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Protein

Xaa-Pro dipeptidyl-peptidase

Gene

pepX

Organism
Lactobacillus helveticus (Lactobacillus suntoryeus)
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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei363 – 3631Charge relay systemUniRule annotation
Active sitei483 – 4831Charge relay systemUniRule annotation
Active sitei514 – 5141Charge relay systemUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Protein family/group databases

ESTHERilache-pepx. Lactobacillus_peptidase.
MEROPSiS15.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Xaa-Pro dipeptidyl-peptidaseUniRule annotation (EC:3.4.14.11UniRule annotation)
Alternative name(s):
X-Pro dipeptidyl-peptidaseUniRule annotation
X-prolyl-dipeptidyl aminopeptidaseUniRule annotation
Short name:
X-PDAPUniRule annotation
Gene namesi
Name:pepXUniRule annotation
OrganismiLactobacillus helveticus (Lactobacillus suntoryeus)
Taxonomic identifieri1587 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 793793Xaa-Pro dipeptidyl-peptidasePRO_0000220219Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi405566.lhv_1436.

Structurei

3D structure databases

ProteinModelPortaliQ59485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S15 family.UniRule annotation

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.
IPR005674. CocE/Ser_esterase.
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.
TIGRFAMsiTIGR00976. /NonD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59485-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYNQYAYVE TDFQQQVKEL IDINFLPKNY QVWDFSSLLA KLVKNAIAEA
60 70 80 90 100
KTDAAKNAKL AEFAVSDHQT LADFLKEKPT EIGTKQFYNV ALQLLGYHVH
110 120 130 140 150
YDYDFADPTG FMQRNALPFL QDISDNQKLI SAFYRLLNTR AKNGQILLDV
160 170 180 190 200
MAGKGYFTQF WGQNKFKFFN GKSIPVFDTN KVIREVVYVE TDLDTDHDGK
210 220 230 240 250
SDLIQVTVFR PEETNKGLKV PALYTASPYF GGIIANEKRN HNVDENLSDS
260 270 280 290 300
TEWNDPQYVH SPIVKAEKPD GSSRPATEEA VHKSSYPLNE YMLARGFASV
310 320 330 340 350
FAGAIGTRGS DGVRITGAPE ETESAAAVIE WLHGDRVAYT DRTRTVQTTA
360 370 380 390 400
DWCNGNIGMT GRSYLGTLQI AIATTGVKGL KTVVSEAAIS SWYDYYREHG
410 420 430 440 450
LVIAPEACQG EDLDLLAETC QSNLWDAGSY LKIKPEYDKM QKQLREKEDR
460 470 480 490 500
NTGQYSDFWE ARNYRHHADG IKCSWISVHG LNDWNVKPKN VYKIWQLVKK
510 520 530 540 550
MPMKHHLFLH QGPHYNMNNL VSIDFTDLMN LWFVHELLGI ENNAYNQWPT
560 570 580 590 600
VMIQDNLQAD KWHEEPDWSN DLGQEKIYYP TDEGELFQDG NGKAQKSFTD
610 620 630 640 650
VGGIEFKKAG ISESDWQYKF ICGDEKWAKP SLRFETDEFT HPTTIVGRPE
660 670 680 690 700
VKVRVSASLP KGEISVALVE LGERQRLTAT PKFLMHGGQE LGYRFGTDTL
710 720 730 740 750
QEFVPDKKTK AKLITKAHMN LQNFKDMKKP EAIDADKFYD LDFLLQPTYY
760 770 780 790
TIPSGSKLAL IIYSTDQGMT KRPLEDETYT IDLANTEIKF YEK
Length:793
Mass (Da):90,487
Last modified:November 1, 1996 - v1
Checksum:i585F6F0DB08B82A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851K → E in CAA88273 (PubMed:8574400).Curated
Sequence conflicti120 – 1201L → V in CAA88273 (PubMed:8574400).Curated
Sequence conflicti259 – 2591V → I in CAA88273 (PubMed:8574400).Curated
Sequence conflicti385 – 3851S → A in CAA88273 (PubMed:8574400).Curated
Sequence conflicti520 – 5201L → F in CAA88273 (PubMed:8574400).Curated
Sequence conflicti528 – 5281L → F in CAA88273 (PubMed:8574400).Curated
Sequence conflicti640 – 6401T → I in CAA88273 (PubMed:8574400).Curated
Sequence conflicti686 – 6861H → R in CAA88273 (PubMed:8574400).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22900 Genomic DNA. Translation: AAB50275.1.
Z48236 Genomic DNA. Translation: CAA88273.1.
RefSeqiWP_003629197.1. NZ_LSVJ01000182.1.

Genome annotation databases

GeneIDi16793804.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22900 Genomic DNA. Translation: AAB50275.1.
Z48236 Genomic DNA. Translation: CAA88273.1.
RefSeqiWP_003629197.1. NZ_LSVJ01000182.1.

3D structure databases

ProteinModelPortaliQ59485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi405566.lhv_1436.

Protein family/group databases

ESTHERilache-pepx. Lactobacillus_peptidase.
MEROPSiS15.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16793804.

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.
IPR005674. CocE/Ser_esterase.
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.
TIGRFAMsiTIGR00976. /NonD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "DNA sequence analysis, expression, distribution, and physiological role of the Xaa-prolyldipeptidyl aminopeptidase gene from Lactobacillus helveticus CNRZ32."
    Yuksel G.U., Steele J.L.
    Appl. Microbiol. Biotechnol. 44:766-773(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CNRZ 32.
  2. "An X-prolyl dipeptidyl aminopeptidase (pepX) gene from Lactobacillus helveticus."
    Vesanto E., Savijoki K., Rantanen T., Steele J.L., Palva A.
    Microbiology 141:3067-3075(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.

Entry informationi

Entry nameiPEPX_LACHE
AccessioniPrimary (citable) accession number: Q59485
Secondary accession number(s): Q48571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.