ID   DPPB_LACLM              Reviewed;         303 AA.
AC   A2RI75; Q93QH6;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Dipeptide transport system permease protein DppB {ECO:0000305};
GN   Name=dppB {ECO:0000303|PubMed:11409543};
GN   OrderedLocusNames=llmg_0364 {ECO:0000312|EMBL:CAL96969.1};
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, AND DISRUPTION
RP   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).
CC   -!- FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide
CC       transport (PubMed:11409543). Responsible for the translocation of the
CC       substrate across the membrane (Probable). {ECO:0000269|PubMed:11409543,
CC       ECO:0000305}.
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:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
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 binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK58898.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF247635; AAK58898.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AM406671; CAL96969.1; -; Genomic_DNA.
DR   RefSeq; WP_011834421.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; A2RI75; -.
DR   SMR; A2RI75; -.
DR   STRING; 416870.llmg_0364; -.
DR   EnsemblBacteria; CAL96969; CAL96969; llmg_0364.
DR   GeneID; 61108668; -.
DR   KEGG; llm:llmg_0364; -.
DR   eggNOG; COG0601; Bacteria.
DR   HOGENOM; CLU_036879_1_2_9; -.
DR   OMA; FLMVNVM; -.
DR   PhylomeDB; A2RI75; -.
DR   BioCyc; LLAC416870:LLMG_RS01875-MON; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR045621; BPD_transp_1_N.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF19300; BPD_transp_1_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Peptide transport; Protein transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..303
FT                   /note="Dipeptide transport system permease protein DppB"
FT                   /id="PRO_0000452193"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          93..290
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   CONFLICT        201..203
FT                   /note="DYI -> ELH (in Ref. 1; AAK58898)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  33237 MW;  92E84B8DFF573994 CRC64;
     MVKYILKRLG LLLLTLFLIV TLTFFMMQVM PGTPFSNPKL TPDQLEILKH AYGLDKPLWQ
     QYFIYVGHMF TGNFGTSFIY TNQPVITMIA QRLPVSMQLG TQALILGTVL GALMGKASAR
     RKNGLLDGIF GFLSVLGISV PSFVIGTLIL LYLGFNLNLF PISGWGTFSQ TIMPTIALSF
     APMAVVTRFV RSEMIESLSS DYILLARAKG LSEKEVVNKH ALRNSLIPML TLIGPMAAGL
     LTGSVLIEKI FSIPGIGAQF VDSIPAKDFP VIMATTIVYA VILMVFILVT DILTAIVDPR
     VRL