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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)DescriptionActionsGraphical viewLength
Active sitei348Charge relay system1 Publication1
Active sitei468Charge relay system1
Active sitei498Charge relay system1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002202211 – 763Xaa-Pro dipeptidyl-peptidaseAdd BLAST763

Proteomic databases

PRIDEiP22346.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi416870.llmg_2328.

Structurei

Secondary structure

1763
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 22Combined sources10
Helixi33 – 42Combined sources10
Beta strandi44 – 46Combined sources3
Helixi48 – 50Combined sources3
Beta strandi54 – 56Combined sources3
Helixi59 – 64Combined sources6
Helixi71 – 81Combined sources11
Turni86 – 88Combined sources3
Helixi95 – 101Combined sources7
Helixi113 – 125Combined sources13
Beta strandi131 – 133Combined sources3
Helixi134 – 140Combined sources7
Helixi163 – 165Combined sources3
Beta strandi167 – 174Combined sources8
Beta strandi182 – 184Combined sources3
Beta strandi187 – 194Combined sources8
Beta strandi201 – 207Combined sources7
Helixi216 – 222Combined sources7
Beta strandi235 – 237Combined sources3
Helixi272 – 278Combined sources7
Turni279 – 281Combined sources3
Beta strandi283 – 287Combined sources5
Helixi304 – 317Combined sources14
Beta strandi323 – 326Combined sources4
Beta strandi338 – 347Combined sources10
Helixi349 – 358Combined sources10
Turni359 – 361Combined sources3
Beta strandi365 – 372Combined sources8
Helixi377 – 381Combined sources5
Beta strandi382 – 387Combined sources6
Helixi398 – 405Combined sources8
Helixi407 – 410Combined sources4
Helixi412 – 433Combined sources22
Turni435 – 437Combined sources3
Helixi442 – 445Combined sources4
Helixi449 – 455Combined sources7
Beta strandi458 – 465Combined sources8
Helixi474 – 482Combined sources9
Beta strandi489 – 495Combined sources7
Beta strandi504 – 506Combined sources3
Helixi509 – 521Combined sources13
Beta strandi532 – 536Combined sources5
Beta strandi540 – 542Combined sources3
Beta strandi544 – 548Combined sources5
Beta strandi555 – 560Combined sources6
Beta strandi562 – 565Combined sources4
Beta strandi567 – 572Combined sources6
Helixi576 – 584Combined sources9
Helixi586 – 594Combined sources9
Beta strandi601 – 606Combined sources6
Beta strandi611 – 615Combined sources5
Beta strandi618 – 628Combined sources11
Beta strandi631 – 645Combined sources15
Beta strandi650 – 657Combined sources8
Beta strandi659 – 662Combined sources4
Beta strandi666 – 670Combined sources5
Beta strandi673 – 687Combined sources15
Beta strandi690 – 692Combined sources3
Beta strandi705 – 710Combined sources6
Beta strandi714 – 718Combined sources5
Beta strandi723 – 730Combined sources8
Turni733 – 735Combined sources3
Beta strandi744 – 748Combined sources5
Helixi749 – 751Combined sources3
Beta strandi753 – 758Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LNSX-ray2.20A1-763[»]
ProteinModelPortaliP22346.
SMRiP22346.
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. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti50A → D in AAA25232 (PubMed:1674655).Curated1
Sequence conflicti130T → N in AAA25232 (PubMed:1674655).Curated1
Sequence conflicti367L → V in AAA25232 (PubMed:1674655).Curated1
Sequence conflicti573N → H in AAA25232 (PubMed:1674655).Curated1
Sequence conflicti649V → A in AAA25232 (PubMed:1674655).Curated1
Sequence conflicti681V → I in AAA25232 (PubMed:1674655).Curated1
Sequence conflicti692S → N in AAA25232 (PubMed:1674655).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LNSX-ray2.20A1-763[»]
ProteinModelPortaliP22346.
SMRiP22346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_2328.

Protein family/group databases

ESTHERilacla-pepx. Lactobacillus_peptidase.

Proteomic databases

PRIDEiP22346.

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. 1 hit.
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...

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: November 2, 2016
This is version 105 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.