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Conserved domains on  [gi|490280611|ref|WP_004176533|]
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MULTISPECIES: signal peptide peptidase SppA [Klebsiella]

Protein Classification

signal peptide peptidase SppA( domain architecture ID 11485121)

signal peptide peptidase A (SppA) is a membrane-bound serine protease that functions to cleave remnant signal peptides in the membrane left behind by the action of signal peptidases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10949 PRK10949
signal peptide peptidase SppA;
1-617 0e+00

signal peptide peptidase SppA;


:

Pssm-ID: 182860 [Multi-domain]  Cd Length: 618  Bit Score: 1325.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611   1 MRTLWRLIASFFKWTWRILNFIRKLALNAIFLVLVLVCIGIWSQFSS-TTSEHAARGALLLDITGVVVDKPSASSKLGVI 79
Cdd:PRK10949   1 MRTLWRIIAGFFKWTWRLLNFVRELVLNLFFIFLILVGVGIWMQVSNgDTPETASRGALLLDISGVIVDKPSSSNKLSQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  80 GRQLFGASSDRLQENSLFDIVQTIRQAKDDRNITGIVLDLKNFVGGDQPSMQYIGKALREFRDSGKPVYAVGSSYSQGQY 159
Cdd:PRK10949  81 GRQLLGASSDRLQENSLFDIVNTIRQAKDDRNITGIVLDLKNFAGADQPSMQYIGKALREFRDSGKPVYAVGDSYSQGQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 160 YLASFANKIWLSPQGEVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYL 239
Cdd:PRK10949 161 YLASFANKIYLSPQGVVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 240 NTIAANRQITAQQLFPGALGIIDGLRKVGGDTAKYALDNKLVDELATSTEVEKALTKQFGWSKADNNYRAISYYDYNVKT 319
Cdd:PRK10949 241 NTVAANRQITPQQLFPGAQGILEGLTKVGGDTAKYALDNKLVDALASSAEIEKALTKAFGWSKTDKNYRAISIYDYALKT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 320 PSDQGSAIAVIFANGAIMDGEETPGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVV 399
Cdd:PRK10949 321 PADTGGSIAVIFANGAIMDGEETPGNVGGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAGKPVV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 400 VSMGGMAASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADVSSTKALPPEVQQLMQLS 479
Cdd:PRK10949 401 VSMGGMAASGGYWISTPANYIVASPSTLTGSIGIFGVINTVENSLDSIGVHTDGVSTSPLADVSITKALPPEFQQMMQLS 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 480 IENGYQRFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAKLKTWHLNYYQEEPTFFSMV 559
Cdd:PRK10949 481 IENGYKRFITLVADSRHKTPEQIDKIAQGHVWTGQDAKANGLVDSLGDFDDAVAKAAELAKLKQWHLNWYVDEPTFFDMV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490280611 560 LDSLTGSVRASLPAAIQAWLPAPVAAAAETVKAESDKLAAFNDPQNRYAFCLTCANIR 617
Cdd:PRK10949 561 MDQMSGSVRAMLPDAIQAMLPAPLASVASTVKSESDKLAAFNDPQNRYAFCLTCANVR 618
 
Name Accession Description Interval E-value
PRK10949 PRK10949
signal peptide peptidase SppA;
1-617 0e+00

signal peptide peptidase SppA;


Pssm-ID: 182860 [Multi-domain]  Cd Length: 618  Bit Score: 1325.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611   1 MRTLWRLIASFFKWTWRILNFIRKLALNAIFLVLVLVCIGIWSQFSS-TTSEHAARGALLLDITGVVVDKPSASSKLGVI 79
Cdd:PRK10949   1 MRTLWRIIAGFFKWTWRLLNFVRELVLNLFFIFLILVGVGIWMQVSNgDTPETASRGALLLDISGVIVDKPSSSNKLSQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  80 GRQLFGASSDRLQENSLFDIVQTIRQAKDDRNITGIVLDLKNFVGGDQPSMQYIGKALREFRDSGKPVYAVGSSYSQGQY 159
Cdd:PRK10949  81 GRQLLGASSDRLQENSLFDIVNTIRQAKDDRNITGIVLDLKNFAGADQPSMQYIGKALREFRDSGKPVYAVGDSYSQGQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 160 YLASFANKIWLSPQGEVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYL 239
Cdd:PRK10949 161 YLASFANKIYLSPQGVVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 240 NTIAANRQITAQQLFPGALGIIDGLRKVGGDTAKYALDNKLVDELATSTEVEKALTKQFGWSKADNNYRAISYYDYNVKT 319
Cdd:PRK10949 241 NTVAANRQITPQQLFPGAQGILEGLTKVGGDTAKYALDNKLVDALASSAEIEKALTKAFGWSKTDKNYRAISIYDYALKT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 320 PSDQGSAIAVIFANGAIMDGEETPGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVV 399
Cdd:PRK10949 321 PADTGGSIAVIFANGAIMDGEETPGNVGGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAGKPVV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 400 VSMGGMAASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADVSSTKALPPEVQQLMQLS 479
Cdd:PRK10949 401 VSMGGMAASGGYWISTPANYIVASPSTLTGSIGIFGVINTVENSLDSIGVHTDGVSTSPLADVSITKALPPEFQQMMQLS 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 480 IENGYQRFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAKLKTWHLNYYQEEPTFFSMV 559
Cdd:PRK10949 481 IENGYKRFITLVADSRHKTPEQIDKIAQGHVWTGQDAKANGLVDSLGDFDDAVAKAAELAKLKQWHLNWYVDEPTFFDMV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490280611 560 LDSLTGSVRASLPAAIQAWLPAPVAAAAETVKAESDKLAAFNDPQNRYAFCLTCANIR 617
Cdd:PRK10949 561 MDQMSGSVRAMLPDAIQAMLPAPLASVASTVKSESDKLAAFNDPQNRYAFCLTCANVR 618
SppA_67K TIGR00705
signal peptide peptidase SppA, 67K type; This model represents the signal peptide peptidase A ...
16-608 0e+00

signal peptide peptidase SppA, 67K type; This model represents the signal peptide peptidase A (SppA, protease IV) as found in E. coli, Treponema pallidum, Mycobacterium leprae, and several other species, in which it has a molecular mass around 67 kDa and a duplication such that the N-terminal half shares extensive homology with the C-terminal half. This enzyme was shown in E. coli to form homotetramers. E. coli SohB, which is most closely homologous to the C-terminal duplication of SppA, is predicted to perform a similar function of small peptide degradation, but in the periplasm. Many prokaryotes have a single SppA/SohB homolog that may perform the function of either or both. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273226 [Multi-domain]  Cd Length: 584  Bit Score: 840.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611   16 WRILNFIRKLALNAIFLVLVLVCIGIWSQFSS--TTSEHAARGALLLDITgvVVDKPSASSKLGVIgRQLFGASSDRlqE 93
Cdd:TIGR00705   1 WMVLNFVRLLVLNVVFLLLVLLGVKILVGDSSgrPSQKLVSSGALLLDLP--VGDVTDQSPRVSLQ-GTLLGNPKGR--A 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611   94 NSLFDIVQTIRQAKDDRNITGIVLDLKNFVGGDQPSMQYIGKALREFRDSGKPVYAVGSSYSQGQYYLASFANKIWLSPQ 173
Cdd:TIGR00705  76 ISLFDIVNAIRQAADDRRIEGLVFDLSNFSGWDSPHLVEIGSALSEFKDSGKPVYAYGTNYSQGQYYLASFADEIILNPM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  174 GEVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYLNTIAANRQITAQQL 253
Cdd:TIGR00705 156 GSVDLHGFYTETLFYKGMLDKLGVRWH*FRVGTYKGAVEPFSRKDMSPEARRNYQRWLGELWQNYLSSVSRNRAIPVQQL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  254 FPGALGIIDGLRKVGGDTAKYALDNKLVDELATSTEVEKALTKQFGWSkADNNYRAISYYDYNVKTP--SDQGSAIAVIF 331
Cdd:TIGR00705 236 APYAQGLLELLQKLNGDGARYALAEKLVTAVCSYAEAGKALKFLFEDD-YDKAKNFISLDDYNRDRPqrHDVQDKIGIVH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  332 ANGAIMDGEETPGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVVVSMGGMAASGGY 411
Cdd:TIGR00705 315 LEGPIADGRDTEGNTGGDTVAALLRVARSDPDIKAVVLRINSPGGSVFASEIIRRELARAQARGKPVIVSMGAMAASGGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  412 WISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADVSSTKALPPEVQQLMQLSIENGYQRFITLV 491
Cdd:TIGR00705 395 WIASAADYIVASPNTITGSIGVFSVLPTFENSLDRIGVHVDGVSTHELANVSLLRPLTAEDQAIMQLSVEAGYRRFLSVV 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  492 ANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAKL-KTWHLNYYQEEPTFFSMVLDSLTGsvraS 570
Cdd:TIGR00705 475 SAGRNLTPTQVDKVAQGRVWTGEDAVSNGLVDALGGLDEAVAKAAKLAHCrEQWSVEVYKDSATLGSELLQNLWD----G 550
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 490280611  571 LPAAIQAWLPAPVAaaaeTVKAESDKLAAFNDPQNRYA 608
Cdd:TIGR00705 551 LQKRSLAFLPAPLV----ILEREWGELAQFNDPKGTYA 584
S49_SppA_1 cd07019
Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal ...
326-536 2.21e-108

Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppAs in this subfamily are found in all three domains of life and are involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Site-directed mutagenesis and sequence analysis have shown these bacterial, archaeal and thylakoid SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain, similar to Arabidopsis thaliana SppA1 peptidase. Others, including sohB peptidase, protein C and archaeal signal peptide peptidase, do not contain the amino-terminal domain. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain.


Pssm-ID: 132930 [Multi-domain]  Cd Length: 211  Bit Score: 324.67  E-value: 2.21e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 326 AIAVIFANGAIMDGEETPGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVVVSMGGM 405
Cdd:cd07019    1 SIGVVFANGAIVDGEETQGNVGGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAGKPVVVSAGGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 406 AASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADVSSTKALPPEVQQLMQLSIENGYQ 485
Cdd:cd07019   81 AASGGYWISTPANYIVANPSTLTGSIGIFGVITTVENSLDSIGVHTDGVSTSPLADVSITRALPPEAQLGLQLSIENGYK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490280611 486 RFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAA 536
Cdd:cd07019  161 RFITLVADARHSTPEQIDKIAQGHVWTGQDAKANGLVDSLGDFDDAVAKAA 211
SppA COG0616
Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, ...
318-528 7.73e-88

Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440381 [Multi-domain]  Cd Length: 215  Bit Score: 272.05  E-value: 7.73e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 318 KTPSDQGSAIAVIFANGAIMDGEETP-GNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGK 396
Cdd:COG0616    3 ARPPKVKPSIAVIDLEGTIVDGGGPPsGEIGLEDILAALRKAAEDPDVKAVVLRINSPGGSVAASEEIRDALRRLRAKGK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 397 PVVVSMGGMAASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLAD-VSSTKALPPEVQQL 475
Cdd:COG0616   83 PVVASMGDVAASGGYYIASAADKIYANPTTITGSIGVIAQGPNFKGLLEKLGVEVEVVTAGEYKDaLSPFRPLSEEEREQ 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490280611 476 MQLSIENGYQRFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDF 528
Cdd:COG0616  163 LQALLDDIYDQFVEDVAEGRGLSLEEVREIADGRVWTGEQALELGLVDELGTL 215
Peptidase_S49 pfam01343
Peptidase family S49;
390-542 4.00e-61

Peptidase family S49;


Pssm-ID: 396077  Cd Length: 154  Bit Score: 199.82  E-value: 4.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  390 AAKAAGKPVVVSMGGMAASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLAD-VSSTKAL 468
Cdd:pfam01343   1 ALLDAGKPVVASAGNYAASGGYYLASAADKIVANPSTIVGSIGVITQGLNVENLLDKLGVSVDTIRAGEYKDaGSPRREL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490280611  469 PPEVQQLMQLSIENGYQRFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAKLK 542
Cdd:pfam01343  81 TPEEREILQRMLDETYQLFVQTVAKNRNLPVDQVDKIAQGRVWTGQQALKLGLVDELGTSDDAVTRAAELAGVK 154
 
Name Accession Description Interval E-value
PRK10949 PRK10949
signal peptide peptidase SppA;
1-617 0e+00

signal peptide peptidase SppA;


Pssm-ID: 182860 [Multi-domain]  Cd Length: 618  Bit Score: 1325.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611   1 MRTLWRLIASFFKWTWRILNFIRKLALNAIFLVLVLVCIGIWSQFSS-TTSEHAARGALLLDITGVVVDKPSASSKLGVI 79
Cdd:PRK10949   1 MRTLWRIIAGFFKWTWRLLNFVRELVLNLFFIFLILVGVGIWMQVSNgDTPETASRGALLLDISGVIVDKPSSSNKLSQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  80 GRQLFGASSDRLQENSLFDIVQTIRQAKDDRNITGIVLDLKNFVGGDQPSMQYIGKALREFRDSGKPVYAVGSSYSQGQY 159
Cdd:PRK10949  81 GRQLLGASSDRLQENSLFDIVNTIRQAKDDRNITGIVLDLKNFAGADQPSMQYIGKALREFRDSGKPVYAVGDSYSQGQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 160 YLASFANKIWLSPQGEVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYL 239
Cdd:PRK10949 161 YLASFANKIYLSPQGVVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 240 NTIAANRQITAQQLFPGALGIIDGLRKVGGDTAKYALDNKLVDELATSTEVEKALTKQFGWSKADNNYRAISYYDYNVKT 319
Cdd:PRK10949 241 NTVAANRQITPQQLFPGAQGILEGLTKVGGDTAKYALDNKLVDALASSAEIEKALTKAFGWSKTDKNYRAISIYDYALKT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 320 PSDQGSAIAVIFANGAIMDGEETPGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVV 399
Cdd:PRK10949 321 PADTGGSIAVIFANGAIMDGEETPGNVGGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAGKPVV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 400 VSMGGMAASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADVSSTKALPPEVQQLMQLS 479
Cdd:PRK10949 401 VSMGGMAASGGYWISTPANYIVASPSTLTGSIGIFGVINTVENSLDSIGVHTDGVSTSPLADVSITKALPPEFQQMMQLS 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 480 IENGYQRFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAKLKTWHLNYYQEEPTFFSMV 559
Cdd:PRK10949 481 IENGYKRFITLVADSRHKTPEQIDKIAQGHVWTGQDAKANGLVDSLGDFDDAVAKAAELAKLKQWHLNWYVDEPTFFDMV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490280611 560 LDSLTGSVRASLPAAIQAWLPAPVAAAAETVKAESDKLAAFNDPQNRYAFCLTCANIR 617
Cdd:PRK10949 561 MDQMSGSVRAMLPDAIQAMLPAPLASVASTVKSESDKLAAFNDPQNRYAFCLTCANVR 618
SppA_67K TIGR00705
signal peptide peptidase SppA, 67K type; This model represents the signal peptide peptidase A ...
16-608 0e+00

signal peptide peptidase SppA, 67K type; This model represents the signal peptide peptidase A (SppA, protease IV) as found in E. coli, Treponema pallidum, Mycobacterium leprae, and several other species, in which it has a molecular mass around 67 kDa and a duplication such that the N-terminal half shares extensive homology with the C-terminal half. This enzyme was shown in E. coli to form homotetramers. E. coli SohB, which is most closely homologous to the C-terminal duplication of SppA, is predicted to perform a similar function of small peptide degradation, but in the periplasm. Many prokaryotes have a single SppA/SohB homolog that may perform the function of either or both. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273226 [Multi-domain]  Cd Length: 584  Bit Score: 840.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611   16 WRILNFIRKLALNAIFLVLVLVCIGIWSQFSS--TTSEHAARGALLLDITgvVVDKPSASSKLGVIgRQLFGASSDRlqE 93
Cdd:TIGR00705   1 WMVLNFVRLLVLNVVFLLLVLLGVKILVGDSSgrPSQKLVSSGALLLDLP--VGDVTDQSPRVSLQ-GTLLGNPKGR--A 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611   94 NSLFDIVQTIRQAKDDRNITGIVLDLKNFVGGDQPSMQYIGKALREFRDSGKPVYAVGSSYSQGQYYLASFANKIWLSPQ 173
Cdd:TIGR00705  76 ISLFDIVNAIRQAADDRRIEGLVFDLSNFSGWDSPHLVEIGSALSEFKDSGKPVYAYGTNYSQGQYYLASFADEIILNPM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  174 GEVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYLNTIAANRQITAQQL 253
Cdd:TIGR00705 156 GSVDLHGFYTETLFYKGMLDKLGVRWH*FRVGTYKGAVEPFSRKDMSPEARRNYQRWLGELWQNYLSSVSRNRAIPVQQL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  254 FPGALGIIDGLRKVGGDTAKYALDNKLVDELATSTEVEKALTKQFGWSkADNNYRAISYYDYNVKTP--SDQGSAIAVIF 331
Cdd:TIGR00705 236 APYAQGLLELLQKLNGDGARYALAEKLVTAVCSYAEAGKALKFLFEDD-YDKAKNFISLDDYNRDRPqrHDVQDKIGIVH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  332 ANGAIMDGEETPGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVVVSMGGMAASGGY 411
Cdd:TIGR00705 315 LEGPIADGRDTEGNTGGDTVAALLRVARSDPDIKAVVLRINSPGGSVFASEIIRRELARAQARGKPVIVSMGAMAASGGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  412 WISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADVSSTKALPPEVQQLMQLSIENGYQRFITLV 491
Cdd:TIGR00705 395 WIASAADYIVASPNTITGSIGVFSVLPTFENSLDRIGVHVDGVSTHELANVSLLRPLTAEDQAIMQLSVEAGYRRFLSVV 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  492 ANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAKL-KTWHLNYYQEEPTFFSMVLDSLTGsvraS 570
Cdd:TIGR00705 475 SAGRNLTPTQVDKVAQGRVWTGEDAVSNGLVDALGGLDEAVAKAAKLAHCrEQWSVEVYKDSATLGSELLQNLWD----G 550
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 490280611  571 LPAAIQAWLPAPVAaaaeTVKAESDKLAAFNDPQNRYA 608
Cdd:TIGR00705 551 LQKRSLAFLPAPLV----ILEREWGELAQFNDPKGTYA 584
S49_SppA_1 cd07019
Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal ...
326-536 2.21e-108

Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppAs in this subfamily are found in all three domains of life and are involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Site-directed mutagenesis and sequence analysis have shown these bacterial, archaeal and thylakoid SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain, similar to Arabidopsis thaliana SppA1 peptidase. Others, including sohB peptidase, protein C and archaeal signal peptide peptidase, do not contain the amino-terminal domain. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain.


Pssm-ID: 132930 [Multi-domain]  Cd Length: 211  Bit Score: 324.67  E-value: 2.21e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 326 AIAVIFANGAIMDGEETPGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVVVSMGGM 405
Cdd:cd07019    1 SIGVVFANGAIVDGEETQGNVGGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAGKPVVVSAGGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 406 AASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADVSSTKALPPEVQQLMQLSIENGYQ 485
Cdd:cd07019   81 AASGGYWISTPANYIVANPSTLTGSIGIFGVITTVENSLDSIGVHTDGVSTSPLADVSITRALPPEAQLGLQLSIENGYK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490280611 486 RFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAA 536
Cdd:cd07019  161 RFITLVADARHSTPEQIDKIAQGHVWTGQDAKANGLVDSLGDFDDAVAKAA 211
S49_SppA_67K_type cd07018
Signal peptide peptidase A (SppA) 67K type, a serine protease, has catalytic Ser-Lys dyad; ...
58-296 3.92e-98

Signal peptide peptidase A (SppA) 67K type, a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 67K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily contain an amino-terminal domain in addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members (sometimes referred to as 67K type), similar to E. coli and Arabidopsis thaliana SppA peptidases. Unlike the eukaryotic functional homologs that are proposed to be aspartic proteases, site-directed mutagenesis and sequence analysis have shown that members in this subfamily, mostly bacterial, are serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain.


Pssm-ID: 132929 [Multi-domain]  Cd Length: 222  Bit Score: 298.69  E-value: 3.92e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  58 LLLDITGVVVDKPSASSklgvigrqLFGASSDRLQENSLFDIVQTIRQAKDDRNITGIVLDLKNFVGGdQPSMQYIGKAL 137
Cdd:cd07018    1 LVLDLSGSLVEQPPPSP--------PLLLGGGESSELSLRDLLEALEKAAEDDRIKGIVLDLDGLSGG-LAKLEELRQAL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 138 REFRDSGKPVYAVGSSYSQGQYYLASFANKIWLSPQGEVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRD 217
Cdd:cd07018   72 ERFRASGKPVIAYADGYSQGQYYLASAADEIYLNPSGSVELTGLSAETLFFKGLLDKLGVEVQVFRVGEYKSAVEPFTRD 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490280611 218 DMSPAAREADSRWIGELWQNYLNTIAANRQITAQQLfpgalgiiDGLRKVGGDTAKYALDNKLVDELATSTEVEKALTK 296
Cdd:cd07018  152 DMSPEAREQTQALLDSLWDQYLADVAASRGLSPDAL--------EALIDLGGDSAEEALEAGLVDGLAYRDELEARLKE 222
S49_Sppa_N_C cd07023
Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal ...
327-536 8.38e-98

Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. This subfamily contains members with either a single domain (sometimes referred to as 36K type), such as sohB peptidase, protein C and archaeal signal peptide peptidase, or an amino-terminal domain in addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members (sometimes referred to as 67K type), similar to E. coli and Arabidopsis thaliana SppA peptidases. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain.


Pssm-ID: 132934 [Multi-domain]  Cd Length: 208  Bit Score: 297.48  E-value: 8.38e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 327 IAVIFANGAIMDGeetpGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVVVSMGGMA 406
Cdd:cd07023    2 IAVIDIEGTISDG----GGIGADSLIEQLRKAREDDSVKAVVLRINSPGGSVVASEEIYREIRRLRKAKKPVVASMGDVA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 407 ASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADV-SSTKALPPEVQQLMQLSIENGYQ 485
Cdd:cd07023   78 ASGGYYIAAAADKIVANPTTITGSIGVIGQGPNLEELLDKLGIERDTIKSGPGKDKgSPDRPLTEEERAILQALVDDIYD 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490280611 486 RFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAA 536
Cdd:cd07023  158 QFVDVVAEGRGMSGERLDKLADGRVWTGRQALELGLVDELGGLDDAIAKAA 208
SppA COG0616
Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, ...
318-528 7.73e-88

Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440381 [Multi-domain]  Cd Length: 215  Bit Score: 272.05  E-value: 7.73e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 318 KTPSDQGSAIAVIFANGAIMDGEETP-GNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGK 396
Cdd:COG0616    3 ARPPKVKPSIAVIDLEGTIVDGGGPPsGEIGLEDILAALRKAAEDPDVKAVVLRINSPGGSVAASEEIRDALRRLRAKGK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 397 PVVVSMGGMAASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLAD-VSSTKALPPEVQQL 475
Cdd:COG0616   83 PVVASMGDVAASGGYYIASAADKIYANPTTITGSIGVIAQGPNFKGLLEKLGVEVEVVTAGEYKDaLSPFRPLSEEEREQ 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490280611 476 MQLSIENGYQRFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDF 528
Cdd:COG0616  163 LQALLDDIYDQFVEDVAEGRGLSLEEVREIADGRVWTGEQALELGLVDELGTL 215
S49_SppA cd07014
Signal peptide peptidase A; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): ...
329-536 1.66e-64

Signal peptide peptidase A; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppA is an intramembrane enzyme found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Unlike the eukaryotic functional homologs that are proposed to be aspartic proteases, site-directed mutagenesis and sequence analysis have shown these bacterial, archaeal and thylakoid SppAs to be ClpP-like serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain, cleaving peptide bonds in the plane of the lipid bilayer. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain (sometimes referred to as 67K type). Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain (sometimes referred to as 36K type). Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain. This family also contains homologs that either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity of peptidases.


Pssm-ID: 132925 [Multi-domain]  Cd Length: 177  Bit Score: 209.78  E-value: 1.66e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 329 VIFANGAIMDGEE----TPGNVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVVVSMGG 404
Cdd:cd07014    1 VVFANGVIVDGEEsssdTQGNVSGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAGKPVVASGGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 405 MAASGGYWISTPADYIVANPSTLTGSIGIFGVintventlgsigvhtdgvatspladvsstkalppevQQLMQLSIENGY 484
Cdd:cd07014   81 NAASGGYWISTPANYIVANPSTLVGSIGIFGV------------------------------------QLADQLSIENGY 124
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490280611 485 QRFITLVANARKSTPEK-IDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAA 536
Cdd:cd07014  125 KRFITLVADNRHSTPEQqIDKIAQGGVWTGQDAKANGLVDSLGSFDDAVAKLA 177
Peptidase_S49 pfam01343
Peptidase family S49;
390-542 4.00e-61

Peptidase family S49;


Pssm-ID: 396077  Cd Length: 154  Bit Score: 199.82  E-value: 4.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  390 AAKAAGKPVVVSMGGMAASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLAD-VSSTKAL 468
Cdd:pfam01343   1 ALLDAGKPVVASAGNYAASGGYYLASAADKIVANPSTIVGSIGVITQGLNVENLLDKLGVSVDTIRAGEYKDaGSPRREL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490280611  469 PPEVQQLMQLSIENGYQRFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAKLK 542
Cdd:pfam01343  81 TPEEREILQRMLDETYQLFVQTVAKNRNLPVDQVDKIAQGRVWTGQQALKLGLVDELGTSDDAVTRAAELAGVK 154
S49_SppA cd07014
Signal peptide peptidase A; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): ...
59-295 1.46e-60

Signal peptide peptidase A; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppA is an intramembrane enzyme found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Unlike the eukaryotic functional homologs that are proposed to be aspartic proteases, site-directed mutagenesis and sequence analysis have shown these bacterial, archaeal and thylakoid SppAs to be ClpP-like serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain, cleaving peptide bonds in the plane of the lipid bilayer. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain (sometimes referred to as 67K type). Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain (sometimes referred to as 36K type). Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain. This family also contains homologs that either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity of peptidases.


Pssm-ID: 132925 [Multi-domain]  Cd Length: 177  Bit Score: 199.38  E-value: 1.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  59 LLDITGVVVDKPSASSklgvigrqlfgassDRLQENSLFDIVQTIRQAKDDRNITGIVLDLKNFvGGDQPSMQYIGKALR 138
Cdd:cd07014    1 VVFANGVIVDGEESSS--------------DTQGNVSGDTTAAQIRDARLDPKVKAIVLRVNSP-GGSVTASEVIRAELA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 139 EFRDSGKPVYAV-GSSYSQGQYYLASFANKIWLSPQGEVDLHGFATNglyykslldklkvsthvfrvgtyksavepfird 217
Cdd:cd07014   66 AARAAGKPVVASgGGNAASGGYWISTPANYIVANPSTLVGSIGIFGV--------------------------------- 112
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490280611 218 dmspaaREADSRWIGELWQNYLNTIAANRQITAQQLfpgalgiIDGLRKVGGDTAKYALDNKLVDELATSTEVEKALT 295
Cdd:cd07014  113 ------QLADQLSIENGYKRFITLVADNRHSTPEQQ-------IDKIAQGGVWTGQDAKANGLVDSLGSFDDAVAKLA 177
SppA_dom TIGR00706
signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein ...
327-540 1.32e-59

signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein SppA (protease IV) of E. coli was shown experimentally to degrade signal peptides as are released by protein processing and secretion. This protein shows stronger homology to the C-terminal region of SppA than to the N-terminal domain or to the related putative protease SuhB. The member of this family from Bacillus subtilis was shown to have properties consistent with a role in degrading signal peptides after cleavage from precursor proteins, although it was not demonstrated conclusively. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273227 [Multi-domain]  Cd Length: 208  Bit Score: 197.98  E-value: 1.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  327 IAVIFANGAIMDGEEtpgnvggDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAaGKPVVVSMGGMA 406
Cdd:TIGR00706   2 IAVLEVSGAIADVSP-------EDFDKKLERIKDDKTIKALVLRINSPGGTVVASEEIYKKLEKLKA-KKPVVASMGGMA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  407 ASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVHTDGVATSPLADVSS-TKALPPEVQQLMQLSIENGYQ 485
Cdd:TIGR00706  74 ASGGYYISMAADEIFANPGTITGSIGVILQGANVEKLAEKLGISFEVIKSGAYKDIGSpTRELTPEEKNILQSLVNESYE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490280611  486 RFITLVANARKSTPEKIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAK 540
Cdd:TIGR00706 154 QFVQVVSKGRNLPVEEVKKFADGRVFTGRQALKLRLVDKLGTLDDAIKWLKKLSG 208
SppA COG0616
Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, ...
46-287 2.71e-48

Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440381 [Multi-domain]  Cd Length: 215  Bit Score: 168.05  E-value: 2.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  46 SSTTSEHAARGALLLDITGVVVDKPSASSklgvigrqlfgassdrlQENSLFDIVQTIRQAKDDRNITGIVLDLkNFVGG 125
Cdd:COG0616    1 AKARPPKVKPSIAVIDLEGTIVDGGGPPS-----------------GEIGLEDILAALRKAAEDPDVKAVVLRI-NSPGG 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 126 DQPSMQYIGKALREFRDSGKPVYA-VGSSYSQGQYYLASFANKIWLSPQGEVDLHGFATNGLYYKSLLDKLKVSTHVFRV 204
Cdd:COG0616   63 SVAASEEIRDALRRLRAKGKPVVAsMGDVAASGGYYIASAADKIYANPTTITGSIGVIAQGPNFKGLLEKLGVEVEVVTA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 205 GTYKSAVEPFIRddMSPAAREADSRWIGELWQNYLNTIAANRQITAQQLfpgaLGIIDGLrkvgGDTAKYALDNKLVDEL 284
Cdd:COG0616  143 GEYKDALSPFRP--LSEEEREQLQALLDDIYDQFVEDVAEGRGLSLEEV----REIADGR----VWTGEQALELGLVDEL 212

                 ...
gi 490280611 285 ATS 287
Cdd:COG0616  213 GTL 215
Peptidase_S49 pfam01343
Peptidase family S49;
139-297 1.81e-46

Peptidase family S49;


Pssm-ID: 396077  Cd Length: 154  Bit Score: 160.92  E-value: 1.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  139 EFRDSGKPVYAVGSSYSQ-GQYYLASFANKIWLSPQGEVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVepFIRD 217
Cdd:pfam01343   1 ALLDAGKPVVASAGNYAAsGGYYLASAADKIVANPSTIVGSIGVITQGLNVENLLDKLGVSVDTIRAGEYKDAG--SPRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  218 DMSPAAREADSRWIGELWQNYLNTIAANRQITAQQLFPGALGiidglrkvGGDTAKYALDNKLVDELATSTEVEKALTKQ 297
Cdd:pfam01343  79 ELTPEEREILQRMLDETYQLFVQTVAKNRNLPVDQVDKIAQG--------RVWTGQQALKLGLVDELGTSDDAVTRAAEL 150
Clp_protease_like cd00394
Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ...
329-525 1.19e-43

Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ClpP; endopeptidase Clp; Peptidase S14; ATP-dependent protease, ClpAP)-like enzymes are highly conserved serine proteases and belong to the ClpP/Crotonase superfamily. Included in this family are Clp proteases that are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. The functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP. Active site consists of the triad Ser, His and Asp, preferring hydrophobic or non-polar residues at P1 or P1' positions. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function. Another family included in this class of enzymes is the signal peptide peptidase A (SppA; S49) which is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Mutagenesis studies suggest that the catalytic center of SppA comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain. Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain. The third family included in this hierarchy is nodulation formation efficiency D (NfeD) which is a membrane-bound Clp-class protease and only found in bacteria and archaea. Majority of the NfeD genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named stomatin operon partner protein (STOPP). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 from Pyrococcus horikoshii has been shown to possess serine protease activity having a Ser-Lys catalytic dyad.


Pssm-ID: 132923 [Multi-domain]  Cd Length: 161  Bit Score: 153.32  E-value: 1.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 329 VIFANGAIMDgeetpgnVGGDTTAAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKaagKPVVVSMGGMAAS 408
Cdd:cd00394    1 VIFINGVIED-------VSADQLAAQIRFAEADNSVKAIVLEVNTPGGRVDAGMNIVDALQASR---KPVIAYVGGQAAS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 409 GGYWISTPADYIVANPSTLTGSIGIFGVINTVENtlgsigvhtdgvatspladvsstkalpPEVQQLMQLSIENGYQRFI 488
Cdd:cd00394   71 AGYYIATAANKIVMAPGTRVGSHGPIGGYGGNGN---------------------------PTAQEADQRIILYFIARFI 123
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490280611 489 TLVANARKSTPEKIDQ-IAQGHVWTGEDAKANGLVDSL 525
Cdd:cd00394  124 SLVAENRGQTTEKLEEdIEKDLVLTAQEALEYGLVDAL 161
Clp_protease_like cd00394
Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ...
94-284 3.09e-40

Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ClpP; endopeptidase Clp; Peptidase S14; ATP-dependent protease, ClpAP)-like enzymes are highly conserved serine proteases and belong to the ClpP/Crotonase superfamily. Included in this family are Clp proteases that are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. The functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP. Active site consists of the triad Ser, His and Asp, preferring hydrophobic or non-polar residues at P1 or P1' positions. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function. Another family included in this class of enzymes is the signal peptide peptidase A (SppA; S49) which is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Mutagenesis studies suggest that the catalytic center of SppA comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain. Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain. The third family included in this hierarchy is nodulation formation efficiency D (NfeD) which is a membrane-bound Clp-class protease and only found in bacteria and archaea. Majority of the NfeD genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named stomatin operon partner protein (STOPP). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 from Pyrococcus horikoshii has been shown to possess serine protease activity having a Ser-Lys catalytic dyad.


Pssm-ID: 132923 [Multi-domain]  Cd Length: 161  Bit Score: 144.07  E-value: 3.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  94 NSLFDIVQTIRQAKDDRNITGIVLDLKNFvGGDQPSMQYIGKALREFRdsgKPVYA-VGSSYSQGQYYLASFANKIWLSP 172
Cdd:cd00394   11 VSADQLAAQIRFAEADNSVKAIVLEVNTP-GGRVDAGMNIVDALQASR---KPVIAyVGGQAASAGYYIATAANKIVMAP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 173 QGEVDLHGFATNGLYYKslldklkvsthvfrvgtyksavepfirddmSPAAREADSRWIGELWQNYLNTIAANRQITAQQ 252
Cdd:cd00394   87 GTRVGSHGPIGGYGGNG------------------------------NPTAQEADQRIILYFIARFISLVAENRGQTTEK 136
                        170       180       190
                 ....*....|....*....|....*....|..
gi 490280611 253 LfpgalgiIDGLRKVGGDTAKYALDNKLVDEL 284
Cdd:cd00394  137 L-------EEDIEKDLVLTAQEALEYGLVDAL 161
S49_Sppa_36K_type cd07022
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ...
326-533 7.85e-31

Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 36K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily are all bacterial and include sohB peptidase and protein C. These are sometimes referred to as 36K type since they contain only one domain, unlike E. coli SppA that also contains an amino-terminal domain. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases.


Pssm-ID: 132933 [Multi-domain]  Cd Length: 214  Bit Score: 119.97  E-value: 7.85e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 326 AIAVIFANGAIMDGEETPGNVGGDTT----AAQIRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAkAAGKPVVVS 401
Cdd:cd07022    1 GVAVIPVHGVLVPRGSWLEASSGLTSyegiAAAIRAALADPDVRAIVLDIDSPGGEVAGVFELADAIRAA-RAGKPIVAF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 402 MGGMAASGGYWISTPADYIVANPSTLTGSIGIFGVINTVENTLGSIGVH-TDGVATSPLADVSSTKALPPEVQQLMQLSI 480
Cdd:cd07022   80 VNGLAASAAYWIASAADRIVVTPTAGVGSIGVVASHVDQSKALEKAGLKvTLIFAGAHKVDGNPDEPLSDEARARLQAEV 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490280611 481 ENGYQRFITLVANARKSTPEKIDQiAQGHVWTGEDAKANGLVDSLGDFDDAVA 533
Cdd:cd07022  160 DALYAMFVAAVARNRGLSAAAVRA-TEGGVFRGQEAVAAGLADAVGTLDDALA 211
S49_SppA_67K_type cd07018
Signal peptide peptidase A (SppA) 67K type, a serine protease, has catalytic Ser-Lys dyad; ...
355-537 1.11e-23

Signal peptide peptidase A (SppA) 67K type, a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 67K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily contain an amino-terminal domain in addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members (sometimes referred to as 67K type), similar to E. coli and Arabidopsis thaliana SppA peptidases. Unlike the eukaryotic functional homologs that are proposed to be aspartic proteases, site-directed mutagenesis and sequence analysis have shown that members in this subfamily, mostly bacterial, are serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain.


Pssm-ID: 132929 [Multi-domain]  Cd Length: 222  Bit Score: 99.54  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 355 IRDARLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPvVVSMGGMAASGGYWISTPADYIVANPStltGSIGIF 434
Cdd:cd07018   38 LEKAAEDDRIKGIVLDLDGLSGGLAKLEELRQALERFRASGKP-VIAYADGYSQGQYYLASAADEIYLNPS---GSVELT 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 435 GVinTVENT-----LGSIGVHTDGV-------ATSPLadvsSTKALPPEVQQLMQLSIENGYQRFITLVANARKSTPEKI 502
Cdd:cd07018  114 GL--SAETLffkglLDKLGVEVQVFrvgeyksAVEPF----TRDDMSPEAREQTQALLDSLWDQYLADVAASRGLSPDAL 187
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490280611 503 DQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAE 537
Cdd:cd07018  188 EALIDLGGDSAEEALEAGLVDGLAYRDELEARLKE 222
SppA_dom TIGR00706
signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein ...
98-296 2.46e-17

signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein SppA (protease IV) of E. coli was shown experimentally to degrade signal peptides as are released by protein processing and secretion. This protein shows stronger homology to the C-terminal region of SppA than to the N-terminal domain or to the related putative protease SuhB. The member of this family from Bacillus subtilis was shown to have properties consistent with a role in degrading signal peptides after cleavage from precursor proteins, although it was not demonstrated conclusively. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273227 [Multi-domain]  Cd Length: 208  Bit Score: 80.88  E-value: 2.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611   98 DIVQTIRQAKDDRNITGIVLDLkNFVGGDQPSMQYIGKALREFrDSGKPVYA-VGSSYSQGQYYLASFANKIWLSPQGEV 176
Cdd:TIGR00706  18 DFDKKLERIKDDKTIKALVLRI-NSPGGTVVASEEIYKKLEKL-KAKKPVVAsMGGMAASGGYYISMAADEIFANPGTIT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  177 DLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFirDDMSPAAREADSRWIGELWQNYLNTIAANRQITAQQLFPG 256
Cdd:TIGR00706  96 GSIGVILQGANVEKLAEKLGISFEVIKSGAYKDIGSPT--RELTPEEKNILQSLVNESYEQFVQVVSKGRNLPVEEVKKF 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 490280611  257 ALGIIdglrkvggDTAKYALDNKLVDELATSTEVEKALTK 296
Cdd:TIGR00706 174 ADGRV--------FTGRQALKLRLVDKLGTLDDAIKWLKK 205
S49_Sppa_N_C cd07023
Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal ...
75-293 1.58e-16

Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. This subfamily contains members with either a single domain (sometimes referred to as 36K type), such as sohB peptidase, protein C and archaeal signal peptide peptidase, or an amino-terminal domain in addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members (sometimes referred to as 67K type), similar to E. coli and Arabidopsis thaliana SppA peptidases. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain.


Pssm-ID: 132934 [Multi-domain]  Cd Length: 208  Bit Score: 78.68  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  75 KLGVIgrQLFGASSDRLQENSLfDIVQTIRQAKDDRNITGIVLDLkNFVGGD-QPSmQYIGKALREFRDSGKPVYAVGSS 153
Cdd:cd07023    1 KIAVI--DIEGTISDGGGIGAD-SLIEQLRKAREDDSVKAVVLRI-NSPGGSvVAS-EEIYREIRRLRKAKKPVVASMGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 154 Y--SqGQYYLASFANKIWLSPQ---GEVdlhGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFirDDMSPAAREADS 228
Cdd:cd07023   76 VaaS-GGYYIAAAADKIVANPTtitGSI---GVIGQGPNLEELLDKLGIERDTIKSGPGKDKGSPD--RPLTEEERAILQ 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490280611 229 RWIGELWQNYLNTIAANRQITAQQLfpgaLGIIDGlrKVggDTAKYALDNKLVDELATSTE-VEKA 293
Cdd:cd07023  150 ALVDDIYDQFVDVVAEGRGMSGERL----DKLADG--RV--WTGRQALELGLVDELGGLDDaIAKA 207
PRK11778 PRK11778
putative inner membrane peptidase; Provisional
367-579 4.42e-15

putative inner membrane peptidase; Provisional


Pssm-ID: 236978 [Multi-domain]  Cd Length: 330  Bit Score: 76.79  E-value: 4.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 367 IVLRVNSPGGSVTASEiireeLAAA-----KAAGKPVVVSMGGMAASGGYWISTPADYIVANPSTLTGSIgifGVINTVE 441
Cdd:PRK11778 126 VLLRLESPGGVVHGYG-----LAASqlqrlRDAGIPLTVAVDKVAASGGYMMACVADKIIAAPFAIVGSI---GVVAQIP 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 442 N----------------------TLGSIGVHTDgvatspladvsstkalppEVQQLMQLSIENGYQRFITLVANARkstP 499
Cdd:PRK11778 198 NfhrllkkhdidvelhtageykrTLTLFGENTE------------------EGREKFREELEETHQLFKDFVQRYR---P 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 500 E-KIDQIAQGHVWTGEDAKANGLVDSLGDFDDAVAKAAELAKLktWHLNYYQEEPtffsmVLDSLTGSVRASLPAAIQAW 578
Cdd:PRK11778 257 QlDIDKVATGEHWYGQQALELGLVDEIQTSDDYLLELMKEHEV--LEVRYQQKKK-----LAERLGGSAAESADRLLLRW 329

                 .
gi 490280611 579 L 579
Cdd:PRK11778 330 W 330
S49_Sppa_36K_type cd07022
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ...
56-295 6.18e-10

Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 36K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily are all bacterial and include sohB peptidase and protein C. These are sometimes referred to as 36K type since they contain only one domain, unlike E. coli SppA that also contains an amino-terminal domain. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases.


Pssm-ID: 132933 [Multi-domain]  Cd Length: 214  Bit Score: 59.50  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  56 GALLLDITGVVVdkpsasSKLGVIGRQLFGASSDrlqenslfDIVQTIRQAKDDRNITGIVLDLKNFvGGDQPSMQYIGK 135
Cdd:cd07022    1 GVAVIPVHGVLV------PRGSWLEASSGLTSYE--------GIAAAIRAALADPDVRAIVLDIDSP-GGEVAGVFELAD 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 136 ALREFRdSGKPVYAV--GSSYSQGqYYLASFANKIWLSPQGEVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEP 213
Cdd:cd07022   66 AIRAAR-AGKPIVAFvnGLAASAA-YWIASAADRIVVTPTAGVGSIGVVASHVDQSKALEKAGLKVTLIFAGAHKVDGNP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 214 FirDDMSPAAREADSRWIGELWQNYLNTIAANRQITAQQlfpgalgiidgLRKVGGDT--AKYALDNKLVDELATSTEVE 291
Cdd:cd07022  144 D--EPLSDEARARLQAEVDALYAMFVAAVARNRGLSAAA-----------VRATEGGVfrGQEAVAAGLADAVGTLDDAL 210

                 ....
gi 490280611 292 KALT 295
Cdd:cd07022  211 AALA 214
NfeD COG1030
Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein ...
365-430 7.63e-07

Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440653 [Multi-domain]  Cd Length: 413  Bit Score: 51.78  E-value: 7.63e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490280611 365 KAIVLRVNSPGGSVTASEIIREELAAAKaagKPVV--VSMGGMAASGGYWISTPADYIVANPSTLTGS 430
Cdd:COG1030   58 DAVVLELDTPGGLVDSAREIVDAILASP---VPVIvyVASGARAASAGAYILLASHIAAMAPGTNIGA 122
S14_ClpP_1 cd07016
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
349-525 5.00e-05

Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. This subfamily only contains bacterial sequences. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function.


Pssm-ID: 132927 [Multi-domain]  Cd Length: 160  Bit Score: 44.06  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 349 DTTAAQIRDArLD--PKIKAIVLRVNSPGGSV-TASEIIreelAAAKAAGKPVVVSMGGMAASGGYWISTPADYIVA--- 422
Cdd:cd07016   14 GVTAKEFKDA-LDalGDDSDITVRINSPGGDVfAGLAIY----NALKRHKGKVTVKIDGLAASAASVIAMAGDEVEMppn 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 423 ------NPSTltgsigifgvintventlGSIGVHTDGVATSPLADvsstkalppevqqLMQLSIENGYqrfitlvanARK 496
Cdd:cd07016   89 amlmihNPST------------------GAAGNADDLRKAADLLD-------------KIDESIANAY---------AEK 128
                        170       180       190
                 ....*....|....*....|....*....|..
gi 490280611 497 S--TPEKIDQIAQGHVW-TGEDAKANGLVDSL 525
Cdd:cd07016  129 TglSEEEISALMDAETWlTAQEAVELGFADEI 160
Clp_protease_NfeD_like cd07021
Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation ...
365-438 7.62e-05

Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control.


Pssm-ID: 132932 [Multi-domain]  Cd Length: 178  Bit Score: 43.73  E-value: 7.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490280611 365 KAIVLRVNSPGGSVTASEIIREELAAAKAagkPVVVSMGGMAASGGYWISTPADYIVANPstlTGSIGIFGVIN 438
Cdd:cd07021   31 DAVVLDIDTPGGRVDSALEIVDLILNSPI---PTIAYVNDRAASAGALIALAADEIYMAP---GATIGAAEPIP 98
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
344-431 3.73e-04

Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173801 [Multi-domain]  Cd Length: 346  Bit Score: 43.02  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 344 GNVGGDTTAAQIRDArLDPKIKAIVLRVNSPGGSVTASEIIREELAAAKAAGKPVVVSMGGMAASGGYWISTPADYI--- 420
Cdd:cd07475  126 GSTYDDAYAKAIEDA-VKLGADVINMSLGSTAGFVDLDDPEQQAIKRAREAGVVVVVAAGNDGNSGSGTSKPLATNNpdt 204
                         90
                 ....*....|...
gi 490280611 421 --VANPSTLTGSI 431
Cdd:cd07475  205 gtVGSPATADDVL 217
S49_SppA_1 cd07019
Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal ...
98-176 4.30e-04

Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppAs in this subfamily are found in all three domains of life and are involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Site-directed mutagenesis and sequence analysis have shown these bacterial, archaeal and thylakoid SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain, similar to Arabidopsis thaliana SppA1 peptidase. Others, including sohB peptidase, protein C and archaeal signal peptide peptidase, do not contain the amino-terminal domain. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain.


Pssm-ID: 132930 [Multi-domain]  Cd Length: 211  Bit Score: 41.94  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611  98 DIVQTIRQAKDDRNITGIVLDLkNFVGGDQPSMQYIGKALREFRDSGKPVYAV-GSSYSQGQYYLASFANKIWLSPQGEV 176
Cdd:cd07019   25 TTAAQIRDARLDPKVKAIVLRV-NSPGGSVTASEVIRAELAAARAAGKPVVVSaGGAAASGGYWISTPANYIVANPSTLT 103
Clp_protease_NfeD cd07015
Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation ...
366-430 1.27e-03

Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control.


Pssm-ID: 132926  Cd Length: 172  Bit Score: 40.07  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490280611 366 AIVLRVNSPGGSVTASEIIREELAAAKAAGKPVVVSMGGMAASGGYWISTPADYIVANPSTLTGS 430
Cdd:cd07015   32 AIIIELDTPGGRADAAGNIVQRIQQSKIPVIIYVYPPGASAASAGTYIALGSHLIAMAPGTSIGA 96
Clp_protease_NfeD_1 cd07020
Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation ...
366-430 1.53e-03

Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control.


Pssm-ID: 132931 [Multi-domain]  Cd Length: 187  Bit Score: 39.85  E-value: 1.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490280611 366 AIVLRVNSPGGSVTASEIIREELAAAKAagkPVVV---SMGGMAASGGYWISTPADYIVANPSTLTGS 430
Cdd:cd07020   32 ALIIELDTPGGLLDSTREIVQAILASPV---PVVVyvyPSGARAASAGTYILLAAHIAAMAPGTNIGA 96
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
352-540 2.74e-03

Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase/carnithine racemase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440647 [Multi-domain]  Cd Length: 249  Bit Score: 39.77  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 352 AAQIRDARLDPKIKAIVLR-----------------VNSPGGSVTASEIIREELAAAKAAGKPVVVSMGGMAASGGYWIS 414
Cdd:COG1024   32 AAALDEAEADPDVRVVVLTgagkafcagadlkelaaAADPEEARAFARGLQRLFRALRRLPKPVIAAVNGAALGGGLELA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280611 415 TPADYIVANPSTltgsigifgVINTVENTLGSIgvhtdgvatsplADVSSTKALPPEVqqlmqlsienGYQRFITLVANA 494
Cdd:COG1024  112 LACDLRIAAEDA---------RFGLPEVRLGLI------------PGGGGTQRLPRLV----------GLARAKELLLTG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490280611 495 RKstpekidqiaqghvWTGEDAKANGLVDSLGDFDDAVAKAAELAK 540
Cdd:COG1024  161 RR--------------IDAEEALELGLVNRVVPDDELLAAALALAA 192
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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