SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR00923

Identifier
LACTOPTASE  [View Relations]  [View Alignment]  
Accession
PR00923
No. of Motifs
7
Creation Date
21-JUN-1998  (UPDATE 07-JUN-1999)
Title
Lactococcus X-Pro dipeptidyl-peptidase (S15) family signature 
Database References

INTERPRO; IPR000383
Literature References
1. RAWLINGS, N.D. AND BARRETT, A.J.
Families of serine peptidases.
METHODS ENZYMOL. 244 19-61 (1994).
 
2. RAWLINGS, N.D. AND BARRETT, A.J.
Evolutionary families of peptidases.
BIOCHEM.J. 290 205-218 (1993).
 
3. BAIROCH, A. AND RAWLINGS, N.
Classification of peptidase families and index of peptidase entries in
SWISS-PROT.
http://expasy.hcuge.ch/cgi-bin/lists?peptidas.txt

Documentation
Proteolytic enzymes that use serine in their catalytic machinery are 
widespread and numerous, being found in viruses, bacteria and eukaryotes
[1]. They encompass a range of peptidase activity, including exopeptidase,
endopeptidase, oligopeptidase and omega-peptidase. More than 20 serine
protease families (denoted S1 - S27) have been identified, which have been
grouped into 6 clans (SA, SB, SC, SE, SF and SG) on the basis of structural
and functional similarities [1]. Structures from four clans have been
examined (SA, SB, SC and SE): these appear to be unrelated, suggesting at 
least four evolutionary origins of serine peptidase, and possibly many more
[1]. Since that examination structural representaions from the other two 
clan members (SF, SG) have been determined [3].
 
Notwithstanding their different evolutionary origins, there are similarities
in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin
and carboxypeptidase C clans have a catalytic triad of serine, aspartate and
histidine in common: serine acts as a nucleophile, aspartate as an
electrophile, and histidine as a base [1]. The geometric orientations of
the catalytic residues are similar between families, despite different 
protein folds [1]. The linear arrangements of the catalytic residues
commonly reflect clan relationships. For example the catalytic triad in 
the chymotrypsin clan (SA) is ordered HDS, but is ordered DHS in the
subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [1,2].
 
Lactococcus X-Pro dipeptidyl-peptidase proteins belong to the S15 family of 
the carboxypeptidase (SC) clan [1,3]. These proteins, which have similar 
specificity to mammalian dipeptidyl-peptidase IV, cleave Xaa-Pro-|-X bonds, 
releasing N-terminal dipeptides. The penultimate residue must be proline. 
In Lactococcus, the proteins exist as cytoplasmic homodimers [1]. 
 
LACTOPTASE is a 7-element fingerprint that provides a signature for the 
Lactococcus X-Pro dipeptidyl-peptidase (S15) family of serine proteases. The
fingerprint was derived from an initial alignment of 3 sequences: the 
motifs were drawn from conserved regions spanning virtually the full 
alignment length. The active site serine lies in the region between motifs
4 and 5. Note that previously-reported positions for the active Asp and His
residues are not conserved in this alignment - however, other positions are
conserved and might be better candidates for these two active site residues. 
Two iterations on OWL30.1 were required to reach convergence, at which point
a true set comprising five sequences was identified.
 
An update on SPTR37_9f identified a true set of 5 sequences.
Summary Information
5 codes involving  7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
75555555
60000000
50000000
40000000
30000000
20000000
1234567
True Positives
PEPX_LACDL    PEPX_LACLA    PEPX_LACLC    Q48571        
Q59485
Sequence Titles
PEPX_LACDL  XAA-PRO DIPEPTIDYL-PEPTIDASE (EC 3.4.14.11) (X-PRO DIPEPTIDYL- PEPTIDASE) (X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE) - LACTOBACILLUS DELBRUECKII (SUBSP. LACTIS). 
PEPX_LACLA XAA-PRO DIPEPTIDYL-PEPTIDASE (EC 3.4.14.11) (X-PRO DIPEPTIDYL- PEPTIDASE) (X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE) (X-PDAP) - LACTOCOCCUS LACTIS (SUBSP. LACTIS) (STREPTOCOCCUS LACTIS).
PEPX_LACLC XAA-PRO DIPEPTIDYL-PEPTIDASE (EC 3.4.14.11) (X-PRO DIPEPTIDYL- PEPTIDASE) (X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE) (X-PDAP) - LACTOCOCCUS LACTIS (SUBSP. CREMORIS) (STREPTOCOCCUS CREMORIS).
Q48571 X-PROLYL DIPEPTIDYL AMINOPEPTIDASE - LACTOBACILLUS HELVETICUS.
Q59485 PEPX (EC 3.4.14.5) (DIPEPTIDYL-PEPTIDASE IV) (DIPEPTIDYL AMINOPEPTIDASE IV) (XAA-PRO-DIPEPTIDYLAMINOPEPTIDASE) (GLY-PRO NAPHTHYLAMIDASE) (POST-PROLINE DIPEPTIDYL AMINOPEPTIDASE IV) - LACTOBACILLUS HELVETICUS.
Scan History
OWL30_1    2  20   NSINGLE    
SPTR37_9f 2 6 NSINGLE
Initial Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
FFNGKSLPVFDTS PEPX_LACDL 168 168 -
FFNDKSLATFDSS PEPX_LACLA 152 152 -
FFNDKSLATFDSS PEPX_LACLC 152 152 -

Motif 2 width=11
Element Seqn Id St Int Rpt
REVVYVQSDLD PEPX_LACDL 184 3 -
REVLWVESPVD PEPX_LACLA 168 3 -
REVLWVESPVD PEPX_LACLC 168 3 -

Motif 3 width=10
Element Seqn Id St Int Rpt
DLLPVTVFRP PEPX_LACDL 202 7 -
DLIKIQIIRP PEPX_LACLA 186 7 -
DLIKIQIIRP PEPX_LACLC 186 7 -

Motif 4 width=17
Element Seqn Id St Int Rpt
KVPALYTASPYFGGIID PEPX_LACDL 219 7 -
KLPVVMTASPYHLGIND PEPX_LACLA 200 4 -
KLPVVMTASPYHLGIND PEPX_LACLC 200 4 -

Motif 5 width=17
Element Seqn Id St Int Rpt
EAAISSWYDYYREHGLV PEPX_LACDL 386 150 -
EAGISSWYNYYRENGLV PEPX_LACLA 371 154 -
EAGISSWYNYYRENGLV PEPX_LACLC 371 154 -

Motif 6 width=17
Element Seqn Id St Int Rpt
SIDFTDLMNLWFVHELL PEPX_LACDL 521 118 -
SIDFSETINAYFVAKLL PEPX_LACLA 506 118 -
SIDFSETINAYFVAKLL PEPX_LACLC 506 118 -

Motif 7 width=16
Element Seqn Id St Int Rpt
KLGLIIYSTDQGMTKR PEPX_LACDL 756 218 -
KLRVILYSTDFEHTVR PEPX_LACLA 723 200 -
KLRVILYSTDFEHTVR PEPX_LACLC 723 200 -
Final Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
FFNGKSIPVFDTN Q59485 168 168 -
FFNGKSIPVFDTN Q48571 168 168 -
FFNGKSLPVFDTS PEPX_LACDL 168 168 -
FFNDKSLATFDSS PEPX_LACLA 152 152 -
FFNDKSLATFDSS PEPX_LACLC 152 152 -

Motif 2 width=11
Element Seqn Id St Int Rpt
REVVYVETDLD Q59485 184 3 -
REVVYVETDLD Q48571 184 3 -
REVVYVQSDLD PEPX_LACDL 184 3 -
REVLWVESPVD PEPX_LACLA 168 3 -
REVLWVESPVD PEPX_LACLC 168 3 -

Motif 3 width=10
Element Seqn Id St Int Rpt
DLIQVTVFRP Q59485 202 7 -
DLIQVTVFRP Q48571 202 7 -
DLLPVTVFRP PEPX_LACDL 202 7 -
DLIKIQIIRP PEPX_LACLA 186 7 -
DLIKIQIIRP PEPX_LACLC 186 7 -

Motif 4 width=17
Element Seqn Id St Int Rpt
KVPALYTASPYFGGIIA Q59485 219 7 -
KVPALYTASPYFGGIIA Q48571 219 7 -
KVPALYTASPYFGGIID PEPX_LACDL 219 7 -
KLPVVMTASPYHLGIND PEPX_LACLA 200 4 -
KLPVVMTASPYHLGIND PEPX_LACLC 200 4 -

Motif 5 width=17
Element Seqn Id St Int Rpt
EAAISSWYDYYREHGLV Q59485 386 150 -
EAAISSWYDYYREHGLV Q48571 386 150 -
EAAISSWYDYYREHGLV PEPX_LACDL 386 150 -
EAGISSWYNYYRENGLV PEPX_LACLA 371 154 -
EAGISSWYNYYRENGLV PEPX_LACLC 371 154 -

Motif 6 width=17
Element Seqn Id St Int Rpt
SIDFTDLMNLWFVHELL Q59485 522 119 -
SIDFTDFMNLWFVHELL Q48571 522 119 -
SIDFTDLMNLWFVHELL PEPX_LACDL 521 118 -
SIDFSETINAYFVAKLL PEPX_LACLA 506 118 -
SIDFSETINAYFVAKLL PEPX_LACLC 506 118 -

Motif 7 width=16
Element Seqn Id St Int Rpt
KLALIIYSTDQGMTKR Q59485 757 218 -
KLALIIYSTDQGMTKR Q48571 757 218 -
KLGLIIYSTDQGMTKR PEPX_LACDL 756 218 -
KLRVILYSTDFEHTVR PEPX_LACLA 723 200 -
KLRVILYSTDFEHTVR PEPX_LACLC 723 200 -