ID OPPA_SALTY Reviewed; 543 AA. AC P06202; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 02-SEP-2026, entry version 161. DE RecName: Full=Periplasmic oligopeptide-binding protein OppA {ECO:0000305}; DE Flags: Precursor; GN Name=oppA {ECO:0000303|PubMed:3525163}; OrderedLocusNames=STM1746; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-41, AND RP SUBCELLULAR LOCATION. RX PubMed=3525163; DOI=10.1111/j.1432-1033.1986.tb09791.x; RA Hiles I.D., Higgins C.F.; RT "Peptide uptake by Salmonella typhimurium. The periplasmic oligopeptide- RT binding protein."; RL Eur. J. Biochem. 158:561-567(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, RP AND INDUCTION. RC STRAIN=LT2; RX PubMed=2821267; DOI=10.1016/0022-2836(87)90332-9; RA Hiles I.D., Gallagher M.P., Jamieson D.J., Higgins C.F.; RT "Molecular characterization of the oligopeptide permease of Salmonella RT typhimurium."; RL J. Mol. Biol. 195:125-142(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=LT2; RX PubMed=3301822; DOI=10.1128/jb.169.8.3861-3865.1987; RA Goodell E.W., Higgins C.F.; RT "Uptake of cell wall peptides by Salmonella typhimurium and Escherichia RT coli."; RL J. Bacteriol. 169:3861-3865(1987). RN [5] {ECO:0007744|PDB:1OLA} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-543 IN COMPLEX WITH A RP TETRAPEPTIDE, FUNCTION, AND DISULFIDE BOND. RX PubMed=8202710; DOI=10.1126/science.8202710; RA Tame J.R.H., Murshudov G.N., Dodson E.J., Neil T.K., Dodson G.G., RA Higgins C.F., Wilkinson A.J.; RT "The structural basis of sequence-independent peptide binding by OppA RT protein."; RL Science 264:1578-1581(1994). RN [6] {ECO:0007744|PDB:1OLC, ECO:0007744|PDB:2OLB} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 27-543 IN COMPLEXES WITH A RP TRIPEPTIDE AND A TETRAPEPTIDE, FUNCTION, DOMAIN, AND DISULFIDE BOND. RX PubMed=8747465; DOI=10.1016/s0969-2126(01)00276-3; RA Tame J.R.H., Dodson E.J., Murshudov G.N., Higgins C.F., Wilkinson A.J.; RT "The crystal structures of the oligopeptide-binding protein OppA complexed RT with tripeptide and tetrapeptide ligands."; RL Structure 3:1395-1406(1995). RN [7] {ECO:0007744|PDB:1JET, ECO:0007744|PDB:1JEU, ECO:0007744|PDB:1JEV} RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 27-543 IN COMPLEXES WITH RP TRIPEPTIDES, FUNCTION, DOMAIN, AND DISULFIDE BOND. RX PubMed=8946852; DOI=10.1038/nsb1296-998; RA Tame J.R., Sleigh S.H., Wilkinson A.J., Ladbury J.E.; RT "The role of water in sequence-independent ligand binding by an RT oligopeptide transporter protein."; RL Nat. Struct. Biol. 3:998-1001(1996). RN [8] {ECO:0007744|PDB:1RKM, ECO:0007744|PDB:2RKM} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 27-543 OF APOPROTEIN AND IN RP COMPLEX WITH A DIPEPTIDE, FUNCTION, AND DISULFIDE BOND. RX PubMed=9245406; DOI=10.1021/bi970457u; RA Sleigh S.H., Tame J.R., Dodson E.J., Wilkinson A.J.; RT "Peptide binding in OppA, the crystal structures of the periplasmic RT oligopeptide binding protein in the unliganded form and in complex with RT lysyllysine."; RL Biochemistry 36:9747-9758(1997). RN [9] {ECO:0007744|PDB:1B0H, ECO:0007744|PDB:1B1H, ECO:0007744|PDB:1B2H, ECO:0007744|PDB:1B3H, ECO:0007744|PDB:1B4H, ECO:0007744|PDB:1B5H, ECO:0007744|PDB:1B6H, ECO:0007744|PDB:1B7H} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 27-543 IN COMPLEXES WITH RP TRIPEPTIDES CONTAINING AN ABNORMAL RESIDUE, AND DISULFIDE BOND. RX PubMed=10422831; DOI=10.1110/ps.8.7.1432; RA Davies T.G., Hubbard R.E., Tame J.R.H.; RT "Relating structure to thermodynamics: the crystal structures and binding RT affinity of eight OppA-peptide complexes."; RL Protein Sci. 8:1432-1444(1999). RN [10] {ECO:0007744|PDB:1B05, ECO:0007744|PDB:1B32, ECO:0007744|PDB:1B3F, ECO:0007744|PDB:1B3G, ECO:0007744|PDB:1B3L, ECO:0007744|PDB:1B40, ECO:0007744|PDB:1B46, ECO:0007744|PDB:1B4Z, ECO:0007744|PDB:1B51, ECO:0007744|PDB:1B52, ECO:0007744|PDB:1B58} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 27-543 IN COMPLEXES WITH RP LYS-X-LYS TRIPEPTIDES, FUNCTION, DOMAIN, AND DISULFIDE BOND. RX PubMed=10438628; DOI=10.1006/jmbi.1999.2929; RA Sleigh S.H., Seavers P.R., Wilkinson A.J., Ladbury J.E., Tame J.R.H.; RT "Crystallographic and calorimetric analysis of peptide binding to OppA RT protein."; RL J. Mol. Biol. 291:393-415(1999). CC -!- FUNCTION: Part of the ABC transporter complex OppABCDF involved in the CC uptake of oligopeptides, including the cell wall murein tripeptide L- CC alanyl-gamma-D-glutamyl-meso-diaminopimelate (PubMed:2821267, CC PubMed:3301822). Plays an important nutritional role and is involved in CC the recycling of cell wall peptides (PubMed:2821267, PubMed:3301822). CC Binds peptides containing from two to five amino acid residues CC regardless of their sequence (PubMed:10438628, PubMed:8202710, CC PubMed:8747465, PubMed:8946852, PubMed:9245406). Also binds cell wall CC peptides, such as L-alanyl-gamma-D-glutamyl-meso-diaminopimelate CC (PubMed:3301822). {ECO:0000269|PubMed:10438628, CC ECO:0000269|PubMed:2821267, ECO:0000269|PubMed:3301822, CC ECO:0000269|PubMed:8202710, ECO:0000269|PubMed:8747465, CC ECO:0000269|PubMed:8946852, ECO:0000269|PubMed:9245406}. 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). {ECO:0000269|PubMed:2821267}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2821267, CC ECO:0000269|PubMed:3525163}. CC -!- INDUCTION: Part of the opp operon, which is constitutively expressed. CC {ECO:0000269|PubMed:2821267}. CC -!- DOMAIN: Accommodates the ligand side chains in large hydrated pockets CC which impose little specificity on binding (PubMed:10438628, CC PubMed:8747465, PubMed:8946852). Tight binding is achieved by utilising CC the hydrogen-bonding potential of the main chain of the ligand CC (PubMed:10438628, PubMed:8747465). {ECO:0000269|PubMed:10438628, CC ECO:0000269|PubMed:8747465, ECO:0000269|PubMed:8946852}. CC -!- DISRUPTION PHENOTYPE: Mutant cannot take up cell wall peptides. CC {ECO:0000269|PubMed:3301822}. CC -!- MISCELLANEOUS: Isothermal titration calorimetric measurements of the CC binding of lysine-containing peptides of different lengths to OppA show CC that the dipeptide Lys-Lys is bound with 60-fold lower affinity than CC related tri- and tetrapeptides (Lys-Lys-Lys and Lys-Lys-Lys-Ala, CC respectively). {ECO:0000269|PubMed:9245406}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL20664.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04194; CAA27785.1; -; Genomic_DNA. DR EMBL; X05491; CAA29039.1; -; Genomic_DNA. DR EMBL; AE006468; AAL20664.1; ALT_INIT; Genomic_DNA. DR PIR; A25011; QREBOA. DR RefSeq; NP_460705.3; NC_003197.2. DR RefSeq; WP_000560668.1; NC_003197.2. DR PDB; 1B05; X-ray; 2.00 A; A=27-543. DR PDB; 1B0H; X-ray; 1.90 A; A=27-543. DR PDB; 1B1H; X-ray; 1.80 A; A=27-543. DR PDB; 1B2H; X-ray; 1.90 A; A=27-543. DR PDB; 1B32; X-ray; 1.75 A; A=27-543. DR PDB; 1B3F; X-ray; 1.80 A; A=27-543. DR PDB; 1B3G; X-ray; 2.00 A; A=27-543. DR PDB; 1B3H; X-ray; 2.00 A; A=27-543. DR PDB; 1B3L; X-ray; 2.00 A; A/C=27-543. DR PDB; 1B40; X-ray; 2.20 A; A=27-543. DR PDB; 1B46; X-ray; 1.80 A; A=27-543. DR PDB; 1B4H; X-ray; 1.90 A; A=27-543. DR PDB; 1B4Z; X-ray; 1.75 A; A=27-543. DR PDB; 1B51; X-ray; 1.80 A; A=27-543. DR PDB; 1B52; X-ray; 2.30 A; A=27-543. DR PDB; 1B58; X-ray; 1.80 A; A=27-543. DR PDB; 1B5H; X-ray; 1.90 A; A=27-543. DR PDB; 1B5I; X-ray; 1.90 A; A=27-543. DR PDB; 1B5J; X-ray; 1.80 A; A=27-543. DR PDB; 1B6H; X-ray; 1.80 A; A=27-543. DR PDB; 1B7H; X-ray; 2.00 A; A=27-543. DR PDB; 1B9J; X-ray; 1.80 A; A=27-543. DR PDB; 1JET; X-ray; 1.20 A; A=27-543. DR PDB; 1JEU; X-ray; 1.25 A; A=27-543. DR PDB; 1JEV; X-ray; 1.30 A; A=27-543. DR PDB; 1OLA; X-ray; 2.10 A; A=27-543. DR PDB; 1OLC; X-ray; 2.10 A; A=27-543. DR PDB; 1QKA; X-ray; 1.80 A; A=27-543. DR PDB; 1QKB; X-ray; 1.80 A; A=27-543. DR PDB; 1RKM; X-ray; 2.40 A; A=27-543. DR PDB; 2OLB; X-ray; 1.40 A; A=27-543. DR PDB; 2RKM; X-ray; 1.80 A; A=27-543. DR AlphaFoldDB; P06202; -. DR BMRB; P06202; -. DR MDposit; P06202; -. DR MDRepo; P06202; -. DR SMR; P06202; -. DR STRING; 99287.STM1746; -. DR DrugBank; DB07365; 1-Naphthyl-L-alanine. DR TCDB; 3.A.1.5.1; the atp-binding cassette (abc) superfamily. DR PaxDb; 99287-STM1746; -. DR GeneID; 1253265; -. DR KEGG; stm:STM1746; -. DR PATRIC; fig|99287.12.peg.1843; -. DR HOGENOM; CLU_017028_0_3_6; -. DR OMA; GEHEMAF; -. DR PhylomeDB; P06202; -. DR EvolutionaryTrace; P06202; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0042597; C:periplasmic space; EXP:UniProtKB. DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GO_Central. DR CDD; cd08504; PBP2_OppA; 1. DR FunFam; 3.90.76.10:FF:000001; Oligopeptide ABC transporter substrate-binding protein; 1. DR FunFam; 3.10.105.10:FF:000001; Oligopeptide ABC transporter, oligopeptide-binding protein; 1. DR FunFam; 3.40.190.10:FF:000018; Oligopeptide ABC transporter, oligopeptide-binding protein; 1. DR Gene3D; 3.90.76.10; Dipeptide-binding Protein, Domain 1; 1. DR Gene3D; 3.10.105.10; Dipeptide-binding Protein, Domain 3; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR039424; SBP_5. DR InterPro; IPR023765; SBP_5_CS. DR InterPro; IPR000914; SBP_5_dom. DR NCBIfam; NF011684; PRK15104.1; 1. DR PANTHER; PTHR30290; PERIPLASMIC BINDING COMPONENT OF ABC TRANSPORTER; 1. DR PANTHER; PTHR30290:SF10; PERIPLASMIC OLIGOPEPTIDE-BINDING PROTEIN-RELATED; 1. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. DR PDBsum; 1B05; -. DR PDBsum; 1B0H; -. DR PDBsum; 1B1H; -. DR PDBsum; 1B2H; -. DR PDBsum; 1B32; -. DR PDBsum; 1B3F; -. DR PDBsum; 1B3G; -. DR PDBsum; 1B3H; -. DR PDBsum; 1B3L; -. DR PDBsum; 1B40; -. DR PDBsum; 1B46; -. DR PDBsum; 1B4H; -. DR PDBsum; 1B4Z; -. DR PDBsum; 1B51; -. DR PDBsum; 1B52; -. DR PDBsum; 1B58; -. DR PDBsum; 1B5H; -. DR PDBsum; 1B5I; -. DR PDBsum; 1B5J; -. DR PDBsum; 1B6H; -. DR PDBsum; 1B7H; -. DR PDBsum; 1B9J; -. DR PDBsum; 1JET; -. DR PDBsum; 1JEU; -. DR PDBsum; 1JEV; -. DR PDBsum; 1OLA; -. DR PDBsum; 1OLC; -. DR PDBsum; 1QKA; -. DR PDBsum; 1QKB; -. DR PDBsum; 1RKM; -. DR PDBsum; 2OLB; -. DR PDBsum; 2RKM; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Peptide transport; KW Periplasm; Protein transport; Reference proteome; Signal; Transport. FT SIGNAL 1..26 FT /evidence="ECO:0000269|PubMed:3525163" FT CHAIN 27..543 FT /note="Periplasmic oligopeptide-binding protein OppA" FT /id="PRO_0000031798" FT DISULFID 297..443 FT /evidence="ECO:0000269|PubMed:10422831, FT ECO:0000269|PubMed:10438628, ECO:0000269|PubMed:8202710, FT ECO:0000269|PubMed:8747465, ECO:0000269|PubMed:8946852, FT ECO:0000269|PubMed:9245406, ECO:0007744|PDB:1JET, FT ECO:0007744|PDB:1JEU, ECO:0007744|PDB:1JEV, FT ECO:0007744|PDB:1OLA, ECO:0007744|PDB:1OLC, FT ECO:0007744|PDB:1RKM, ECO:0007744|PDB:2OLB, FT ECO:0007744|PDB:2RKM" FT CONFLICT 22..24 FT /note="SAA -> TP (in Ref. 1; CAA27785 and 2; CAA29039)" FT /evidence="ECO:0000305" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:1JET" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:1B1H" FT HELIX 60..69 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 73..76 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 82..93 FT /evidence="ECO:0007829|PDB:1JET" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 97..102 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 116..127 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:1JET" FT TURN 134..137 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 138..141 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 147..151 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 160..166 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 169..176 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 181..184 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 195..201 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 202..204 FT /evidence="ECO:0007829|PDB:1JET" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 215..223 FT /evidence="ECO:0007829|PDB:1JET" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 227..232 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 246..250 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 255..263 FT /evidence="ECO:0007829|PDB:1JET" FT TURN 276..278 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 279..285 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 290..303 FT /evidence="ECO:0007829|PDB:1JET" FT TURN 308..311 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 313..322 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 327..333 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 353..356 FT /evidence="ECO:0007829|PDB:1JEU" FT HELIX 357..360 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 363..376 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 381..383 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 386..393 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 395..412 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 415..421 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 423..432 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 436..443 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 445..448 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 450..453 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 454..456 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 470..478 FT /evidence="ECO:0007829|PDB:1JET" FT TURN 479..481 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:1JEU" FT HELIX 485..501 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 505..517 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 521..523 FT /evidence="ECO:0007829|PDB:1JET" FT HELIX 535..537 FT /evidence="ECO:0007829|PDB:1JET" FT STRAND 539..541 FT /evidence="ECO:0007829|PDB:1JET" SQ SEQUENCE 543 AA; 61292 MW; EF344E7C7991CA47 CRC64; MSNITKKSLI AAGILTALIA ASAATAADVP AGVQLADKQT LVRNNGSEVQ SLDPHKIEGV PESNVSRDLF EGLLISDVEG HPSPGVAEKW ENKDFKVWTF HLRENAKWSD GTPVTAHDFV YSWQRLADPN TASPYASYLQ YGHIANIDDI IAGKKPATDL GVKALDDHTF EVTLSEPVPY FYKLLVHPSV SPVPKSAVEK FGDKWTQPAN IVTNGAYKLK NWVVNERIVL ERNPQYWDNA KTVINQVTYL PISSEVTDVN RYRSGEIDMT YNNMPIELFQ KLKKEIPNEV RVDPYLCTYY YEINNQKAPF NDVRVRTALK LALDRDIIVN KVKNQGDLPA YSYTPPYTDG AKLVEPEWFK WSQQKRNEEA KKLLAEAGFT ADKPLTFDLL YNTSDLHKKL AIAVASIWKK NLGVNVNLEN QEWKTFLDTR HQGTFDVARA GWCADYNEPT SFLNTMLSDS SNNTAHYKSP AFDKLIADTL KVADDTQRSE LYAKAEQQLD KDSAIVPVYY YVNARLVKPW VGGYTGKDPL DNIYVKNLYI IKH //