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Conserved domains on  [gi|1757305402|ref|WP_151026974|]
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Clp protease ClpP [Enterococcus durans]

Protein Classification

Clp protease ClpP( domain architecture ID 10161508)

Clp protease ClpP is a serine protease, involved in several cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins

CATH:  3.90.226.10
EC:  3.4.21.92
Gene Ontology:  GO:0004176|GO:0006508|GO:0004252
MEROPS:  S14
PubMed:  17499722
SCOP:  4003574

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S14_ClpP_1 cd07016
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 18-179 5.73e-53

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: 167.71  E-value: 5.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  18 QIFIQGFIGSSWffeGNTDKGIKNILDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAM 97
Cdd:cd07016     2 EIYIYGDIGSDW---GVTAKEFKDALDALGDDSDITVRINSPGGDVFAGLAIYNALKRHKGKVTVKIDGLAASAASVIAM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  98 AGDTVKIYNNAQLMIHRASTYGEGNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVD 177
Cdd:cd07016    79 AGDEVEMPPNAMLMIHNPSTGAAGNADDLRKAADLLDKIDESIANAYAEKTGLSEEEISALMDAETWLTAQEAVELGFAD 158


                  ..
gi 1757305402 178 EI 179
Cdd:cd07016   159 EI 160
 
Name Accession Description Interval E-value
S14_ClpP_1 cd07016
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 18-179 5.73e-53

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: 167.71  E-value: 5.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  18 QIFIQGFIGSSWffeGNTDKGIKNILDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAM 97
Cdd:cd07016     2 EIYIYGDIGSDW---GVTAKEFKDALDALGDDSDITVRINSPGGDVFAGLAIYNALKRHKGKVTVKIDGLAASAASVIAM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  98 AGDTVKIYNNAQLMIHRASTYGEGNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVD 177
Cdd:cd07016    79 AGDEVEMPPNAMLMIHNPSTGAAGNADDLRKAADLLDKIDESIANAYAEKTGLSEEEISALMDAETWLTAQEAVELGFAD 158


                  ..
gi 1757305402 178 EI 179
Cdd:cd07016   159 EI 160
CLP_protease pfam00574
Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ...
 43-181 3.15e-19

Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large insertions, Swiss:P42380 contains one large insertion.


Pssm-ID: 425759 [Multi-domain]  Cd Length: 181  Bit Score: 81.46  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  43 LDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVKIYN--NAQLMIHRASTYGE 120
Cdd:pfam00574  40 LEAEDPDKDIYLYINSPGGSVTAGLAIYDTMQYIKPDVSTICLGLAASMGSFLLAAGAKGKRFAlpNARIMIHQPLGGAQ 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305402 121 GNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEIID 181
Cdd:pfam00574 120 GQASDIEIQAKEILKIKERLNEIYAKHTGQSLEKIEKDTDRDFFMSAEEAKEYGLIDEVIE 180
PRK14513 PRK14513
ATP-dependent Clp protease proteolytic subunit; Provisional
 42-181 6.65e-15

ATP-dependent Clp protease proteolytic subunit; Provisional


Pssm-ID: 237742 [Multi-domain]  Cd Length: 201  Bit Score: 70.35  E-value: 6.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  42 ILDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVK--IYNNAQLMIHRASTYG 119
Cdd:PRK14513   50 LLDSQNPEQEIQMYINCPGGEVYAGLAIYDTMRYIKAPVSTICVGIAMSMGSVLLMAGDKGKrmALPNSRIMIHQGSAGF 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757305402 120 EGNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEIID 181
Cdd:PRK14513  130 RGNTPDLEVQAKEVLFLRDTLVDIYHRHTDLPHEKLLRDMERDYFMSPEEAKAYGLIDSVIE 191
ClpP COG0740
ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein ...
 43-181 2.72e-12

ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440503  Cd Length: 194  Bit Score: 63.18  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  43 LDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVK--IYNNAQLMIHRASTYGE 120
Cdd:COG0740    50 LEAEDPDKDILLYINSPGGSVTAGLAIYDTMQFIKPDVSTICLGQAASMGAFLLAAGTKGKrfALPNARIMIHQPSGGAQ 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305402 121 GNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEIID 181
Cdd:COG0740   130 GQASDIEIQAREILKMRERLNEILAEHTGQPLEKIEKDTDRDTWMTAEEAVEYGLIDEVIE 190
 
Name Accession Description Interval E-value
S14_ClpP_1 cd07016
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 18-179 5.73e-53

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: 167.71  E-value: 5.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  18 QIFIQGFIGSSWffeGNTDKGIKNILDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAM 97
Cdd:cd07016     2 EIYIYGDIGSDW---GVTAKEFKDALDALGDDSDITVRINSPGGDVFAGLAIYNALKRHKGKVTVKIDGLAASAASVIAM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  98 AGDTVKIYNNAQLMIHRASTYGEGNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVD 177
Cdd:cd07016    79 AGDEVEMPPNAMLMIHNPSTGAAGNADDLRKAADLLDKIDESIANAYAEKTGLSEEEISALMDAETWLTAQEAVELGFAD 158


                  ..
gi 1757305402 178 EI 179
Cdd:cd07016   159 EI 160
CLP_protease pfam00574
Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ...
 43-181 3.15e-19

Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large insertions, Swiss:P42380 contains one large insertion.


Pssm-ID: 425759 [Multi-domain]  Cd Length: 181  Bit Score: 81.46  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  43 LDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVKIYN--NAQLMIHRASTYGE 120
Cdd:pfam00574  40 LEAEDPDKDIYLYINSPGGSVTAGLAIYDTMQYIKPDVSTICLGLAASMGSFLLAAGAKGKRFAlpNARIMIHQPLGGAQ 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305402 121 GNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEIID 181
Cdd:pfam00574 120 GQASDIEIQAKEILKIKERLNEIYAKHTGQSLEKIEKDTDRDFFMSAEEAKEYGLIDEVIE 180
PRK14513 PRK14513
ATP-dependent Clp protease proteolytic subunit; Provisional
 42-181 6.65e-15

ATP-dependent Clp protease proteolytic subunit; Provisional


Pssm-ID: 237742 [Multi-domain]  Cd Length: 201  Bit Score: 70.35  E-value: 6.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  42 ILDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVK--IYNNAQLMIHRASTYG 119
Cdd:PRK14513   50 LLDSQNPEQEIQMYINCPGGEVYAGLAIYDTMRYIKAPVSTICVGIAMSMGSVLLMAGDKGKrmALPNSRIMIHQGSAGF 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757305402 120 EGNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEIID 181
Cdd:PRK14513  130 RGNTPDLEVQAKEVLFLRDTLVDIYHRHTDLPHEKLLRDMERDYFMSPEEAKAYGLIDSVIE 191
S14_ClpP cd07013
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 43-179 3.23e-14

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. 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. Additionally, they are 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: 132924 [Multi-domain]  Cd Length: 162  Bit Score: 67.68  E-value: 3.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  43 LDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVK--IYNNAQLMIHRASTYGE 120
Cdd:cd07013    24 LGAVNPEKDIYLYINSPGGDVFAGMAIYDTIKFIKADVVTIIDGLAASMGSVIAMAGAKGKrfILPNAMMMIHQPWGGTL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1757305402 121 GNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEI 179
Cdd:cd07013   104 GDATDMRIYADLLLKVEGNLVSAYAHKTGQSEEELHADLERDTWLSAREAVEYGFADTI 162
ClpP COG0740
ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein ...
 43-181 2.72e-12

ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440503  Cd Length: 194  Bit Score: 63.18  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  43 LDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVK--IYNNAQLMIHRASTYGE 120
Cdd:COG0740    50 LEAEDPDKDILLYINSPGGSVTAGLAIYDTMQFIKPDVSTICLGQAASMGAFLLAAGTKGKrfALPNARIMIHQPSGGAQ 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305402 121 GNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEIID 181
Cdd:COG0740   130 GQASDIEIQAREILKMRERLNEILAEHTGQPLEKIEKDTDRDTWMTAEEAVEYGLIDEVIE 190
S14_ClpP_2 cd07017
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 43-179 8.54e-10

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. 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: 132928 [Multi-domain]  Cd Length: 171  Bit Score: 55.91  E-value: 8.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  43 LDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVK--IYNNAQLMIHRASTYGE 120
Cdd:cd07017    33 LESEDPKKPIYLYINSPGGSVTAGLAIYDTMQYIKPPVSTICLGLAASMGALLLAAGTKGKryALPNSRIMIHQPLGGAG 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402 121 GNVDDFRTIADQLESIdKSVKASYKTRFNG-TDEALQELLEKESFMDAETALSYGLVDEI 179
Cdd:cd07017   113 GQASDIEIQAKEILRL-RRRLNEILAKHTGqPLEKIEKDTDRDRYMSAEEAKEYGLIDKI 171
PRK12551 PRK12551
ATP-dependent Clp protease proteolytic subunit; Reviewed
 49-181 3.26e-08

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 139060  Cd Length: 196  Bit Score: 51.75  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  49 QEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVK--IYNNAQLMIHRASTYGEGNVDDF 126
Cdd:PRK12551   55 EKDIYLYINSPGGSVYDGLGIFDTMQHVKPDVHTVCVGLAASMGAFLLCAGAKGKrsSLQHSRIMIHQPLGGARGQASDI 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1757305402 127 RTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEIID 181
Cdd:PRK12551  135 RIQADEILFLKERLNTELSERTGQPLERIQEDTDRDFFMSPSEAVEYGLIDLVID 189
clpP CHL00028
ATP-dependent Clp protease proteolytic subunit
 48-185 9.89e-08

ATP-dependent Clp protease proteolytic subunit


Pssm-ID: 214340  Cd Length: 200  Bit Score: 50.63  E-value: 9.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  48 DQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVK--IYNNAQLMIHR-ASTYGEGNVD 124
Cdd:CHL00028   59 DTKDLYLFINSPGGSVISGLAIYDTMQFVKPDVHTICLGLAASMASFILAGGEITKrlAFPHARVMIHQpASSFYEGQAS 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305402 125 DFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEIIDAENS 185
Cdd:CHL00028  139 EFVLEAEELLKLRETITRVYAQRTGKPLWVISEDMERDVFMSATEAKAYGIVDLVAVNNEE 199
PRK12553 PRK12553
ATP-dependent Clp protease proteolytic subunit; Reviewed
 42-184 8.55e-07

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 237133  Cd Length: 207  Bit Score: 48.02  E-value: 8.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  42 ILDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVKIYN--NAQLMIHRASTYG 119
Cdd:PRK12553   58 VLESIDPDRDITLYINSPGGSVTAGDAIYDTIQFIRPDVQTVCTGQAASAGAVLLAAGTPGKRFAlpNARILIHQPSLGG 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757305402 120 --EGNVDDfrtIADQLESIDKS--------VKASYKTRfngtdEALQELLEKESFMDAETALSYGLVDEIIDAEN 184
Cdd:PRK12553  138 giRGQASD---LEIQAREILRMrerlerilAEHTGQSV-----EKIRKDTDRDKWLTAEEAKDYGLVDQIITSYR 204
PRK14514 PRK14514
ATP-dependent Clp endopeptidase proteolytic subunit ClpP;
43-180 3.31e-05

ATP-dependent Clp endopeptidase proteolytic subunit ClpP;


Pssm-ID: 184722  Cd Length: 221  Bit Score: 43.37  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  43 LDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVKIYN--NAQLMIHRASTYGE 120
Cdd:PRK14514   78 LDSVDPGKDISIYINSPGGSVYAGLGIYDTMQFISSDVATICTGMAASMASVLLVAGTKGKRSAlpHSRVMIHQPLGGAQ 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402 121 GNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEII 180
Cdd:PRK14514  158 GQASDIEITAREIQKLKKELYTIIADHSGTPFDKVWADSDRDYWMTAQEAKEYGMIDEVL 217
clpP PRK00277
ATP-dependent Clp protease proteolytic subunit; Reviewed
 107-180 3.31e-04

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 178955  Cd Length: 200  Bit Score: 40.15  E-value: 3.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1757305402 107 NAQLMIHRASTYGEGNVDDFRTIADQLESIDKSVKASYKTRFNGTDEALQELLEKESFMDAETALSYGLVDEII 180
Cdd:PRK00277  121 NSRIMIHQPLGGFQGQATDIEIHAREILKLKKRLNEILAEHTGQPLEKIEKDTDRDNFMSAEEAKEYGLIDEVL 194
PRK14512 PRK14512
ATP-dependent Clp protease proteolytic subunit; Provisional
 42-180 2.33e-03

ATP-dependent Clp protease proteolytic subunit; Provisional


Pssm-ID: 237741  Cd Length: 197  Bit Score: 37.85  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  42 ILDSLGDQEEIEVVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVKIYN--NAQLMIHRASTYG 119
Cdd:PRK14512   46 LLEALDSKKPIFVYIDSEGGDIDAGFAIFNMIRFVKPKVFTIGVGLVASAAALIFLAAKKESRFSlpNARYLLHQPLSGF 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1757305402 120 EGNVDDFRTIADQLESIdksvkasyKTRFNG--TDEALQEL--LEKES----FMDAETALSYGLVDEII 180
Cdd:PRK14512  126 KGVATDIEIYANELNKV--------KSELNDiiAKETGQELdkVEKDTdrdfWLDSSSAVKYGLVFEVV 186
COG3904 COG3904
Predicted periplasmic protein [Function unknown];
54-182 4.93e-03

Predicted periplasmic protein [Function unknown];


Pssm-ID: 443110 [Multi-domain]  Cd Length: 197  Bit Score: 36.93  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305402  54 VVINSNGGDVFQGIAIGNLLKSNKAKINVVINGLAASAASIIAMAGDTVKIYNNAQLMIHRASTYGegnvDDFRTIADQL 133
Cdd:COG3904    67 VVLNSPGGSVAEALALGRLIRARGLDTAVPAGAYCASACVLAFAGGVERYVEPGARVGVHQPYLGG----GDALPAAEAV 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1757305402 134 ESIDKSVK--ASYKTRFNGTDEALQELLEKES----FMDAETALSYGLVDEIIDA 182
Cdd:COG3904   143 SDTQRATArlARYLREMGVDPELLELALSTPPddmrYLTPEELLRYGLVTGPLPA 197
 
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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