ID   DPPE_BACSU              Reviewed;         543 AA.
AC   P26906; O34801;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 4.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Dipeptide-binding protein DppE;
DE   Flags: Precursor;
GN   Name=dppE; Synonyms=dciAE; OrderedLocusNames=BSU12960;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=1766370; DOI=10.1111/j.1365-2958.1991.tb00814.x;
RA   Mathiopoulos C., Mueller J.P., Slack F.J., Murphy C.G., Patankar S.,
RA   Bukusoglu G., Sonenshein A.L.;
RT   "A Bacillus subtilis dipeptide transport system expressed early during
RT   sporulation.";
RL   Mol. Microbiol. 5:1903-1913(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Devine K.M.;
RT   "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 339.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Probably part of the ABC transporter DppBCDE involved in
CC       dipeptide transport. {ECO:0000305|PubMed:1766370}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed early during sporulation.
CC   -!- INDUCTION: Nutrient deficiency conditions.
CC   -!- DISRUPTION PHENOTYPE: A null mutation abolishes the ability of a
CC       proline auxotroph to grow in a medium containing the dipeptide Pro-Gly
CC       as sole proline source. {ECO:0000269|PubMed:1766370}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA05576.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAB13153.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X56678; CAA40006.1; -; Genomic_DNA.
DR   EMBL; AJ002571; CAA05576.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB13153.2; ALT_INIT; Genomic_DNA.
DR   PIR; G69618; G69618.
DR   RefSeq; NP_389179.2; NC_000964.3.
DR   AlphaFoldDB; P26906; -.
DR   SMR; P26906; -.
DR   STRING; 224308.BSU12960; -.
DR   TCDB; 3.A.1.5.2; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P26906; -.
DR   PRIDE; P26906; -.
DR   EnsemblBacteria; CAB13153; CAB13153; BSU_12960.
DR   GeneID; 938099; -.
DR   KEGG; bsu:BSU12960; -.
DR   PATRIC; fig|224308.179.peg.1408; -.
DR   eggNOG; COG4166; Bacteria.
DR   InParanoid; P26906; -.
DR   BioCyc; BSUB:BSU12960-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Peptide transport;
KW   Protein transport; Reference proteome; Signal; Sporulation; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..543
FT                   /note="Dipeptide-binding protein DppE"
FT                   /id="PRO_0000031788"
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"
FT   CONFLICT        339
FT                   /note="P -> T (in Ref. 2; CAA05576)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   543 AA;  61819 MW;  9554DDA6F8FDE528 CRC64;
     MKRVKKLWGM GLALGLSFAL MGCTANEQAG KEGSHDKAKT SGEKVLYVNN ENEPTSFDPP
     IGFNNVSWQP LNNIMEGLTR LGKDHEPEPA MAEKWSVSKD NKTYTFTIRE NAKWTNGDPV
     TAGDFEYAWK RMLDPKKGAS SAFLGYFIEG GEAYNSGKGK KDDVKVTAKD DRTLEVTLEA
     PQKYFLSVVS NPAYFPVNEK VDKDNPKWFA ESDTFVGNGP FKLTEWKHDD SITMEKSDTY
     WDKDTVKLDK VKWAMVSDRN TDYQMFQSGE LDTAYVPAEL SDQLLDQDNV NIVDQAGLYF
     YRFNVNMEPF QNENIRKAFA MAVDQEEIVK YVTKNNEKPA HAFVSPGFTQ PDGKDFREAG
     GDLIKPNESK AKQLLEKGMK EENYNKLPAI TLTYSTKPEH KKIAEAIQQK LKNSLGVDVK
     LANMEWNVFL EDQKALKFQF SQSSFLPDYA DPISFLEAFQ TGNSMNRTGW ANKEYDQLIK
     QAKNEADEKT RFSLMHQAEE LLINEAPIIP VYFYNQVHLQ NEQVKGIVRH PVGYIDLKWA
     DKN