P36936 (PEPE_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidase E
EC=3.4.13.21

Alternative name(s):
Alpha-aspartyl dipeptidase
Asp-specific dipeptidase
Dipeptidase E

Gene names

Name:	pepE
Ordered Locus Names:	STM4190

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	229 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. HAMAP-Rule MF_00510
Catalytic activity	Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides. HAMAP-Rule MF_00510
Subcellular location	Cytoplasm HAMAP-Rule MF_00510.
Sequence similarities	Belongs to the peptidase S51 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Dipeptidase Hydrolase Protease Serine protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dipeptidase activity Inferred from electronic annotation. Source: HAMAP serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 229

229

Peptidase E HAMAP-Rule MF_00510

PRO_0000209961

Sites

Active site

120

1

Charge relay system Ref.3

Active site

135

1

Charge relay system Ref.3

Active site

157

1

Charge relay system Ref.3

Natural variations

Natural variant

120

1

S → T in pepE1; deficient.

Natural variant

137

1

P → S in pepE1; deficient.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

229

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Turn

16 – 20

5

Helix

21 – 28

8

Beta strand

33 – 37

5

Helix

46 – 57

12

Helix

58 – 60

3

Beta strand

63 – 66

4

Beta strand

69 – 71

3

Helix

73 – 79

7

Beta strand

81 – 85

5

Helix

90 – 99

10

Helix

103 – 111

9

Beta strand

115 – 119

5

Helix

121 – 125

5

Beta strand

127 – 130

4

Beta strand

150 – 155

6

Helix

171 – 181

11

Beta strand

186 – 189

4

Beta strand

195 – 198

4

Beta strand

203 – 209

7

Beta strand

211 – 215

5

Beta strand

218 – 223

6

Sequences

	Sequence		Length	Mass (Da)
	P36936 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 41D40652C7D32220	FASTA	229	24,769
	10 20 30 40 50 60 MELLLLSNST LPGKAWLEHA LPLIANQLNG RRSAVFIPFA GVTQTWDEYT DKTAEVLAPL 70 80 90 100 110 120 GVNVTGIHRV ADPLAAIEKA EIIIVGGGNT FQLLKESRER GLLAPMADRV KRGALYIGWS 130 140 150 160 170 180 AGANLACPTI RTTNDMPIVD PNGFDALDLF PLQINPHFTN ALPEGHKGET REQRIRELLV 190 200 210 220 VAPELTVIGL PEGNWIQVSN GQAVLGGPNT TWVFKAGEEA VALEAGHRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of the cyclic AMP receptor protein-regulated Salmonella typhimurium pepE gene and crystallization of its product, an alpha-aspartyl dipeptidase." Conlin C.A., Hakensson K., Liljas A., Miller C.G. J. Bacteriol. 176:166-172(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25. Strain: LT2.
[2]	"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.
[3]	"Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase." Lassy R.A., Miller C.G. J. Bacteriol. 182:2536-2543(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, ACTIVE SITES, MUTAGENESIS.
[4]	"The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad." Hakansson K., Wang A.H.-J., Miller C.G. Proc. Natl. Acad. Sci. U.S.A. 97:14097-14102(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U01246 Unassigned DNA. Translation: AAA18923.1.
AE006468 Genomic DNA. Translation: AAL23014.1.

PIR

A36867.

RefSeq

NP_463055.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FY2	X-ray	1.20	A	1-229	[»]
1FYE	X-ray	1.20	A	1-229	[»]

ProteinModelPortal

P36936.

SMR

P36936. Positions 1-229.

ModBase

Search...

Protein-protein interaction databases

STRING

99287.STM4190.

Proteomic databases

PRIDE

P36936.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL23014; AAL23014; STM4190.

GeneID

1255716.

KEGG

stm:STM4190.

PATRIC

32387273. VBISalEnt20916_4404.

Phylogenomic databases

HOGENOM

HOG000281834.

KO

K05995.

OMA

SIHTTND.

ProtClustDB

PRK05282.

Family and domain databases

HAMAP

MF_00510. Peptidase_E.

InterPro

IPR005320. Peptidase_S51.
IPR023172. Peptidase_S51_dipeptidase-E.
[Graphical view]

Pfam

PF03575. Peptidase_S51. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P36936.

Entry information

Entry name

PEPE_SALTY

Accession

Primary (citable) accession number: P36936

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program