P06202 (OPPA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Periplasmic oligopeptide-binding protein

Gene names

Name:	oppA
Ordered Locus Names:	STM1746

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Peptide transport Protein transport Transport
Cellular component	Periplasm
Domain	Signal
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptide transport Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Chain

27 – 543

517

Periplasmic oligopeptide-binding protein

PRO_0000031798

Amino acid modifications

Disulfide bond

297 ↔ 443

Experimental info

Sequence conflict

22 – 24

3

SAA → TP Ref.1

Sequence conflict

22 – 24

3

SAA → TP Ref.2

Secondary structure

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543

Helix Strand Turn

Details...

Beta strand

40 – 44

5

Turn

54 – 56

3

Helix

60 – 69

10

Beta strand

73 – 76

4

Beta strand

82 – 93

12

Turn

94 – 96

3

Beta strand

97 – 102

6

Helix

116 – 127

12

Helix

129 – 131

3

Turn

134 – 137

4

Helix

138 – 141

4

Helix

147 – 151

5

Helix

157 – 159

3

Beta strand

160 – 166

7

Beta strand

169 – 176

8

Helix

181 – 184

4

Helix

188 – 190

3

Helix

195 – 201

7

Helix

202 – 204

3

Turn

208 – 210

3

Beta strand

215 – 223

9

Turn

224 – 226

3

Beta strand

227 – 232

6

Helix

239 – 241

3

Beta strand

246 – 250

5

Helix

255 – 263

9

Turn

276 – 278

3

Helix

279 – 285

7

Helix

287 – 289

3

Beta strand

290 – 303

14

Turn

308 – 311

4

Helix

313 – 322

10

Helix

325 – 330

6

Turn

331 – 333

3

Beta strand

341 – 344

4

Helix

357 – 360

4

Helix

363 – 376

14

Beta strand

381 – 383

3

Beta strand

386 – 393

8

Helix

395 – 412

18

Beta strand

415 – 421

7

Helix

423 – 432

10

Beta strand

436 – 443

8

Beta strand

445 – 448

4

Helix

450 – 453

4

Helix

454 – 456

3

Helix

470 – 478

9

Turn

479 – 481

3

Beta strand

482 – 484

3

Helix

485 – 501

17

Beta strand

505 – 517

13

Beta strand

521 – 523

3

Helix

535 – 537

3

Beta strand

539 – 541

3

Sequences

	Sequence		Length	Mass (Da)
	P06202 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: EF344E7C7991CA47	FASTA	543	61,292
	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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

PIR

QREBOA. A25011.

RefSeq

NP_460705.2. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B05	X-ray	2.00	A	27-543	[»]
1B0H	X-ray	1.90	A	27-543	[»]
1B1H	X-ray	1.80	A	27-543	[»]
1B2H	X-ray	1.90	A	27-543	[»]
1B32	X-ray	1.75	A	27-543	[»]
1B3F	X-ray	1.80	A	27-543	[»]
1B3G	X-ray	2.00	A	27-543	[»]
1B3H	X-ray	2.00	A	27-543	[»]
1B3L	X-ray	2.00	A/C	27-543	[»]
1B40	X-ray	2.20	A	27-543	[»]
1B46	X-ray	1.80	A	27-543	[»]
1B4H	X-ray	1.90	A	27-543	[»]
1B4Z	X-ray	1.75	A	27-543	[»]
1B51	X-ray	1.80	A	27-543	[»]
1B52	X-ray	2.30	A	27-543	[»]
1B58	X-ray	1.80	A	27-543	[»]
1B5H	X-ray	1.90	A	27-543	[»]
1B5I	X-ray	1.90	A	27-543	[»]
1B5J	X-ray	1.80	A	27-543	[»]
1B6H	X-ray	1.80	A	27-543	[»]
1B7H	X-ray	2.00	A	27-543	[»]
1B9J	X-ray	1.80	A	27-543	[»]
1JET	X-ray	1.20	A	27-542	[»]
1JEU	X-ray	1.25	A	27-542	[»]
1JEV	X-ray	1.30	A	27-542	[»]
1OLA	X-ray	2.10	A	27-543	[»]
1OLC	X-ray	2.10	A	27-543	[»]
1QKA	X-ray	1.80	A	27-543	[»]
1QKB	X-ray	1.80	A	27-543	[»]
1RKM	X-ray	2.40	A	27-542	[»]
2OLB	X-ray	1.40	A	27-543	[»]
2RKM	X-ray	1.80	A	27-542	[»]

ProteinModelPortal

P06202.

SMR

P06202. Positions 27-543.

ModBase

Search...

Protein-protein interaction databases

STRING

99287.STM1746.S.

Protein family/group databases

TCDB

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

Proteomic databases

PaxDb

P06202.

PRIDE

P06202.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL20664; AAL20664; STM1746.

GeneID

1253265.

KEGG

stm:STM1746.S.

PATRIC

32382007. VBISalEnt20916_1843.

Phylogenomic databases

eggNOG

COG4166.

KO

K15580.

OMA

LANPNTA.

ProtClustDB

PRK15104.

Family and domain databases

InterPro

IPR000914. SBP_bac_5.
IPR023765. SBP_bac_5_CS.
[Graphical view]

Pfam

PF00496. SBP_bac_5. 1 hit.
[Graphical view]

PROSITE

PS01040. SBP_BACTERIAL_5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06202.

Entry information

Entry name

OPPA_SALTY

Accession

Primary (citable) accession number: P06202

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program