DPPA_LACLM
ID DPPA_LACLM Reviewed; 550 AA.
AC A2RI74; Q93QH8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Dipeptide-binding protein {ECO:0000305};
DE Flags: Precursor;
GN Name=dppA {ECO:0000303|PubMed:10769143};
GN OrderedLocusNames=llmg_0362 {ECO:0000312|EMBL:CAL96967.1};
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=MG1363;
RX PubMed=11409543; DOI=10.1007/s002030100270;
RA Sanz Y., Lanfermeijer F.C., Renault P., Bolotin A., Konings W.N.,
RA Poolman B.;
RT "Genetic and functional characterization of dpp genes encoding a dipeptide
RT transport system in Lactococcus lactis.";
RL Arch. Microbiol. 175:334-343(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [3]
RP FUNCTION.
RC STRAIN=MG1363;
RX PubMed=10769143; DOI=10.1021/bi992720s;
RA Sanz Y., Lanfermeijer F.C., Konings W.N., Poolman B.;
RT "Kinetics and structural requirements for the binding protein of the Di-
RT tripeptide transport system of Lactococcus lactis.";
RL Biochemistry 39:4855-4862(2000).
CC -!- FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide
CC transport (PubMed:11409543). Binds di- and tripeptides with high
CC affinity. Requires a free N-terminal alpha-amino group and an alpha-
CC peptide bound contiguous with the N-terminal amino group, has a strong
CC selectivity for L-residues, and shows preference for dipeptides
CC containing methionine or arginine, followed by hydrophobic tripeptides
CC consisting of leucine or valine residues (PubMed:10769143).
CC {ECO:0000269|PubMed:10769143, ECO:0000269|PubMed:11409543}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (DppD and
CC DppF), two transmembrane proteins (DppB and DppC) and a solute-binding
CC protein (DppA). {ECO:0000305|PubMed:11409543}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:11409543}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Expression is regulated by the peptide content of the growth
CC media. {ECO:0000269|PubMed:11409543}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene impairs growth on low
CC concentrations of di-valine. {ECO:0000269|PubMed:11409543}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; AF247635; AAK58896.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL96967.1; -; Genomic_DNA.
DR RefSeq; WP_011834420.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RI74; -.
DR SMR; A2RI74; -.
DR STRING; 416870.llmg_0362; -.
DR EnsemblBacteria; CAL96967; CAL96967; llmg_0362.
DR KEGG; llm:llmg_0362; -.
DR eggNOG; COG4166; Bacteria.
DR HOGENOM; CLU_017028_0_4_9; -.
DR OMA; SSWGDPQ; -.
DR PhylomeDB; A2RI74; -.
DR BioCyc; LLAC416870:LLMG_RS01865-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProt.
DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Peptide transport;
KW Protein transport; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..550
FT /note="Dipeptide-binding protein"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5002645778"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 550 AA; 59910 MW; CC7C843C779387DB CRC64;
MKQAKIIGLS TVIALSGIIL VACGSKTSEQ KNIQFSIPTD VASLDTTILT DQYSYDVAGN
VEEGLTRVDS KGNAALALAK SIDVSKDGLT YTVTLKDNLK WSNGDKLTAK DFVYSWKRAV
DPKTGSEYAY LMGAVSGAND IISGKSSLDT LGIKAESDTE FTVTLAQPTP YFKFLLSEPV
YYPLDQKVVD KYGKQYGTSS DKTVYNGPFM FKSDKAWTGT NKNFSIYANP NYYDKSAVKS
KQIDFQVISN ANTGAQLYKQ GKLDFTLLST TDLINANKKT EGYTVFKQAR TDYIEYNQSG
KNASSPDAQK ALANQDIRQA LNLATNRAEV VKTALPGSTA ATSFTPVGMS KTSTGEDFAT
YAKQDYSYDP TKAKELWAKG LKELGLTKLS LSLEAAGDLA PSEATANFLQ TAYQQNLPGL
TVNLKLVPFK QRLNDAQNGN FDMVLSGWGG DYAEPSTFLQ LFTTGQSYND GKFSSKTYDD
AFKAATTTPD VLEPAKVDEH YKAAEAALYE GSYINPIDFQ ANPALMNPKI TGLEFHSTGL
AYDLKSAYIK
