SHELP Reviewed; 336 AA.
AC A3QCW5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=C4-dicarboxylate-binding periplasmic protein DctP {ECO:0000305};
DE Flags: Precursor;
GN Name=dctP {ECO:0000250|UniProtKB:Q9HU18};
GN OrderedLocusNames=Shew_1446 {ECO:0000312|EMBL:ABO23313.1};
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850 {ECO:0000312|EMBL:ABO23313.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION [LARGE SCALE ANALYSIS], AND SUBUNIT.
RX PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL Nature 557:503-509(2018).
RN [3] {ECO:0007744|PDB:4O7M, ECO:0007744|PDB:4OA4}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 32-336 IN COMPLEXES WITH
RP SUCCINATE AND (S)-MALATE, 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: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system DctPQM involved in C4-dicarboxylates uptake (By
CC similarity). Required for the utilization of succinate, fumarate, L-
CC malate and alpha-ketoglutarate (PubMed:29769716). Binds succinate and
CC malate (PubMed:25540822). {ECO:0000250|UniProtKB:Q9HU18,
CC ECO:0000269|PubMed:25540822, ECO:0000269|PubMed:29769716}.
CC -!- SUBUNIT: The complex comprises the extracytoplasmic solute receptor
CC protein DctP, and the two transmembrane proteins DctQ and DctM.
CC {ECO:0000250|UniProtKB:Q9HU18, ECO:0000305|PubMed:29769716}.
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; CP000606; ABO23313.1; -; Genomic_DNA.
DR RefSeq; WP_011865245.1; NC_009092.1.
DR PDB; 4O7M; X-ray; 1.50 A; A/B/C/D=32-336.
DR PDB; 4OA4; X-ray; 1.60 A; A/B/C/D=32-336.
DR PDBsum; 4O7M; -.
DR PDBsum; 4OA4; -.
DR AlphaFoldDB; A3QCW5; -.
DR SMR; A3QCW5; -.
DR STRING; 323850.Shew_1446; -.
DR EnsemblBacteria; ABO23313; ABO23313; Shew_1446.
DR KEGG; slo:Shew_1446; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_1_3_6; -.
DR OMA; AFWHNGM; -.
DR OrthoDB; 752834at2; -.
DR Proteomes; UP000001558; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
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; 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; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..336
FT /note="C4-dicarboxylate-binding periplasmic protein DctP"
FT /id="PRO_5002656810"
FT BINDING 48
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4O7M"
FT BINDING 48
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OA4"
FT BINDING 101
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4O7M"
FT BINDING 101
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OA4"
FT BINDING 176
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4O7M"
FT BINDING 176
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OA4"
FT BINDING 216
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4O7M"
FT BINDING 216
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OA4"
FT BINDING 220
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4O7M"
FT BINDING 220
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OA4"
FT BINDING 243
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4O7M"
FT BINDING 243
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OA4"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:4O7M"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4O7M"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4O7M"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 145..162
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:4O7M"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 231..248
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 257..292
FT /evidence="ECO:0007829|PDB:4O7M"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:4O7M"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:4O7M"
SQ SEQUENCE 336 AA; 37603 MW; A7BDA58F75F137FA CRC64;
MTRLNTCTFI KQIVKMTSIA ALLGASLNSW AAPTEIKFSH VVAENTPKGQ MALKFKQLVE
ERLPGEYQVN VFPNSQLFGD NNELSALLLN DVQFVAPSLS KFERYTKKLQ LFDLPFLFKD
MDAVNRFQQS DAGQQLLNSM KRKGVVGLGY LHNGMKQFSA SSPLVLPEDA QGKKFRIMAS
DVLAAQFQAV EAIPVKKPFS EVFTLLQTRA IDGQENTWSN IYSKKFYEVQ SNITESNHGV
LDYMVVTSNT FWKSLPADKR KVIKASLDEA IAYGNEIAAA KVNKDKQAII DSKRSEVTYL
TPEQRAAWVN AMKPVWAQFE DKIGKDLIDA AVASNE
