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P06202 (OPPA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Periplasmic oligopeptide-binding protein
Gene names
Name:oppA
Ordered Locus Names:STM1746
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the bacterial solute-binding protein 5 family.

Sequence caution

The sequence AAL20664.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPeptide transport
Protein transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpeptide transport

Inferred from electronic annotation. Source: UniProtKB-KW

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontransporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 543517Periplasmic oligopeptide-binding protein
PRO_0000031798

Amino acid modifications

Disulfide bond297 ↔ 443

Experimental info

Sequence conflict22 – 243SAA → TP Ref.1
Sequence conflict22 – 243SAA → TP Ref.2

Secondary structure

............................................................................................. 543
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06202 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: EF344E7C7991CA47

FASTA54361,292
        10         20         30         40         50         60 
MSNITKKSLI AAGILTALIA ASAATAADVP AGVQLADKQT LVRNNGSEVQ SLDPHKIEGV 

        70         80         90        100        110        120 
PESNVSRDLF EGLLISDVEG HPSPGVAEKW ENKDFKVWTF HLRENAKWSD GTPVTAHDFV 

       130        140        150        160        170        180 
YSWQRLADPN TASPYASYLQ YGHIANIDDI IAGKKPATDL GVKALDDHTF EVTLSEPVPY 

       190        200        210        220        230        240 
FYKLLVHPSV SPVPKSAVEK FGDKWTQPAN IVTNGAYKLK NWVVNERIVL ERNPQYWDNA 

       250        260        270        280        290        300 
KTVINQVTYL PISSEVTDVN RYRSGEIDMT YNNMPIELFQ KLKKEIPNEV RVDPYLCTYY 

       310        320        330        340        350        360 
YEINNQKAPF NDVRVRTALK LALDRDIIVN KVKNQGDLPA YSYTPPYTDG AKLVEPEWFK 

       370        380        390        400        410        420 
WSQQKRNEEA KKLLAEAGFT ADKPLTFDLL YNTSDLHKKL AIAVASIWKK NLGVNVNLEN 

       430        440        450        460        470        480 
QEWKTFLDTR HQGTFDVARA GWCADYNEPT SFLNTMLSDS SNNTAHYKSP AFDKLIADTL 

       490        500        510        520        530        540 
KVADDTQRSE LYAKAEQQLD KDSAIVPVYY YVNARLVKPW VGGYTGKDPL DNIYVKNLYI 


IKH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of the oligopeptide permease of Salmonella typhimurium."
Hiles I.D., Gallagher M.P., Jamieson D.J., Higgins C.F.
J. Mol. Biol. 195:125-142(1987) [PubMed: 2821267] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Peptide uptake by Salmonella typhimurium. The periplasmic oligopeptide-binding protein."
Hiles I.D., Higgins C.F.
Eur. J. Biochem. 158:561-567(1986) [PubMed: 3525163] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[4]"The structural basis of sequence-independent peptide binding by OppA protein."
Tame J.R.H., Murshudov G.N., Dodson E.J., Neil T.K., Dodson G.G., Higgins C.F., Wilkinson A.J.
Science 264:1578-1581(1994) [PubMed: 8202710] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[5]"The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands."
Tame J.R.H., Dodson E.J., Murshudov G.N., Higgins C.F., Wilkinson A.J.
Structure 3:1395-1406(1995) [PubMed: 8747465] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
[6]"Relating structure to thermodynamics: the crystal structures and binding affinity of eight OppA-peptide complexes."
Davies T.G., Hubbard R.E., Tame J.R.H.
Protein Sci. 8:1432-1444(1999) [PubMed: 10422831] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[7]"Crystallographic and calorimetric analysis of peptide binding to OppA protein."
Sleigh S.H., Seavers P.R., Wilkinson A.J., Ladbury J.E., Tame J.R.H.
J. Mol. Biol. 291:393-415(1999) [PubMed: 10438628] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04194 Genomic DNA. Translation: CAA27785.1.
X05491 Genomic DNA. Translation: CAA29039.1.
AE006468 Genomic DNA. Translation: AAL20664.1. Different initiation.
PIRQREBOA. A25011.
RefSeqNP_460705.2. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B05X-ray2.00A27-543[»]
1B0HX-ray1.90A27-543[»]
1B1HX-ray1.80A27-543[»]
1B2HX-ray1.90A27-543[»]
1B32X-ray1.75A27-543[»]
1B3FX-ray1.80A27-543[»]
1B3GX-ray2.00A27-543[»]
1B3HX-ray2.00A27-543[»]
1B3LX-ray2.00A/C27-543[»]
1B40X-ray2.20A27-543[»]
1B46X-ray1.80A27-543[»]
1B4HX-ray1.90A27-543[»]
1B4ZX-ray1.75A27-543[»]
1B51X-ray1.80A27-543[»]
1B52X-ray2.30A27-543[»]
1B58X-ray1.80A27-543[»]
1B5HX-ray1.90A27-543[»]
1B5IX-ray1.90A27-543[»]
1B5JX-ray1.80A27-543[»]
1B6HX-ray1.80A27-543[»]
1B7HX-ray2.00A27-543[»]
1B9JX-ray1.80A27-543[»]
1JETX-ray1.20A27-542[»]
1JEUX-ray1.25A27-542[»]
1JEVX-ray1.30A27-542[»]
1OLAX-ray2.10A27-543[»]
1OLCX-ray2.10A27-543[»]
1QKAX-ray1.80A27-543[»]
1QKBX-ray1.80A27-543[»]
1RKMX-ray2.40A27-542[»]
2OLBX-ray1.40A27-543[»]
2RKMX-ray1.80A27-542[»]
ProteinModelPortalP06202.
SMRP06202. Positions 27-543.
ModBaseSearch...

Protein family/group databases

TCDB3.A.1.5.1. ATP-binding cassette (ABC) superfamily.

Proteomic databases

PRIDEP06202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1253265.
GenomeReviewsGene locus STM1746 in contig AE006468_GR.
NMPDRfig|99287.1.peg.1691.
PATRIC32382007. VBISalEnt20916_1843.

Phylogenomic databases

HOGENOMHBG688042.
OMALANPNTA.
ProtClustDBPRK15104.

Enzyme and pathway databases

BioCycSTYP99287:STM1746-MONOMER.

Family and domain databases

InterProIPR000914. SBP_bac_5.
IPR023765. SBP_bac_5_CS.
[Graphical view]
PfamPF00496. SBP_bac_5. 1 hit.
[Graphical view]
PROSITEPS01040. SBP_BACTERIAL_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOPPA_SALTY
AccessionPrimary (citable) accession number: P06202
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2002
Last modified: January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families