ID   DPPD_HAEIN              Reviewed;         330 AA.
AC   P45095;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Dipeptide transport ATP-binding protein DppD {ECO:0000250|UniProtKB:P0AAG0};
DE            EC=7.4.2.9 {ECO:0000250|UniProtKB:P0AAG0};
GN   Name=dppD; OrderedLocusNames=HI_1185;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=8550458; DOI=10.1128/jb.178.2.396-402.1996;
RA   Preston A., Maskell D., Johnson A., Moxon E.R.;
RT   "Altered lipopolysaccharide characteristic of the I69 phenotype in
RT   Haemophilus influenzae results from mutations in a novel gene, isn.";
RL   J. Bacteriol. 178:396-402(1996).
CC   -!- FUNCTION: Part of the ABC transporter DppBCDF involved in dipeptide
CC       transport. Responsible for energy coupling to the transport system.
CC       {ECO:0000250|UniProtKB:P0AAG0}.
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:P0AAG0};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; L42023; AAC22838.1; -; Genomic_DNA.
DR   EMBL; U17295; AAA95974.1; -; Genomic_DNA.
DR   PIR; F64188; F64188.
DR   RefSeq; NP_439341.1; NC_000907.1.
DR   RefSeq; WP_005694258.1; NC_000907.1.
DR   AlphaFoldDB; P45095; -.
DR   SMR; P45095; -.
DR   STRING; 71421.HI_1185; -.
DR   TCDB; 3.A.1.5.27; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; AAC22838; AAC22838; HI_1185.
DR   KEGG; hin:HI_1185; -.
DR   PATRIC; fig|71421.8.peg.1236; -.
DR   eggNOG; COG0444; Bacteria.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; GSMPRID; -.
DR   PhylomeDB; P45095; -.
DR   BioCyc; HINF71421:G1GJ1-1216-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..330
FT                   /note="Dipeptide transport ATP-binding protein DppD"
FT                   /id="PRO_0000092315"
FT   DOMAIN          6..254
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   330 AA;  36328 MW;  964801E58D5656DE CRC64;
     MALLDVKELS VHFGDKKTPF KAVDRISYQV AQGEVLGIVG ESGSGKSVSS LAIMGLIDHP
     GRVSAESLQF ENTDLLTLES KAKRQLIGAD VAMIFQDPMT SLNPAYTVGF QIMEALKTHE
     GGTKKARKDR TLELLKLVGI PDPESRIDVY PHQLSGGMSQ RVMIAMAIAC RPKLLIADEP
     TTALDVTIQA QIMELLLELQ KKECMSLILI THDLALVAEA AERIIVMYAG QIVEEGTAKD
     IFREPKHPYT QALLRSLPEF AEGKSRLESL QGVVPGKYDR PTGCLLNPRC PYATEYCRQV
     EPQLHHIGSR KVKCHTPLNE QGNPVEYQGA