OPPA_SALTY
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 25-MAY-2022, entry version 145.
DE RecName: Full=Periplasmic oligopeptide-binding protein;
DE Flags: Precursor;
GN Name=oppA; OrderedLocusNames=STM1746;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [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 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
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: This protein is a component of the oligopeptide permease, a
CC binding protein-dependent transport system, it binds peptides up to
CC five amino acids long with high affinity.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL20664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 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 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; -.
DR AlphaFoldDB; P06202; -.
DR BMRB; 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; P06202; -.
DR PRIDE; P06202; -.
DR EnsemblBacteria; AAL20664; AAL20664; STM1746.
DR GeneID; 1253265; -.
DR KEGG; stm:STM1746; -.
DR PATRIC; fig|99287.12.peg.1843; -.
DR HOGENOM; CLU_017028_0_3_6; -.
DR OMA; YDFFTWE; -.
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:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Peptide transport; Periplasm;
KW Protein transport; Reference proteome; Signal; Transport.
FT SIGNAL 1..26
FT CHAIN 27..543
FT /note="Periplasmic oligopeptide-binding protein"
FT /id="PRO_0000031798"
FT DISULFID 297..443
FT CONFLICT 22..24
FT /note="SAA -> TP (in Ref. 1 and 2)"
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 325..330
FT /evidence="ECO:0007829|PDB:1JET"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:1JET"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1JET"
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
