DPPB_BACSU
ID DPPB_BACSU Reviewed; 308 AA.
AC P26903;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Dipeptide transport system permease protein DppB;
GN Name=dppB; Synonyms=dciAB; OrderedLocusNames=BSU12930;
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 the translocation of
CC the substrate across the membrane (Probable). {ECO:0000305,
CC ECO:0000305|PubMed:1766370}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- DEVELOPMENTAL STAGE: Expressed early during sporulation.
CC -!- INDUCTION: Nutrient deficiency conditions, which also induce
CC sporulation.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X56678; CAA40003.1; -; Genomic_DNA.
DR EMBL; AJ002571; CAA05573.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13150.1; -; Genomic_DNA.
DR PIR; S16648; S16648.
DR RefSeq; NP_389176.1; NC_000964.3.
DR RefSeq; WP_003245446.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P26903; -.
DR SMR; P26903; -.
DR STRING; 224308.BSU12930; -.
DR TCDB; 3.A.1.5.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P26903; -.
DR PRIDE; P26903; -.
DR EnsemblBacteria; CAB13150; CAB13150; BSU_12930.
DR GeneID; 939881; -.
DR KEGG; bsu:BSU12930; -.
DR PATRIC; fig|224308.179.peg.1405; -.
DR eggNOG; COG0601; Bacteria.
DR InParanoid; P26903; -.
DR OMA; IFTAQYT; -.
DR PhylomeDB; P26903; -.
DR BioCyc; BSUB:BSU12930-MON; -.
DR Proteomes; UP000001570; 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:0030435; P:sporulation resulting in formation of a cellular spore; 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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..308
FT /note="Dipeptide transport system permease protein DppB"
FT /id="PRO_0000060003"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 94..295
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 308 AA; 34056 MW; 015C0F43D89C376B CRC64;
MARYMIKRFW AMAATILVIT TLTFVLMKVI PGSPFNEERG TNEAVQKNLE AYYHLDDPLI
FQYIFYLKSI ITFDFGPSIK KPSDSVNDML ERGFPVSFEL GMTAIVIAVI SGLVLGVIAA
LRRNGFLDYA AMSLAVLGIS IPNFILATLL IQQFAVNLKL FPAATWTSPI HMVLPTAALA
VGPMAIIARL TRSSMVEVLT QDYIRTAKAK GLSPFKIIVK HALRNALMPV ITVLGTLVAS
ILTGSFVIEK IFAIPGMGKY FVESINQRDY PVIMGTTVFY SVILIIMLFL VDLAYGLLDP
RIKLHKKG
