DPPD_SHIFL
ID DPPD_SHIFL Reviewed; 327 AA.
AC P0AAG2; P37314;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=SF3576, S4194;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Part of the ABC transporter DppABCDF 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 -!- 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). {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; AE005674; AAN45027.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19161.1; -; Genomic_DNA.
DR RefSeq; NP_709320.1; NC_004337.2.
DR RefSeq; WP_001196486.1; NZ_WPGW01000020.1.
DR AlphaFoldDB; P0AAG2; -.
DR SMR; P0AAG2; -.
DR STRING; 198214.SF3576; -.
DR DNASU; 1080400; -.
DR EnsemblBacteria; AAN45027; AAN45027; SF3576.
DR EnsemblBacteria; AAP19161; AAP19161; S4194.
DR GeneID; 1026341; -.
DR GeneID; 66672571; -.
DR KEGG; sfl:SF3576; -.
DR KEGG; sfx:S4194; -.
DR PATRIC; fig|198214.7.peg.4219; -.
DR HOGENOM; CLU_000604_1_23_6; -.
DR OMA; GSMPRID; -.
DR OrthoDB; 1101128at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 DppD"
FT /id="PRO_0000092316"
FT DOMAIN 4..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 327 AA; 35844 MW; 1CBFD72388EE0569 CRC64;
MALLNVDKLS VHFGDESAPF RAVDRISYSV KQGEVVGIVG ESGSGKSVSS LAIMGLIDYP
GRVMAEKLEF NGQDLQRISE KERRNLVGAE VAMIFQDPMT SLNPCYTVGF QIMEAIKVHQ
GGNKSTRRQR AIDLLNQVGI PDPASRLDVY PHQLSGGMSQ RVMIAMAIAC RPKLLIADEP
TTALDVTIQA QIIELLLELQ QKENMALVLI THDLALVAEA AHKIIVMYAG QVVETGDAHA
IFHAPRHPYT QALLRALPEF AQDKERLASL PGVVPGKYDR PNGCLLNPRC PYATDRCRAE
EPALNMLADG RQSKCHYPLD DAGRPTL
