P45494 (PEPV_LACDL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-Ala-Xaa dipeptidase
EC=3.4.13.-

Alternative name(s):
Beta-Ala-His dipeptidase
Peptidase V

Gene names

Name:

pepV

Organism

Lactobacillus delbrueckii subsp. lactis

Taxonomic identifier

29397 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus delbrueckii

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides. Ref.1
Cofactor	Binds 2 zinc ions per subunit. These two catalytic ions are both involved in the stabilization of the tetrahedral intermediate and in the activation of the catalytic water molecule. Ref.2
Enzyme regulation	Fully inhibited by 1,10-phenanthroline or EDTA. Ref.1
Subcellular location	Cytoplasm Probable Ref.1.
Sequence similarities	Belongs to the peptidase M20A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 470

470

Beta-Ala-Xaa dipeptidase

PRO_0000185276

Sites

Active site

89

1

By similarity

Active site

153

1

Proton acceptor Probable

Metal binding

87

1

Zinc 2

Metal binding

119

1

Zinc 1

Metal binding

119

1

Zinc 2

Metal binding

154

1

Zinc 1

Metal binding

177

1

Zinc 2

Metal binding

439

1

Zinc 1

Binding site

350

1

Substrate

Secondary structure

1

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470

Helix Strand Turn

Details...

Helix

5 – 10

6

Helix

13 – 24

12

Helix

32 – 34

3

Beta strand

37 – 39

3

Helix

43 – 58

16

Beta strand

62 – 66

5

Turn

67 – 69

3

Beta strand

70 – 75

6

Beta strand

79 – 87

9

Beta strand

111 – 114

4

Beta strand

117 – 120

4

Helix

121 – 137

17

Beta strand

142 – 151

10

Turn

153 – 156

4

Helix

158 – 166

9

Beta strand

171 – 186

16

Beta strand

188 – 196

9

Beta strand

204 – 212

9

Beta strand

221 – 228

8

Helix

232 – 246

15

Beta strand

249 – 255

7

Beta strand

258 – 264

7

Helix

273 – 275

3

Helix

279 – 287

9

Helix

294 – 305

12

Turn

306 – 309

4

Turn

314 – 317

4

Turn

323 – 325

3

Beta strand

329 – 338

10

Beta strand

343 – 351

9

Helix

357 – 368

12

Turn

369 – 371

3

Beta strand

372 – 375

4

Helix

390 – 403

14

Beta strand

409 – 414

6

Helix

417 – 420

4

Beta strand

444 – 446

3

Helix

447 – 465

19

Sequences

	Sequence		Length	Mass (Da)
	P45494 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 488117B4F33E4AB0	FASTA	470	51,990
	10 20 30 40 50 60 MDLNFKELAE AKKDAILKDL EELIAIDSSE DLENATEEYP VGKGPVDAMT KFLSFAKRDG 70 80 90 100 110 120 FDTENFANYA GRVNFGAGDK RLGIIGHMDV VPAGEGWTRD PFKMEIDEEG RIYGRGSADD 130 140 150 160 170 180 KGPSLTAYYG MLLLKEAGFK PKKKIDFVLG TNEETNWVGI DYYLKHEPTP DIVFSPDAEY 190 200 210 220 230 240 PIINGEQGIF TLEFSFKNDD TKGDYVLDKF KAGIATNVTP QVTRATISGP DLEAVKLAYE 250 260 270 280 290 300 SFLADKELDG SFEINDESAD IVLIGQGAHA SAPQVGKNSA TFLALFLDQY AFAGRDKNFL 310 320 330 340 350 360 HFLAEVEHED FYGKKLGIFH HDDLMGDLAS SPSMFDYEHA GKASLLNNVR YPQGTDPDTM 370 380 390 400 410 420 IKQVLDKFSG ILDVTYNGFE EPHYVPGSDP MVQTLLKVYE KQTGKPGHEV VIGGGTYGRL 430 440 450 460 470 FERGVAFGAQ PENGPMVMHA ANEFMMLDDL ILSIAIYAEA IYELTKDEEL

References

[1]

"Cloning and nucleotide sequence analysis of pepV, a carnosinase gene from Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial characterization of the enzyme." Vongerichten K.F., Klein J.R., Matern H., Plapp R. Microbiology 140:2591-2600(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION. Strain: DSM 7290 / WS87.

[2]

"Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides." Jozic D., Bourenkow G., Bartunik H., Scholze H., Dive V., Henrich B., Huber R., Bode W., Maskos K. Structure 10:1097-1106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC, COFACTOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z31377 Genomic DNA. Translation: CAA83252.1.

PIR

S57902.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LFW	X-ray	1.80	A	1-470	[»]

ProteinModelPortal

P45494.

SMR

P45494. Positions 1-468.

ModBase

Search...

Protein family/group databases

MEROPS

M20.004.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001261. ArgE/DapE_CS.
IPR011291. Pept_M20A_peptidaseV.
IPR010964. Pept_M20A_pepV-rel.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]

PANTHER

PTHR11014:SF6. PTHR11014:SF6. 1 hit.

Pfam

PF01546. Peptidase_M20. 1 hit.
[Graphical view]

SUPFAM

SSF55031. Peptidase_M20_dimer. 1 hit.

TIGRFAMs

TIGR01886. dipeptidase. 1 hit.
TIGR01887. dipeptidaselike. 1 hit.

PROSITE

PS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P45494.

Entry information

Entry name

PEPV_LACDL

Accession

Primary (citable) accession number: P45494

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program