ID   DPPF_HAEIN              Reviewed;         327 AA.
AC   P45094;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Dipeptide transport ATP-binding protein DppF {ECO:0000250|UniProtKB:P37313};
DE            EC=7.4.2.9 {ECO:0000250|UniProtKB:P37313};
GN   Name=dppF; OrderedLocusNames=HI_1184;
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:P37313}.
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:P37313};
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; AAC22837.1; -; Genomic_DNA.
DR   EMBL; U17295; AAA95975.1; -; Genomic_DNA.
DR   PIR; E64188; E64188.
DR   RefSeq; NP_439340.1; NC_000907.1.
DR   RefSeq; WP_005691143.1; NC_000907.1.
DR   AlphaFoldDB; P45094; -.
DR   SMR; P45094; -.
DR   STRING; 71421.HI_1184; -.
DR   TCDB; 3.A.1.5.27; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; AAC22837; AAC22837; HI_1184.
DR   KEGG; hin:HI_1184; -.
DR   PATRIC; fig|71421.8.peg.1235; -.
DR   eggNOG; COG4608; Bacteria.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; GRYPHMF; -.
DR   PhylomeDB; P45094; -.
DR   BioCyc; HINF71421:G1GJ1-1215-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..327
FT                   /note="Dipeptide transport ATP-binding protein DppF"
FT                   /id="PRO_0000092318"
FT   DOMAIN          12..261
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         54..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   327 AA;  36917 MW;  0BB0BBDE197DA9BE CRC64;
     MTNEVKENTP LLNAIGLKKY YPVKKGLFAK PQQVKALDGV SFQLERGKTL AVVGESGCGK
     STLGRLLTMI EEPTKGELYY KGHNFLENDS ETKALRRKKI QIVFQNPYAS LNPRKKIGSI
     LEEPLIINTK LSAKERREKV LSMMEKVGLR AEFYDRYPHM FSGGQRQRIA IARGLMLDPD
     VVVADEPVSA LDVSVRAQVL NLMMDLQDEL GLSYVFISHD LSVVEHIADE VMVMYLGRCI
     EKGTTEQIFS NPQHPYTKAL LSATPRLSPN LRRERIKLTG ELPSPINPPK GCAFNPRCWK
     ATEKCRENQP HLEQHTDGKL IACFHID