WORKLIST ENTRIES (1):

LEADERPTASE View alignment View Structure     Bacterial leader peptidase 1 (S26A) family signature
 Type of fingerprint: COMPOUND with 3  elements
Links:
   PRINTS; PR00722 CHYMOTRYPSIN; PR00861 ALYTICPTASE; PR00798 TOGAVIRIN
   PRINTS; PR00921 IGASERPTASE; PR00723 SUBTILISIN; PR00862 PROLIGOPTASE
   PRINTS; PR00724 CRBOXYPTASEC; PR00725 DADACBPTASE1; PR00922 DADACBPTASE3
   PRINTS; PR00923 LACTOPTASE; PR00830 ENDOLAPTASE; PR00726 LEXASERPTASE
   PRINTS; PR00728 SIGNALPTASE; PR00729 CDVENDOPTASE; PR00793 PROAMNOPTASE
   PRINTS; PR00995 CAPILLOPTASE; PR00127 CLPPROTEASEP
   INTERPRO; IPR000223
   PROSITE; PS00501 SPASE_I_1; PS00760 SPASE_I_2; PS00761 SPASE_I_3
   PFAM; PF00461 Peptidase_S26

 Creation date 10-MAY-1997; UPDATE 27-JUN-1999

   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).

   Proteolytic enzymes that exploit serine in their catalytic activity are
   ubiquitous, being found in viruses, bacteria and eukaryotes [1]. They 
   include a wide range of peptidase activity, including exopeptidase, endo-
   peptidase, oligopeptidase and omega-peptidase activity. Over 20 families
   (denoted S1-S26) of serine protease have been identified, these being
   grouped into 6 clans (SA, SB, SC, SE, SF and SG) on the basis of structural
   similarity and other functional evidence [1]. Structures are known for four
   of the clans (SA, SB, SC and SE): these appear to be totally unrelated,
   suggesting at least four evolutionary origins of serine peptidases and
   possibly many more [1].
   
   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].
   
   At least 3 eubacterial leader peptidases are known: murein prelipoprotein 
   peptidase, which cleaves the leader peptide from a component of the
   bacterial outer membrane; type IV prepilin leader peptidase; and the serine-
   dependent leader peptidase 1, which has the more general role of cleaving
   the leader peptide from a variety of secreted proteins and proteins directed
   to the periplasm and periplasmic membrane [1]. Leader peptidase 1 is
   similar to the eukaryotic signal peptidase, although the bacterial protein
   is monomeric, while the eukaryotic protein is multimeric [1].
   
   Mitochondria contain a similar two-subunit serine protease that removes
   leader peptides from nuclear- and mitochondrially-encoded proteins, which
   localise in the inner mitochondrial space [1]. The catalytic residues of a
   number of these peptides have been identified as a serine/lysine dyad [1].
   
   LEADERPTASE is a 3-element fingerprint that provides a signature for the 
   bacterial leader peptidase 1 (S26A) family. The fingerprint was derived from
   an initial alignment of 6 sequences: the motifs were drawn from conserved
   regions spanning virtually the full alignment length - motif 1 includes the
   region encoded by PROSITE pattern SPASE_I_1 (PS00501), which contains the
   catalytic serine; motif 2 includes the region encoded by PROSITE pattern
   SPASE_I_2 (PS00760), which contains the active lysine; and motif 3 includes
   the region encoded by PROSITE pattern SPASE_I_3 (PS00761), a conserved
   C-terminal region of unknown function. Two iterations on OWL29.3 were
   required to reach convergence, at which point a true set comprising 23
   sequences was identified. 
  
   An update on SPTR37_9f identified a true set of 42 sequences, and 2
   partial matches.

  SUMMARY INFORMATION
     42 codes involving  3 elements
      2 codes involving  2 elements

   COMPOSITE FINGERPRINT INDEX
  
    3|  42   42   42  
    2|   2    0    2  
   --+----------------
     |   1    2    3  

True positives..
 LEP_BACLI      LEP_PSEFL      LEPA_BACAM     LEPP_BACNA     
 LEP_ECOLI      O69160         LEP_BACAM      LEPT_BACSU     
 LEPQ_BACNA     LEPS_BACSU     LEP_SALTY      Q45225         
 LEP_HAEIN      P72660         O69886         O54237         
 P73157         LEP_MYCTU      O33021         O67088         
 LEP_STAAU      LEPC_BACCL     LEP_PHOLA      LEPU_BACSU     
 Q52697         O69885         O86869         O69884         
 O07560         O84023         O04348         LEP_STRPN      
 O69887         O86870         O83896         IMP1_YEAST     
 O25300         O83215         O74800         IMP2_YEAST     
 LEPH_STAAU     O51061         
Subfamily:  Codes involving 2 elements
 Subfamily True positives..
 O51062         O51278         


  PROTEIN TITLES
   LEP_BACLI        SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   LEP_PSEFL        SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   LEPA_BACAM       SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   LEPP_BACNA       SIGNAL PEPTIDASE I P (EC 3.4.21.89) (SPASE I) (LEADER PEPTID
   LEP_ECOLI        SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   O69160           PROKARYOTIC TYPE I SIGNAL PEPTIDASE SIPF - BRADYRHIZOBIUM JA
   LEP_BACAM        SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   LEPT_BACSU       SIGNAL PEPTIDASE I T (EC 3.4.21.89) (SPASE I) (LEADER PEPTID
   LEPQ_BACNA       SIGNAL PEPTIDASE I P (EC 3.4.21.89) (SPASE I) (LEADER PEPTID
   LEPS_BACSU       SIGNAL PEPTIDASE I S (EC 3.4.21.89) (SPASE I) (LEADER PEPTID
   LEP_SALTY        SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   Q45225           SIPS - BRADYRHIZOBIUM JAPONICUM.
   LEP_HAEIN        SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   P72660           LEADER PEPTIDASE I - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
   O69886           PUTATIVE SIGNAL PEPTIDASE I - STREPTOMYCES COELICOLOR, AND S
   O54237           SIGNAL PEPTIDASE I - STREPTOMYCES LIVIDANS.
   P73157           LEADER PEPTIDASE I - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
   LEP_MYCTU        PROBABLE SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER
   O33021           SIGNAL PEPTIDASE I - MYCOBACTERIUM LEPRAE.
   O67088           TYPE-I SIGNAL PEPTIDASE - AQUIFEX AEOLICUS.
   LEP_STAAU        SIGNAL PEPTIDASE IB (EC 3.4.21.89) (SPASE IB) (LEADER PEPTID
   LEPC_BACCL       SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   LEP_PHOLA        SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   LEPU_BACSU       SIGNAL PEPTIDASE I U (EC 3.4.21.89) (SPASE I) (LEADER PEPTID
   Q52697           LEADER PEPTIDASE - RHODOBACTER CAPSULATUS (RHODOPSEUDOMONAS 
   O69885           PUTATIVE SIGNAL PEPTIDASE I - STREPTOMYCES COELICOLOR.
   O86869           SIGNAL PEPTIDASE I - STREPTOMYCES LIVIDANS.
   O69884           PUTATIVE SIGNAL PEPTIDASE I - STREPTOMYCES COELICOLOR, AND S
   O07560           HYPOTHETICAL 19.0 KD PROTEIN - BACILLUS SUBTILIS.
   O84023           SIGNAL PEPTIDASE I - CHLAMYDIA TRACHOMATIS.
   O04348           CHLOROPLAST THYLAKOIDAL PROCESSING PEPTIDASE (LEADER PEPTIDA
   LEP_STRPN        SIGNAL PEPTIDASE I (EC 3.4.21.89) (SPASE I) (LEADER PEPTIDAS
   O69887           PUTATIVE SIGNAL PEPTIDASE I - STREPTOMYCES COELICOLOR.
   O86870           SIGNAL PEPTIDASE I - STREPTOMYCES LIVIDANS.
   O83896           SIGNAL PEPTIDASE I, PUTATIVE - TREPONEMA PALLIDUM.
   IMP1_YEAST       MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 1 (EC 3.4.99.-
   O25300           SIGNAL PEPTIDASE I (LEPB) - HELICOBACTER PYLORI (CAMPYLOBACT
   O83215           SIGNAL PEPTIDASE I (SIP) - TREPONEMA PALLIDUM.
   O74800           PUTATIVE MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 2 - S
   IMP2_YEAST       MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 2 (EC 3.4.99.-
   LEPH_STAAU       INACTIVE SIGNAL PEPTIDASE IA - STAPHYLOCOCCUS AUREUS.
   O51061           SIGNAL PEPTIDASE I (LEPB-1) - BORRELIA BURGDORFERI (LYME DIS
 
   O51062           SIGNAL PEPTIDASE I (LEPB-2) - BORRELIA BURGDORFERI (LYME DIS
   O51278           SIGNAL PEPTIDASE I (LEPB-3) - BORRELIA BURGDORFERI (LYME DIS

SCAN HISTORY OWL29_3 2 100 NSINGLE SPTR37_9f 2 100 NSINGLE INITIAL MOTIF SETS LEADERPTASE1 Length of motif = 17 Motif number = 1 Bacterial leader peptidase 1 motif I - 1 PCODE ST INT FLFEPYVVEGKSMDPTL LEPP_BACSU 33 33 FLFEPYLVEGTSMDPTL LEP_BACLI 33 33 FLFAPYVVDGESMEPTL LEPA_BACAM 34 34 FLVEPFQIPSGSMKPTL LEP_PSEFL 79 79 FLYEPFQIPSGSMMPTL LEP_SALTY 80 80 FVARPYLIPSESMEPTL LEP_MYCTU 85 85 LEADERPTASE2 Length of motif = 13 Motif number = 2 Bacterial leader peptidase 1 motif II - 1 PCODE ST INT YVKRLIGLPGDTV LEPP_BACSU 84 34 YVKRLIGLPGDTV LEP_BACLI 84 34 YVKRIIGLPGDTV LEPA_BACAM 83 32 YIKRVVGLPGDVV LEP_PSEFL 143 47 YIKRAVGLPGDKI LEP_SALTY 144 47 LVKRVIAVGGQTV LEP_MYCTU 172 70 LEADERPTASE3 Length of motif = 20 Motif number = 3 Bacterial leader peptidase 1 motif III - 1 PCODE ST INT VPKDKYFVMGDNRQESMDSR LEPP_BACSU 138 41 VPEGKYFVMGDNRQRSMDSR LEP_BACLI 138 41 VPDDKYFVMGDNRRNSMDSR LEPA_BACAM 137 41 VPAGHYFMMGDNRDNSNDSR LEP_PSEFL 216 60 VPPGQYFMMGDNRDNSADSR LEP_SALTY 264 107 VPPGRVWVMGDNRTHSADSR LEP_MYCTU 228 43 FINAL MOTIF SETS LEADERPTASE1 Length of motif = 17 Motif number = 1 Bacterial leader peptidase 1 motif I - 2 PCODE ST INT FLFEPYLVEGTSMDPTL LEP_BACLI 33 33 FLVEPFQIPSGSMKPTL LEP_PSEFL 79 79 FLFAPYVVDGESMEPTL LEPA_BACAM 34 34 FLFEPYVVEGKSMDPTL LEPP_BACNA 33 33 FIYEPFQIPSGSMMPTL LEP_ECOLI 80 80 FLFQPFNIPSGSMKATL O69160 33 33 FLFEPYLVEGSSMYPTL LEP_BACAM 40 40 FLFEPYLVEGSSMYPTL LEPT_BACSU 40 40 FLFEPYIVQGESMKPTL LEPQ_BACNA 32 32 FIFAPYVVDGDSMYPTL LEPS_BACSU 32 32 FLYEPFQIPSGSMMPTL LEP_SALTY 80 80 ALAEPFYVPSGSMEPTL Q45225 38 38 FLFEPFQIPSGSMESTL LEP_HAEIN 104 104 FVAEPRYIPSDSMLPTL P72660 33 33 FLVQAFSIPSSSMENTL O69886 103 103 FLVQAFSIPSSSMENTL O54237 58 58 FVAEARYIPSSSMEPTL P73157 41 41 FVARPYLIPSESMEPTL LEP_MYCTU 85 85 FVARPYLIPSESMEPTL O33021 73 73 YIAQAYTIPSASMEPTL O67088 21 21 FIVTPYTIKGESMDPTL LEP_STAAU 25 25 FVFSNYVVEGKSMMPTL LEPC_BACCL 27 27 FVAEARYIPSESMLPTL LEP_PHOLA 48 48 VFYKPFLIEGSSMAPTL LEPU_BACSU 35 35 LFFQPFWIPSGSMKDTL Q52697 29 29 FLVQAFVIPSGSMEQTI O69885 74 74 FLVQAFVIPSGSMEQTI O86869 74 74 FVLQPFQIPSGSMERGL O69884 66 66 AVFIDYKVEGVSMNPTF O07560 23 23 FWFELYEVPTGSMRPTI O84023 102 102 ALAEPKSIPSTSMYPTL O04348 173 173 FFWSNVRVEGHSMDPTL LEP_STRPN 27 27 VVYRPYTVPTSSMTPTI O69887 50 50 VVYRPYTVPTSSMTPTI O86870 50 50 FAFQLYVIPSESMVPSF O83896 76 76 YAYEFTETRGESMLPTL IMP1_YEAST 28 28 FIAQAFIIPSRSMVGTL O25300 27 27 HVVAAYRIQADSMQPTL O83215 40 40 YLFQVQMTSGPSMMPTL O74800 24 24 NVVHIAQVKGTSMQPTL IMP2_YEAST 30 30 FVIVGHVIPNNDMSPTL LEPH_STAAU 24 24 FVLQIFMIKSNEMLPTI O51061 37 37 LEADERPTASE2 Length of motif = 13 Motif number = 2 Bacterial leader peptidase 1 motif II - 2 PCODE ST INT YVKRLIGLPGDTV LEP_BACLI 84 34 YIKRVVGLPGDVV LEP_PSEFL 143 47 YVKRIIGLPGDTV LEPA_BACAM 83 32 YVKRLIGLPGDTV LEPP_BACNA 84 34 YIKRAVGLPGDKV LEP_ECOLI 144 47 YIKRVIGLPGDRV O69160 103 53 YVKRLIGKPGETV LEP_BACAM 91 34 YVKRLIGKPGETV LEPT_BACSU 91 34 YVKRLIGLPGDTI LEPQ_BACNA 83 34 YVKRIIGLPGDTV LEPS_BACSU 81 32 YIKRAVGLPGDKI LEP_SALTY 144 47 WVKRVVGLPGDRI Q45225 109 54 YIKRIVGKGGDRV LEP_HAEIN 194 73 FIKRVIALPGQTV P72660 92 42 LIKRVIGVAGDTV O69886 182 62 LIKRVIGVAGDTV O54237 137 62 FIKRIIGLPGDEV P73157 98 40 LVKRVIAVGGQTV LEP_MYCTU 172 70 LVKRVIAVGGQTV O33021 160 70 FIKRIIARGGDTV O67088 73 35 YVKRVIGVPGDKV LEP_STAAU 75 33 YVKRVIGLPGDRI LEPC_BACCL 77 33 FIKRVIGLPGETV LEP_PHOLA 107 42 FVKRLIGLPGDSI LEPU_BACSU 86 34 FIKRLIGLPGDRI Q52697 103 57 LIKRVVGVGGDHV O69885 159 68 LIKRVVGVGGDHV O86869 159 68 YIKRVVGVGGDHV O69884 120 37 LIKRVIGLPGETI O07560 73 33 YIKRCMGKPGDTV O84023 181 62 FIKRIVASEGDWV O04348 235 45 IVKRVIGMPGDTI LEP_STRPN 74 30 MVKRVVAVGGDTV O69887 100 33 MVKRVVAVGGDTV O86870 100 33 LVKRIVALPGEKV O83896 175 82 ICKRVTGMPGDLV IMP1_YEAST 81 36 YVKRNFAIGGDEV O25300 104 60 QMRRVVGLPGDTV O83215 122 65 VCKRIIGMPGDTI O74800 78 37 YCKRVKGLPFDTI IMP2_YEAST 89 42 YTSRIIAKPGQSM LEPH_STAAU 73 32 KVSRIAAVQGDSV O51061 111 57 LEADERPTASE3 Length of motif = 20 Motif number = 3 Bacterial leader peptidase 1 motif III - 2 PCODE ST INT VPEGKYFVMGDNRQRSMDSR LEP_BACLI 138 41 VPAGHYFMMGDNRDNSNDSR LEP_PSEFL 216 60 VPDDKYFVMGDNRRNSMDSR LEPA_BACAM 137 41 VPKDKYFVMGDNRQESMDSR LEPP_BACNA 138 41 VPPGQYFMMGDNRDNSADSR LEP_ECOLI 264 107 VPAGHFFMMGDNRDNSTDSR O69160 185 69 VPKGKYFVMGDNRLNSMDSR LEP_BACAM 145 41 VPKGKYFVMGDNRLNSMDSR LEPT_BACSU 145 41 VPKDKYFVMGDNRQNSMDSR LEPQ_BACNA 137 41 VPDNKYFVMGDNRRNSMDSR LEPS_BACSU 136 42 VPPGQYFMMGDNRDNSADSR LEP_SALTY 264 107 VPAGHLFVLGDNRDNSADSR Q45225 186 64 VPEGQYFVMGDHRDHSDDSR LEP_HAEIN 288 81 VPDGQVFVMGDNRNNSNDSH P72660 136 31 VPEGKIWVMGDHRQNSRDSR O69886 234 39 VPEGKIWVMGDHRQNSRDSR O54237 189 39 VPDDQYLVLGDNRNNSYDSH P73157 142 31 VPPGRVWVMGDNRTHSADSR LEP_MYCTU 228 43 VPQGRLWVMGDNRIHSADSR O33021 216 43 VPEGYYFVMGDNRDNSQDSR O67088 178 92 IPKGKYLVLGDNREVSKDSR LEP_STAAU 137 49 VPPGCIFVLGDNRLSSWDSR LEPC_BACCL 135 45 VPADSFLVLGDNRNNSYDSH LEP_PHOLA 151 31 VPSGKYFVMGDNRLNSLDSR LEPU_BACSU 139 40 VPEGQYFFMGDNRDNSEDSR Q52697 198 82 VPEGRLWVMGDHRSNSADSR O69885 207 35 VPEGRLWVMGDHRSNSADSR O86869 207 35 VPDGTLFVLGDHRSDSSDSR O69884 169 36 VPKGKYFVVGDNRIYSFDSR O07560 131 45 IPEGHVLVLGDNCPMSADSR O84023 543 349 VPKGYVFVLGDNRNKSFDSH O04348 279 31 VPEGEYLLLGDDRLVSSDSR LEP_STRPN 158 71 VPEGRLFLLGDERRNSVDST O69887 148 35 VPEGRLFLLGDERRNSVDST O86870 148 35 LPEHNYFMMGDNRLNSTDMR O83896 441 253 VPEGHVWVTGDNLSHSLDSR IMP1_YEAST 120 26 INDDEFFMIGDNRDNSSDSR O25300 207 90 LDEHSYFVLCDNRIVSSDSR O83215 188 53 IPLGHVWLAGDNIAHSLDSR O74800 103 12 LPRGHIWVEGDNYFHSIDSN IMP2_YEAST 114 12 IPPNNFVVLNDHDNNQHDSR LEPH_STAAU 125 39 LKKNEFFLLNDNLSVLNDSR O51061 167 43

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