ID   OPPD_ECOLI              Reviewed;         337 AA.
AC   P76027; P77382;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   02-SEP-2026, entry version 179.
DE   RecName: Full=Oligopeptide transport ATP-binding protein OppD {ECO:0000305};
DE            EC=7.4.2.6 {ECO:0000305|PubMed:9495761};
GN   Name=oppD; OrderedLocusNames=b1246, JW1238;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
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   [3]
RP   SEQUENCE REVISION TO 2.
RX   PubMed=16397293; DOI=10.1093/nar/gkj405;
RA   Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA   Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA   Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA   Thomson N.R., Wishart D., Wanner B.L.;
RT   "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT   -- 2005.";
RL   Nucleic Acids Res. 34:1-9(2006).
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, AND SUBUNIT.
RC   STRAIN=K12 / AT980;
RX   PubMed=9495761; DOI=10.1128/jb.180.5.1215-1223.1998;
RA   Park J.T., Raychaudhuri D., Li H., Normark S., Mengin-Lecreulx D.;
RT   "MppA, a periplasmic binding protein essential for import of the bacterial
RT   cell wall peptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate.";
RL   J. Bacteriol. 180:1215-1223(1998).
CC   -!- FUNCTION: Part of the ABC transporter complex OppABCDF involved in the
CC       uptake of oligopeptides and of the ABC transporter complex MppA-OppBCDF
CC       involved in the uptake of the cell wall murein tripeptide L-alanyl-
CC       gamma-D-glutamyl-meso-diaminopimelate (PubMed:9495761). Probably
CC       responsible for energy coupling to the transport system (Probable).
CC       Plays an important nutritional role and is involved in the recycling of
CC       cell wall peptides (PubMed:9495761). {ECO:0000269|PubMed:9495761,
CC       ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a [peptide](out) + ATP + H2O = a [peptide](in) + ADP +
CC         phosphate + H(+); Xref=Rhea:RHEA:78459, Rhea:RHEA-COMP:19083,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33710, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.4.2.6;
CC         Evidence={ECO:0000305|PubMed:9495761};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78460;
CC         Evidence={ECO:0000305|PubMed:9495761};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate(out) + ATP
CC         + H2O = L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate(in) + ADP
CC         + phosphate + H(+); Xref=Rhea:RHEA:29763, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61401, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000305|PubMed:9495761};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29764;
CC         Evidence={ECO:0000305|PubMed:9495761};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OppD and
CC       OppF), two transmembrane proteins (OppB and OppC) and a solute-binding
CC       protein (OppA or MppA). {ECO:0000305|PubMed:9495761}.
CC   -!- INTERACTION:
CC       P76027; P33916: yejF; NbExp=3; IntAct=EBI-560815, EBI-560808;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P04285}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P04285}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; U00096; AAT48129.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14778.1; -; Genomic_DNA.
DR   PIR; A64872; A64872.
DR   RefSeq; WP_000110948.1; NZ_CP009789.1.
DR   RefSeq; YP_025300.1; NC_000913.3.
DR   PDB; 8Z21; EM; 3.17 A; C=1-336.
DR   AlphaFoldDB; P76027; -.
DR   EMDB; EMD-39742; -.
DR   SMR; P76027; -.
DR   BioGRID; 4259494; 329.
DR   BioGRID; 850169; 1.
DR   ComplexPortal; CPX-4343; Murein tripeptide ABC transporter complex.
DR   ComplexPortal; CPX-4344; Oligopeptide ABC transporter complex.
DR   DIP; DIP-10408N; -.
DR   FunCoup; P76027; 411.
DR   IntAct; P76027; 3.
DR   STRING; 511145.b1246; -.
DR   TCDB; 3.A.1.5.41; the atp-binding cassette (abc) superfamily.
DR   jPOST; P76027; -.
DR   PaxDb; 511145-b1246; -.
DR   EnsemblBacteria; AAT48129; AAT48129; b1246.
DR   GeneID; 945802; -.
DR   KEGG; ecj:JW1238; -.
DR   KEGG; eco:b1246; -.
DR   KEGG; ecoc:C3026_07320; -.
DR   PATRIC; fig|1411691.4.peg.1037; -.
DR   EchoBASE; EB0671; -.
DR   eggNOG; COG0444; Bacteria.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   InParanoid; P76027; -.
DR   OMA; CPYADVP; -.
DR   OrthoDB; 9784450at2; -.
DR   PhylomeDB; P76027; -.
DR   BioCyc; EcoCyc:OPPD-MONOMER; -.
DR   BioCyc; MetaCyc:OPPD-MONOMER; -.
DR   PRO; PR:P76027; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P76027; -.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:ComplexPortal.
DR   GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015421; F:ABC-type oligopeptide transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015640; F:peptidoglycan peptide transmembrane transporter activity; EXP:EcoCyc.
DR   GO; GO:0140205; P:oligopeptide import across plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0015834; P:peptidoglycan-associated peptide transport; EXP:EcoCyc.
DR   GO; GO:0140207; P:tripeptide import across plasma membrane; NAS:ComplexPortal.
DR   CDD; cd03257; ABC_NikE_OppD_transporters; 1.
DR   FunFam; 3.40.50.300:FF:000016; Oligopeptide ABC transporter ATP-binding component; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR050388; ABC_Ni/Peptide_Import.
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   NCBIfam; TIGR01727; oligo_HPY; 1.
DR   NCBIfam; NF007010; PRK09473.1; 1.
DR   PANTHER; PTHR43297:SF7; D,D-DIPEPTIDE TRANSPORT ATP-BINDING PROTEIN DDPD-RELATED; 1.
DR   PANTHER; PTHR43297; OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN APPD; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PDBsum; 8Z21; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..337
FT                   /note="Oligopeptide transport ATP-binding protein OppD"
FT                   /id="PRO_0000092658"
FT   DOMAIN          20..269
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         56..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   HELIX           11..14
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          19..29
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          36..46
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          51..55
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           62..70
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          77..85
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   TURN            99..105
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           123..134
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           139..152
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           158..161
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           171..183
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   TURN            195..198
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           201..218
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          221..227
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           229..235
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          237..243
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          246..252
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           253..258
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           263..271
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           284..286
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           288..291
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   TURN            300..304
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           310..313
FT                   /evidence="ECO:0007829|PDB:8Z21"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:8Z21"
SQ   SEQUENCE   337 AA;  37188 MW;  B64BAA2C5794F359 CRC64;
     MSVIETATVP LAQQQADALL NVKDLRVTFS TPDGDVTAVN DLNFSLRAGE TLGIVGESGS
     GKSQTAFALM GLLAANGRIG GSATFNGREI LNLPEHELNK LRAEQISMIF QDPMTSLNPY
     MRVGEQLMEV LMLHKNMSKA EAFEESVRML DAVKMPEARK RMKMYPHEFS GGMRQRVMIA
     MALLCRPKLL IADEPTTALD VTVQAQIMTL LNELKREFNT AIIMITHDLV VVAGICDKVL
     VMYAGRTMEY GNARDVFYQP VHPYSIGLLN AVPRLDAEGE TMLTIPGNPP NLLRLPKGCP
     FQPRCPHAME ICSSAPPLEE FTPGRLRACF KPVEELL
//