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DPPC_BACSU
ID   DPPC_BACSU              Reviewed;         320 AA.
AC   P26904; O34373; Q45678;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Dipeptide transport system permease protein DppC;
GN   Name=dppC; Synonyms=dciAC; OrderedLocusNames=BSU12940;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-85.
RX   PubMed=3145906; DOI=10.1016/0378-1119(88)90207-7;
RA   Smith H., de Jong A., Bron S., Venema G.;
RT   "Characterization of signal-sequence-coding regions selected from the
RT   Bacillus subtilis chromosome.";
RL   Gene 70:351-361(1988).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22823.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; X56678; CAA40004.1; -; Genomic_DNA.
DR   EMBL; AJ002571; CAA05574.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13151.1; -; Genomic_DNA.
DR   EMBL; M22907; AAA22823.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S16649; S16649.
DR   RefSeq; NP_389177.1; NC_000964.3.
DR   RefSeq; WP_003245702.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P26904; -.
DR   STRING; 224308.BSU12940; -.
DR   TCDB; 3.A.1.5.2; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P26904; -.
DR   PRIDE; P26904; -.
DR   EnsemblBacteria; CAB13151; CAB13151; BSU_12940.
DR   GeneID; 938038; -.
DR   KEGG; bsu:BSU12940; -.
DR   PATRIC; fig|224308.179.peg.1406; -.
DR   eggNOG; COG1173; Bacteria.
DR   InParanoid; P26904; -.
DR   OMA; TDWFLVM; -.
DR   PhylomeDB; P26904; -.
DR   BioCyc; BSUB:BSU12940-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; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR025966; OppC_N.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF12911; OppC_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..320
FT                   /note="Dipeptide transport system permease protein DppC"
FT                   /id="PRO_0000060004"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        154..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        230..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          117..307
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   CONFLICT        232
FT                   /note="P -> R (in Ref. 1; CAA40004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="L -> S (in Ref. 1; CAA40004)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35803 MW;  F376C504CC1DA729 CRC64;
     MNLPVQTDER QPEQHNQVPD EWFVLNQEKN READSVKRPS LSYTQDAWRR LKKNKLAMAG
     LFILLFLFVM AVIGPFLSPH SVVRQSLTEQ NLPPSADHWF GTDELGRDVF TRTWYGARIS
     LFVGVMAALI DFLIGVIYGG VAGYKGGRID SIMMRIIEVL YGLPYLLVVI LLMVLMGPGL
     GTIIVALTVT GWVGMARIVR GQVLQIKNYE YVLASKTFGA KTFRIIRKNL LPNTMGAIIV
     QMTLTVPAAI FAESFLSFLG LGIQAPFASW GVMANDGLPT ILSGHWWRLF FPAFFISLTM
     YAFNVLGDGL QDALDPKLRR
 
 
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