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Protein

Xaa-Pro dipeptidyl-peptidase

Gene

pepX

Organism
Lactococcus lactis subsp. cremoris (Streptococcus cremoris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.

Catalytic activityi

Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei348 – 3481Charge relay system1 Publication
Active sitei468 – 4681Charge relay system
Active sitei498 – 4981Charge relay system

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.14.11. 2903.
3.4.14.5. 2903.

Protein family/group databases

ESTHERilacla-pepx. Lactobacillus_peptidase.

Names & Taxonomyi

Protein namesi
Recommended name:
Xaa-Pro dipeptidyl-peptidase (EC:3.4.14.11)
Alternative name(s):
X-Pro dipeptidyl-peptidase
X-prolyl-dipeptidyl aminopeptidase
Short name:
X-PDAP
Gene namesi
Name:pepX
OrganismiLactococcus lactis subsp. cremoris (Streptococcus cremoris)
Taxonomic identifieri1359 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 763763Xaa-Pro dipeptidyl-peptidasePRO_0000220221Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi416870.llmg_2328.

Structurei

Secondary structure

1
763
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2210Combined sources
Helixi33 – 4210Combined sources
Beta strandi44 – 463Combined sources
Helixi48 – 503Combined sources
Beta strandi54 – 563Combined sources
Helixi59 – 646Combined sources
Helixi71 – 8111Combined sources
Turni86 – 883Combined sources
Helixi95 – 1017Combined sources
Helixi113 – 12513Combined sources
Beta strandi131 – 1333Combined sources
Helixi134 – 1407Combined sources
Helixi163 – 1653Combined sources
Beta strandi167 – 1748Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi187 – 1948Combined sources
Beta strandi201 – 2077Combined sources
Helixi216 – 2227Combined sources
Beta strandi235 – 2373Combined sources
Helixi272 – 2787Combined sources
Turni279 – 2813Combined sources
Beta strandi283 – 2875Combined sources
Helixi304 – 31714Combined sources
Beta strandi323 – 3264Combined sources
Beta strandi338 – 34710Combined sources
Helixi349 – 35810Combined sources
Turni359 – 3613Combined sources
Beta strandi365 – 3728Combined sources
Helixi377 – 3815Combined sources
Beta strandi382 – 3876Combined sources
Helixi398 – 4058Combined sources
Helixi407 – 4104Combined sources
Helixi412 – 43322Combined sources
Turni435 – 4373Combined sources
Helixi442 – 4454Combined sources
Helixi449 – 4557Combined sources
Beta strandi458 – 4658Combined sources
Helixi474 – 4829Combined sources
Beta strandi489 – 4957Combined sources
Beta strandi504 – 5063Combined sources
Helixi509 – 52113Combined sources
Beta strandi532 – 5365Combined sources
Beta strandi540 – 5423Combined sources
Beta strandi544 – 5485Combined sources
Beta strandi555 – 5606Combined sources
Beta strandi562 – 5654Combined sources
Beta strandi567 – 5726Combined sources
Helixi576 – 5849Combined sources
Helixi586 – 5949Combined sources
Beta strandi601 – 6066Combined sources
Beta strandi611 – 6155Combined sources
Beta strandi618 – 62811Combined sources
Beta strandi631 – 64515Combined sources
Beta strandi650 – 6578Combined sources
Beta strandi659 – 6624Combined sources
Beta strandi666 – 6705Combined sources
Beta strandi673 – 68715Combined sources
Beta strandi690 – 6923Combined sources
Beta strandi705 – 7106Combined sources
Beta strandi714 – 7185Combined sources
Beta strandi723 – 7308Combined sources
Turni733 – 7353Combined sources
Beta strandi744 – 7485Combined sources
Helixi749 – 7513Combined sources
Beta strandi753 – 7586Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LNSX-ray2.20A1-763[»]
ProteinModelPortaliP22346.
SMRiP22346. Positions 1-763.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22346.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S15 family.Curated

Phylogenomic databases

eggNOGiENOG4105GYP. Bacteria.
ENOG410XPUZ. LUCA.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.40.50.1820. 3 hits.
HAMAPiMF_00698. Aminopeptidase_S15.
InterProiIPR029058. AB_hydrolase.
IPR008979. Galactose-bd-like.
IPR008252. Pept_S15_Xpro.
IPR015251. PepX_N_dom.
IPR000383. Xaa-Pro-like_dom.
IPR013736. Xaa-Pro_dipept_C.
[Graphical view]
PfamiPF02129. Peptidase_S15. 1 hit.
PF08530. PepX_C. 1 hit.
PF09168. PepX_N. 1 hit.
[Graphical view]
PRINTSiPR00923. LACTOPTASE.
SMARTiSM00939. PepX_C. 1 hit.
SM00940. PepX_N. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF53474. SSF53474. 1 hit.
SSF81761. SSF81761. 1 hit.

Sequencei

Sequence statusi: Complete.

P22346-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFNHFSIVD KNFDEQLAEL DQLGFRWSVF WDEKKILKDF LIQSPSDMTA
60 70 80 90 100
LQATAELDVI EFLKSSIELD WEIFWNIALQ LLDFVPNFDF EIGKAFEYAK
110 120 130 140 150
NSNLPQIEAE MTTENIISAF YYLLCTRRKT GMILVEHWVS EGLLPLDNHY
160 170 180 190 200
HFFNDKSLAT FDSSLLEREV LWVESPVDSE QRGENDLIKI QIIRPKSTEK
210 220 230 240 250
LPVVMTASPY HLGINDKAND LALHDMNVEL EEKTSHEIHV EQKLPQKLSA
260 270 280 290 300
KAKELPIVDK APYRFTHGWT YSLNDYFLTR GFASIYVAGV GTRSSDGFQT
310 320 330 340 350
SGDYQQIYSM TAVIDWLNGR ARAYTSRKKT HEIKASWANG KVAMTGKSYL
360 370 380 390 400
GTMAYGAATT GVEGLELILA EAGISSWYNY YRENGLVRSP GGFPGEDLDV
410 420 430 440 450
LAALTYSRNL DGADFLKGNA EYEKRLAEMT AALDRKSGDY NQFWHDRNYL
460 470 480 490 500
INTDKVKADV LIVHGLQDWN VTPEQAYNFW KALPEGHAKH AFLHRGAHIY
510 520 530 540 550
MNSWQSIDFS ETINAYFVAK LLDRDLNLNL PPVILQENSK DQVWTMMNDF
560 570 580 590 600
GANTQIKLPL GKTAVSFAQF DNNYDDETFK KYSKDFNVFK KDLFENKANE
610 620 630 640 650
AVIDLELPSM LTINGPVELE LRLKLNDTKG FLSAQILDFG QKKRLEDKVR
660 670 680 690 700
VKDFKVLDRG RNFMLDDLVE LPLVESPYQL VTKGFTNLQN QSLLTVSDLK
710 720 730 740 750
ADEWFTIKFE LQPTIYHLEK ADKLRVILYS TDFEHTVRDN RKVTYEIDLS
760
QSKLIIPIES VKN
Length:763
Mass (Da):87,697
Last modified:August 1, 1991 - v1
Checksum:iF89D81F88BDD7BEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501A → D in AAA25232 (PubMed:1674655).Curated
Sequence conflicti130 – 1301T → N in AAA25232 (PubMed:1674655).Curated
Sequence conflicti367 – 3671L → V in AAA25232 (PubMed:1674655).Curated
Sequence conflicti573 – 5731N → H in AAA25232 (PubMed:1674655).Curated
Sequence conflicti649 – 6491V → A in AAA25232 (PubMed:1674655).Curated
Sequence conflicti681 – 6811V → I in AAA25232 (PubMed:1674655).Curated
Sequence conflicti692 – 6921S → N in AAA25232 (PubMed:1674655).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35865 Genomic DNA. Translation: AAA25207.1.
M58315 Genomic DNA. Translation: AAA25232.1.
PIRiA43747.
A43748.
RefSeqiWP_011835997.1. NZ_LITG01000138.1.
WP_021165010.1. NZ_LIYE01000151.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35865 Genomic DNA. Translation: AAA25207.1.
M58315 Genomic DNA. Translation: AAA25232.1.
PIRiA43747.
A43748.
RefSeqiWP_011835997.1. NZ_LITG01000138.1.
WP_021165010.1. NZ_LIYE01000151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LNSX-ray2.20A1-763[»]
ProteinModelPortaliP22346.
SMRiP22346. Positions 1-763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_2328.

Protein family/group databases

ESTHERilacla-pepx. Lactobacillus_peptidase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105GYP. Bacteria.
ENOG410XPUZ. LUCA.

Enzyme and pathway databases

BRENDAi3.4.14.11. 2903.
3.4.14.5. 2903.

Miscellaneous databases

EvolutionaryTraceiP22346.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.40.50.1820. 3 hits.
HAMAPiMF_00698. Aminopeptidase_S15.
InterProiIPR029058. AB_hydrolase.
IPR008979. Galactose-bd-like.
IPR008252. Pept_S15_Xpro.
IPR015251. PepX_N_dom.
IPR000383. Xaa-Pro-like_dom.
IPR013736. Xaa-Pro_dipept_C.
[Graphical view]
PfamiPF02129. Peptidase_S15. 1 hit.
PF08530. PepX_C. 1 hit.
PF09168. PepX_N. 1 hit.
[Graphical view]
PRINTSiPR00923. LACTOPTASE.
SMARTiSM00939. PepX_C. 1 hit.
SM00940. PepX_N. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF53474. SSF53474. 1 hit.
SSF81761. SSF81761. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and DNA sequence analysis of an X-prolyl dipeptidyl aminopeptidase gene from Lactococcus lactis subsp. lactis NCDO 763."
    Nardi M., Chopin M.-C., Chopin A., Cals M.M., Gripon J.-C.
    Appl. Environ. Microbiol. 57:45-50(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCDO 763 / ML3.
  2. "Molecular cloning and sequence analysis of the X-prolyl dipeptidyl aminopeptidase gene from Lactococcus lactis subsp. cremoris."
    Mayo B., Kok J., Venema K., Bockelmann W., Teuber M., Reinke H., Venema G.
    Appl. Environ. Microbiol. 57:38-44(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25.
    Strain: P8-2-47.
  3. "Identification of the active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis."
    Chich J.-F., Chapot-Chartier M.P., Ribadeau-Dumas B., Gripon J.-C.
    FEBS Lett. 314:139-142(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE SER-348.
  4. "The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis."
    Rigolet P., Mechin I., Delage M.-M., Chich J.-F.
    Structure 10:1383-1394(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiPEPX_LACLC
AccessioniPrimary (citable) accession number: P22346
Secondary accession number(s): P22093
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 6, 2016
This is version 103 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, Direct protein sequencing

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.