ID   DPPD_BACSU              Reviewed;         335 AA.
AC   P26905;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Dipeptide transport ATP-binding protein DppD;
DE            EC=7.4.2.9 {ECO:0000250|UniProtKB:A2RI77};
GN   Name=dppD; Synonyms=dciAD; OrderedLocusNames=BSU12950;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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).
CC   -!- FUNCTION: Probably part of the ABC transporter DppBCDE involved in
CC       dipeptide transport (Probable). Responsible for energy coupling to the
CC       transport system (Probable). {ECO:0000305, ECO:0000305|PubMed:1766370}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:23120, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:90799, ChEBI:CHEBI:456216; EC=7.4.2.9;
CC         Evidence={ECO:0000250|UniProtKB:A2RI77};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; X56678; CAA40005.1; -; Genomic_DNA.
DR   EMBL; AJ002571; CAA05575.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13152.1; -; Genomic_DNA.
DR   PIR; S16650; S16650.
DR   RefSeq; NP_389178.1; NC_000964.3.
DR   RefSeq; WP_003232615.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P26905; -.
DR   SMR; P26905; -.
DR   STRING; 224308.BSU12950; -.
DR   TCDB; 3.A.1.5.2; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P26905; -.
DR   PRIDE; P26905; -.
DR   EnsemblBacteria; CAB13152; CAB13152; BSU_12950.
DR   GeneID; 938628; -.
DR   KEGG; bsu:BSU12950; -.
DR   PATRIC; fig|224308.179.peg.1407; -.
DR   eggNOG; COG0444; Bacteria.
DR   InParanoid; P26905; -.
DR   OMA; VNCWLQD; -.
DR   PhylomeDB; P26905; -.
DR   BioCyc; BSUB:BSU12950-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
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   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR013563; Oligopep_ABC_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Peptide transport; Protein transport; Reference proteome; Sporulation;
KW   Translocase; Transport.
FT   CHAIN           1..335
FT                   /note="Dipeptide transport ATP-binding protein DppD"
FT                   /id="PRO_0000092312"
FT   DOMAIN          7..256
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   335 AA;  36681 MW;  86A49161878E681B CRC64;
     MEKVLSVQNL HVSFTTYGGT VQAVRGVSFD LYKGETFAIV GESGCGKSVT SQSIMGLLPP
     YSAKVTDGRI LFKNKDLCRL SDKEMRGIRG ADISMIFQDP MTALNPTLTV GDQLGEALLR
     HKKMSKKAAR KEVLSMLSLV GIPDPGERLK QYPHQFSGGM RQRIVIAMAL ICEPDILIAD
     EPTTALDVTI QAQILELFKE IQRKTDVSVI LITHDLGVVA QVADRVAVMY AGKMAEIGTR
     KDIFYQPQHP YTKGLLGSVP RLDLNGAELT PIDGTPPDLF SPPPGCPFAA RCPNRMVVCD
     RVYPGQTIRS DSHTVNCWLQ DQRAEHAVLS GDAKD