ID   DPPB_ECOLI              Reviewed;         339 AA.
AC   P0AEF8; P37316; Q2M7K5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Dipeptide transport system permease protein DppB {ECO:0000305};
GN   Name=dppB; OrderedLocusNames=b3543, JW3512;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=K12 / MM500;
RX   PubMed=7536291; DOI=10.1111/j.1365-2958.1994.tb01340.x;
RA   Abouhamad W.N., Manson M.D.;
RT   "The dipeptide permease of Escherichia coli closely resembles other
RT   bacterial transport systems and shows growth-phase-dependent expression.";
RL   Mol. Microbiol. 14:1077-1092(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION IN 5-AMINOLEVULINIC ACID TRANSPORT.
RX   PubMed=8444807; DOI=10.1128/jb.175.5.1452-1456.1993;
RA   Verkamp E., Backman V.M., Bjoernsson J.M., Soell D., Eggertsson G.;
RT   "The periplasmic dipeptide permease system transports 5-aminolevulinic acid
RT   in Escherichia coli.";
RL   J. Bacteriol. 175:1452-1456(1993).
RN   [6]
RP   TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [7]
RP   FUNCTION IN HEME TRANSPORT, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX   PubMed=16905647; DOI=10.1073/pnas.0605440103;
RA   Letoffe S., Delepelaire P., Wandersman C.;
RT   "The housekeeping dipeptide permease is the Escherichia coli heme
RT   transporter and functions with two optional peptide binding proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:12891-12896(2006).
CC   -!- FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide
CC       transport (PubMed:7536291). Responsible for the translocation of the
CC       substrate across the membrane (Probable). {ECO:0000269|PubMed:7536291,
CC       ECO:0000305}.
CC   -!- FUNCTION: When a foreign outer membrane heme receptor is expressed in
CC       E.coli, DppABCDF can also transport heme and its precursor, 5-
CC       aminolevulinic acid (ALA), from the periplasm into the cytoplasm.
CC       {ECO:0000269|PubMed:16905647, ECO:0000269|PubMed:8444807}.
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) (PubMed:7536291, PubMed:16905647). MppA can replace DppA
CC       as binding protein for heme and ALA transport (PubMed:16905647).
CC       {ECO:0000269|PubMed:16905647, ECO:0000269|PubMed:7536291}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of the gene abolishes use of heme as
CC       an iron source. {ECO:0000269|PubMed:16905647}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
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DR   EMBL; L08399; AAA23703.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18521.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76568.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77751.1; -; Genomic_DNA.
DR   PIR; S47765; S47765.
DR   RefSeq; NP_418000.1; NC_000913.3.
DR   RefSeq; WP_000938855.1; NZ_STEB01000018.1.
DR   AlphaFoldDB; P0AEF8; -.
DR   SMR; P0AEF8; -.
DR   BioGRID; 4262535; 186.
DR   BioGRID; 852371; 1.
DR   ComplexPortal; CPX-4345; Heme/dipeptide ABC transporter complex, dppA variant.
DR   ComplexPortal; CPX-4346; Heme/dipeptide ABC transporter complex, mppA variant.
DR   DIP; DIP-47927N; -.
DR   IntAct; P0AEF8; 2.
DR   STRING; 511145.b3543; -.
DR   jPOST; P0AEF8; -.
DR   PaxDb; P0AEF8; -.
DR   PRIDE; P0AEF8; -.
DR   EnsemblBacteria; AAC76568; AAC76568; b3543.
DR   EnsemblBacteria; BAE77751; BAE77751; BAE77751.
DR   GeneID; 66672569; -.
DR   GeneID; 948063; -.
DR   KEGG; ecj:JW3512; -.
DR   KEGG; eco:b3543; -.
DR   PATRIC; fig|1411691.4.peg.3172; -.
DR   EchoBASE; EB2509; -.
DR   eggNOG; COG0601; Bacteria.
DR   HOGENOM; CLU_036879_0_0_6; -.
DR   InParanoid; P0AEF8; -.
DR   OMA; WPGMGTF; -.
DR   PhylomeDB; P0AEF8; -.
DR   BioCyc; EcoCyc:DPPB-MON; -.
DR   BioCyc; MetaCyc:DPPB-MON; -.
DR   PRO; PR:P0AEF8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0042938; P:dipeptide transport; IC:ComplexPortal.
DR   GO; GO:0035351; P:heme transmembrane transport; IC:ComplexPortal.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 inner membrane; Cell membrane; Membrane; Peptide transport;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..339
FT                   /note="Dipeptide transport system permease protein DppB"
FT                   /id="PRO_0000060005"
FT   TOPO_DOM        1..9
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        31..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        124..135
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        157..171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        193..200
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        222..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        281..309
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        331..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          96..328
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   339 AA;  37497 MW;  B4B9D2965C365AD1 CRC64;
     MLQFILRRLG LVIPTFIGIT LLTFAFVHMI PGDPVMIMAG ERGISPERHA QLLAELGLDK
     PMWQQYLHYI WGVMHGDLGI SMKSRIPVWE EFVPRFQATL ELGVCAMIFA TAVGIPVGVL
     AAVKRGSIFD HTAVGLALTG YSMPIFWWGM MLIMLVSVHW NLTPVSGRVS DMVFLDDSNP
     LTGFMLIDTA IWGEDGNFID AVAHMILPAI VLGTIPLAVI VRMTRSSMLE VLGEDYIRTA
     RAKGLTRMRV IIVHALRNAM LPVVTVIGLQ VGTLLAGAIL TETIFSWPGL GRWLIDALQR
     RDYPVVQGGV LLVATMIILV NLLVDLLYGV VNPRIRHKK