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Protein

Beta-Ala-Xaa dipeptidase

Gene

pepV

Organism
Lactobacillus delbrueckii subsp. lactis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ 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.1 Publication

Enzyme regulationi

Fully inhibited by 1,10-phenanthroline or EDTA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Zinc 21 Publication
Active sitei89 – 891By similarity
Metal bindingi119 – 1191Zinc 11 Publication
Metal bindingi119 – 1191Zinc 21 Publication
Active sitei153 – 1531Proton acceptorCurated
Metal bindingi154 – 1541Zinc 11 Publication
Metal bindingi177 – 1771Zinc 21 Publication
Binding sitei350 – 3501Substrate
Metal bindingi439 – 4391Zinc 11 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM20.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-Ala-Xaa dipeptidase (EC:3.4.13.-)
Alternative name(s):
Beta-Ala-His dipeptidase
Peptidase V
Gene namesi
Name:pepV
OrganismiLactobacillus delbrueckii subsp. lactis
Taxonomic identifieri29397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Beta-Ala-Xaa dipeptidasePRO_0000185276Add
BLAST

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 106Combined sources
Helixi13 – 2412Combined sources
Helixi32 – 343Combined sources
Beta strandi37 – 393Combined sources
Helixi43 – 5816Combined sources
Beta strandi62 – 665Combined sources
Turni67 – 693Combined sources
Beta strandi70 – 756Combined sources
Beta strandi79 – 879Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi117 – 1204Combined sources
Helixi121 – 13717Combined sources
Beta strandi142 – 15110Combined sources
Turni153 – 1564Combined sources
Helixi158 – 1669Combined sources
Beta strandi171 – 18616Combined sources
Beta strandi188 – 1969Combined sources
Beta strandi204 – 2129Combined sources
Beta strandi221 – 2288Combined sources
Helixi232 – 24615Combined sources
Beta strandi249 – 2557Combined sources
Beta strandi258 – 2647Combined sources
Helixi273 – 2753Combined sources
Helixi279 – 2879Combined sources
Helixi294 – 30512Combined sources
Turni306 – 3094Combined sources
Turni314 – 3174Combined sources
Turni323 – 3253Combined sources
Beta strandi329 – 33810Combined sources
Beta strandi343 – 3519Combined sources
Helixi357 – 36812Combined sources
Turni369 – 3713Combined sources
Beta strandi372 – 3754Combined sources
Helixi390 – 40314Combined sources
Beta strandi409 – 4146Combined sources
Helixi417 – 4204Combined sources
Beta strandi444 – 4463Combined sources
Helixi447 – 46519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LFWX-ray1.80A1-470[»]
ProteinModelPortaliP45494.
SMRiP45494. Positions 1-468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45494.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Family and domain databases

Gene3Di3.30.70.360. 2 hits.
InterProiIPR001261. ArgE/DapE_CS.
IPR010964. M20A_pepV-rel.
IPR011291. Pept_M20A_peptidaseV.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01886. dipeptidase. 1 hit.
TIGR01887. dipeptidaselike. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45494-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLNFKELAE AKKDAILKDL EELIAIDSSE DLENATEEYP VGKGPVDAMT
60 70 80 90 100
KFLSFAKRDG FDTENFANYA GRVNFGAGDK RLGIIGHMDV VPAGEGWTRD
110 120 130 140 150
PFKMEIDEEG RIYGRGSADD KGPSLTAYYG MLLLKEAGFK PKKKIDFVLG
160 170 180 190 200
TNEETNWVGI DYYLKHEPTP DIVFSPDAEY PIINGEQGIF TLEFSFKNDD
210 220 230 240 250
TKGDYVLDKF KAGIATNVTP QVTRATISGP DLEAVKLAYE SFLADKELDG
260 270 280 290 300
SFEINDESAD IVLIGQGAHA SAPQVGKNSA TFLALFLDQY AFAGRDKNFL
310 320 330 340 350
HFLAEVEHED FYGKKLGIFH HDDLMGDLAS SPSMFDYEHA GKASLLNNVR
360 370 380 390 400
YPQGTDPDTM IKQVLDKFSG ILDVTYNGFE EPHYVPGSDP MVQTLLKVYE
410 420 430 440 450
KQTGKPGHEV VIGGGTYGRL FERGVAFGAQ PENGPMVMHA ANEFMMLDDL
460 470
ILSIAIYAEA IYELTKDEEL
Length:470
Mass (Da):51,990
Last modified:November 1, 1995 - v1
Checksum:i488117B4F33E4AB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31377 Genomic DNA. Translation: CAA83252.1.
PIRiS57902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31377 Genomic DNA. Translation: CAA83252.1.
PIRiS57902.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LFWX-ray1.80A1-470[»]
ProteinModelPortaliP45494.
SMRiP45494. Positions 1-468.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM20.004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP45494.

Family and domain databases

Gene3Di3.30.70.360. 2 hits.
InterProiIPR001261. ArgE/DapE_CS.
IPR010964. M20A_pepV-rel.
IPR011291. Pept_M20A_peptidaseV.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01886. dipeptidase. 1 hit.
TIGR01887. dipeptidaselike. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPEPV_LACDL
AccessioniPrimary (citable) accession number: P45494
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 14, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.