NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1735337801|ref|WP_149016226|]
View 

S49 family peptidase, partial [Escherichia coli]

Protein Classification

S49 family peptidase( domain architecture ID 10161638)

S49 family peptidase similar to Escherichia virus Lambda capsid assembly protease C, which catalyzes the cleavage of the capsid scaffolding protein after complete procapsid formation

EC:  3.4.21.-
Gene Ontology:  GO:0008233|GO:0006508
MEROPS:  S49
PubMed:  7845208|8439290

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
S49_Sppa_36K_type cd07022
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ...
 1-136 9.65e-52

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: 169.67  E-value: 9.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   1 LCNDTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQR 80
Cdd:cd07022    79 FVNGLAASAAYWIASAADRIVVTPTAGVGSIGVVASHVDQSKALEKAGLKVTLIFAGAHKVDGNPDEPLSDEARARLQAE 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1735337801  81 IDAARRMFAEKVAMYTGLSVDAVTGTEAAVFEGQSGIEAGLADELINASDAISVMA 136
Cdd:cd07022   159 VDALYAMFVAAVARNRGLSAAAVRATEGGVFRGQEAVAAGLADAVGTLDDALAALA 214
 
Name Accession Description Interval E-value
S49_Sppa_36K_type cd07022
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ...
 1-136 9.65e-52

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: 169.67  E-value: 9.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   1 LCNDTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQR 80
Cdd:cd07022    79 FVNGLAASAAYWIASAADRIVVTPTAGVGSIGVVASHVDQSKALEKAGLKVTLIFAGAHKVDGNPDEPLSDEARARLQAE 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1735337801  81 IDAARRMFAEKVAMYTGLSVDAVTGTEAAVFEGQSGIEAGLADELINASDAISVMA 136
Cdd:cd07022   159 VDALYAMFVAAVARNRGLSAAAVRATEGGVFRGQEAVAAGLADAVGTLDDALAALA 214
Peptidase_S49 pfam01343
Peptidase family S49;
3-140 4.25e-32

Peptidase family S49;


Pssm-ID: 396077  Cd Length: 154  Bit Score: 117.00  E-value: 4.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   3 NDTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQRID 82
Cdd:pfam01343  14 GNYAASGGYYLASAADKIVANPSTIVGSIGVITQGLNVENLLDKLGVSVDTIRAGEYKDAGSPRRELTPEEREILQRMLD 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1735337801  83 AARRMFAEKVAMYTGLSVDAV-TGTEAAVFEGQSGIEAGLADELINASDAISVMATALN 140
Cdd:pfam01343  94 ETYQLFVQTVAKNRNLPVDQVdKIAQGRVWTGQQALKLGLVDELGTSDDAVTRAAELAG 152
SppA COG0616
Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, ...
 2-127 2.16e-26

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


Pssm-ID: 440381 [Multi-domain]  Cd Length: 215  Bit Score: 103.72  E-value: 2.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   2 CNDTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQRI 81
Cdd:COG0616    88 MGDVAASGGYYIASAADKIYANPTTITGSIGVIAQGPNFKGLLEKLGVEVEVVTAGEYKDALSPFRPLSEEEREQLQALL 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1735337801  82 DAARRMFAEKVAMYTGLSVDAVTG-TEAAVFEGQSGIEAGLADELIN 127
Cdd:COG0616   168 DDIYDQFVEDVAEGRGLSLEEVREiADGRVWTGEQALELGLVDELGT 214
SppA_dom TIGR00706
signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein ...
 4-137 1.20e-16

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: 77.03  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   4 DTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQRIDA 83
Cdd:TIGR00706  71 GMAASGGYYISMAADEIFANPGTITGSIGVILQGANVEKLAEKLGISFEVIKSGAYKDIGSPTRELTPEEKNILQSLVNE 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1735337801  84 ARRMFAEKVAMYTGLSVDAVTG-TEAAVFEGQSGIEAGLADELINASDAISVMAT 137
Cdd:TIGR00706 151 SYEQFVQVVSKGRNLPVEEVKKfADGRVFTGRQALKLRLVDKLGTLDDAIKWLKK 205
 
Name Accession Description Interval E-value
S49_Sppa_36K_type cd07022
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ...
 1-136 9.65e-52

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: 169.67  E-value: 9.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   1 LCNDTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQR 80
Cdd:cd07022    79 FVNGLAASAAYWIASAADRIVVTPTAGVGSIGVVASHVDQSKALEKAGLKVTLIFAGAHKVDGNPDEPLSDEARARLQAE 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1735337801  81 IDAARRMFAEKVAMYTGLSVDAVTGTEAAVFEGQSGIEAGLADELINASDAISVMA 136
Cdd:cd07022   159 VDALYAMFVAAVARNRGLSAAAVRATEGGVFRGQEAVAAGLADAVGTLDDALAALA 214
Peptidase_S49 pfam01343
Peptidase family S49;
3-140 4.25e-32

Peptidase family S49;


Pssm-ID: 396077  Cd Length: 154  Bit Score: 117.00  E-value: 4.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   3 NDTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQRID 82
Cdd:pfam01343  14 GNYAASGGYYLASAADKIVANPSTIVGSIGVITQGLNVENLLDKLGVSVDTIRAGEYKDAGSPRRELTPEEREILQRMLD 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1735337801  83 AARRMFAEKVAMYTGLSVDAV-TGTEAAVFEGQSGIEAGLADELINASDAISVMATALN 140
Cdd:pfam01343  94 ETYQLFVQTVAKNRNLPVDQVdKIAQGRVWTGQQALKLGLVDELGTSDDAVTRAAELAG 152
SppA COG0616
Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, ...
 2-127 2.16e-26

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


Pssm-ID: 440381 [Multi-domain]  Cd Length: 215  Bit Score: 103.72  E-value: 2.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   2 CNDTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQRI 81
Cdd:COG0616    88 MGDVAASGGYYIASAADKIYANPTTITGSIGVIAQGPNFKGLLEKLGVEVEVVTAGEYKDALSPFRPLSEEEREQLQALL 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1735337801  82 DAARRMFAEKVAMYTGLSVDAVTG-TEAAVFEGQSGIEAGLADELIN 127
Cdd:COG0616   168 DDIYDQFVEDVAEGRGLSLEEVREiADGRVWTGEQALELGLVDELGT 214
SppA_dom TIGR00706
signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein ...
 4-137 1.20e-16

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: 77.03  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   4 DTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQRIDA 83
Cdd:TIGR00706  71 GMAASGGYYISMAADEIFANPGTITGSIGVILQGANVEKLAEKLGISFEVIKSGAYKDIGSPTRELTPEEKNILQSLVNE 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1735337801  84 ARRMFAEKVAMYTGLSVDAVTG-TEAAVFEGQSGIEAGLADELINASDAISVMAT 137
Cdd:TIGR00706 151 SYEQFVQVVSKGRNLPVEEVKKfADGRVFTGRQALKLRLVDKLGTLDDAIKWLKK 205
S49_Sppa_N_C cd07023
Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal ...
 4-136 1.31e-14

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: 71.36  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   4 DTACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKVDGNQFEALPAEVRQDMQQRIDA 83
Cdd:cd07023    75 DVAASGGYYIAAAADKIVANPTTITGSIGVIGQGPNLEELLDKLGIERDTIKSGPGKDKGSPDRPLTEEERAILQALVDD 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1735337801  84 ARRMFAEKVAMYTGLSVDAVTGTEAA-VFEGQSGIEAGLADELINASDAISVMA 136
Cdd:cd07023   155 IYDQFVDVVAEGRGMSGERLDKLADGrVWTGRQALELGLVDELGGLDDAIAKAA 208
S49_SppA_1 cd07019
Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal ...
 6-136 1.39e-10

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: 60.04  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   6 ACSAAMLLASACSRRLVTQTSRIGSIGVMMSHVSYAGHLAQAGVDITLIY-SGAHKVDGNQfeALPAEVRQDMQQRIDAA 84
Cdd:cd07019    81 AASGGYWISTPANYIVANPSTLTGSIGIFGVITTVENSLDSIGVHTDGVStSPLADVSITR--ALPPEAQLGLQLSIENG 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1735337801  85 RRMFAEKVAMYTGLSVDAVTGTE-AAVFEGQSGIEAGLADELINASDAISVMA 136
Cdd:cd07019   159 YKRFITLVADARHSTPEQIDKIAqGHVWTGQDAKANGLVDSLGDFDDAVAKAA 211
SppA_67K TIGR00705
signal peptide peptidase SppA, 67K type; This model represents the signal peptide peptidase A ...
 6-136 7.75e-04

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: 40.97  E-value: 7.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735337801   6 ACSAAMLLASAcSRRLVTQTSRI-GSIGVMMSHVSYAGHLAQAGVDITLIYSGAHKvDGNQFEALPAEVRQDMQQRIDAA 84
Cdd:TIGR00705 389 AASGGYWIASA-ADYIVASPNTItGSIGVFSVLPTFENSLDRIGVHVDGVSTHELA-NVSLLRPLTAEDQAIMQLSVEAG 466

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1735337801  85 RRMFAEKVAMYTGLSVDAVTG-TEAAVFEGQSGIEAGLADELINASDAISVMA 136
Cdd:TIGR00705 467 YRRFLSVVSAGRNLTPTQVDKvAQGRVWTGEDAVSNGLVDALGGLDEAVAKAA 519
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH