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Conserved domains on  [gi|2427919573|ref|WP_270720835|]
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MULTISPECIES: ATP-dependent Clp protease proteolytic subunit, partial [Bacillus cereus group]

Protein Classification

Clp protease/crotonase-like domain-containing protein( domain architecture ID 581041)

Clp protease/crotonase-like domain-containing protein similar to Oryza sativa enoyl-CoA delta isomerase which plays a role in fatty acid metabolism, which involves stabilization of an enolate anion intermediate derived from an acyl-CoA substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
crotonase-like super family cl23717
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
 1-87 1.46e-58

Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.


The actual alignment was detected with superfamily member PRK00277:

Pssm-ID: 474030  Cd Length: 200  Bit Score: 177.66  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:PRK00277  111 GAKGKRFALPNSRIMIHQPLGGFQGQATDIEIHAREILKLKKRLNEILAEHTGQPLEKIEKDTDRDNFMSAEEAKEYGLI 190


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:PRK00277  191 DEVLTKR 197
 
Name Accession Description Interval E-value
clpP PRK00277
ATP-dependent Clp protease proteolytic subunit; Reviewed
 1-87 1.46e-58

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 178955  Cd Length: 200  Bit Score: 177.66  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:PRK00277  111 GAKGKRFALPNSRIMIHQPLGGFQGQATDIEIHAREILKLKKRLNEILAEHTGQPLEKIEKDTDRDNFMSAEEAKEYGLI 190


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:PRK00277  191 DEVLTKR 197
ClpP COG0740
ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein ...
 1-87 2.46e-51

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


Pssm-ID: 440503  Cd Length: 194  Bit Score: 159.09  E-value: 2.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:COG0740   106 GTKGKRFALPNARIMIHQPSGGAQGQASDIEIQAREILKMRERLNEILAEHTGQPLEKIEKDTDRDTWMTAEEAVEYGLI 185


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:COG0740   186 DEVIESR 192
CLP_protease pfam00574
Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ...
 1-86 2.54e-49

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: 153.49  E-value: 2.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:pfam00574  96 GAKGKRFALPNARIMIHQPLGGAQGQASDIEIQAKEILKIKERLNEIYAKHTGQSLEKIEKDTDRDFFMSAEEAKEYGLI 175


                  ....*.
gi 2427919573  81 DKIFTN 86
Cdd:pfam00574 176 DEVIER 181
S14_ClpP_2 cd07017
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 1-83 1.18e-48

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: 151.44  E-value: 1.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:cd07017    89 GTKGKRYALPNSRIMIHQPLGGAGGQASDIEIQAKEILRLRRRLNEILAKHTGQPLEKIEKDTDRDRYMSAEEAKEYGLI 168


                  ...
gi 2427919573  81 DKI 83
Cdd:cd07017   169 DKI 171
 
Name Accession Description Interval E-value
clpP PRK00277
ATP-dependent Clp protease proteolytic subunit; Reviewed
 1-87 1.46e-58

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 178955  Cd Length: 200  Bit Score: 177.66  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:PRK00277  111 GAKGKRFALPNSRIMIHQPLGGFQGQATDIEIHAREILKLKKRLNEILAEHTGQPLEKIEKDTDRDNFMSAEEAKEYGLI 190


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:PRK00277  191 DEVLTKR 197
ClpP COG0740
ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein ...
 1-87 2.46e-51

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


Pssm-ID: 440503  Cd Length: 194  Bit Score: 159.09  E-value: 2.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:COG0740   106 GTKGKRFALPNARIMIHQPSGGAQGQASDIEIQAREILKMRERLNEILAEHTGQPLEKIEKDTDRDTWMTAEEAVEYGLI 185


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:COG0740   186 DEVIESR 192
CLP_protease pfam00574
Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ...
 1-86 2.54e-49

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: 153.49  E-value: 2.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:pfam00574  96 GAKGKRFALPNARIMIHQPLGGAQGQASDIEIQAKEILKIKERLNEIYAKHTGQSLEKIEKDTDRDFFMSAEEAKEYGLI 175


                  ....*.
gi 2427919573  81 DKIFTN 86
Cdd:pfam00574 176 DEVIER 181
S14_ClpP_2 cd07017
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 1-83 1.18e-48

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: 151.44  E-value: 1.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:cd07017    89 GTKGKRYALPNSRIMIHQPLGGAGGQASDIEIQAKEILRLRRRLNEILAKHTGQPLEKIEKDTDRDRYMSAEEAKEYGLI 168


                  ...
gi 2427919573  81 DKI 83
Cdd:cd07017   169 DKI 171
PRK12553 PRK12553
ATP-dependent Clp protease proteolytic subunit; Reviewed
 1-87 4.70e-42

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 237133  Cd Length: 207  Bit Score: 135.85  E-value: 4.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPL--GGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYG 78
Cdd:PRK12553  115 GTPGKRFALPNARILIHQPSlgGGIRGQASDLEIQAREILRMRERLERILAEHTGQSVEKIRKDTDRDKWLTAEEAKDYG 194


                  ....*....
gi 2427919573  79 LIDKIFTNR 87
Cdd:PRK12553  195 LVDQIITSY 203
PRK12551 PRK12551
ATP-dependent Clp protease proteolytic subunit; Reviewed
 1-87 1.69e-38

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 139060  Cd Length: 196  Bit Score: 126.48  E-value: 1.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:PRK12551  105 GAKGKRSSLQHSRIMIHQPLGGARGQASDIRIQADEILFLKERLNTELSERTGQPLERIQEDTDRDFFMSPSEAVEYGLI 184


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:PRK12551  185 DLVIDKR 191
clpP CHL00028
ATP-dependent Clp protease proteolytic subunit
 1-86 5.73e-37

ATP-dependent Clp protease proteolytic subunit


Pssm-ID: 214340  Cd Length: 200  Bit Score: 122.66  E-value: 5.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGA-QGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGL 79
Cdd:CHL00028  110 GEITKRLAFPHARVMIHQPASSFyEGQASEFVLEAEELLKLRETITRVYAQRTGKPLWVISEDMERDVFMSATEAKAYGI 189


                  ....*..
gi 2427919573  80 IDKIFTN 86
Cdd:CHL00028  190 VDLVAVN 196
PRK14514 PRK14514
ATP-dependent Clp endopeptidase proteolytic subunit ClpP;
1-87 3.67e-35

ATP-dependent Clp endopeptidase proteolytic subunit ClpP;


Pssm-ID: 184722  Cd Length: 221  Bit Score: 118.87  E-value: 3.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:PRK14514  134 GTKGKRSALPHSRVMIHQPLGGAQGQASDIEITAREIQKLKKELYTIIADHSGTPFDKVWADSDRDYWMTAQEAKEYGMI 213


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:PRK14514  214 DEVLIKK 220
PRK12552 PRK12552
ATP-dependent Clp protease proteolytic subunit;
1-87 3.94e-32

ATP-dependent Clp protease proteolytic subunit;


Pssm-ID: 183588  Cd Length: 222  Bit Score: 110.98  E-value: 3.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:PRK12552  129 GTKGQRASLPHATIVLHQPRSGARGQATDIQIRAKEVLHNKRTMLEILSRNTGQTVEKLSKDTDRMFYLTPQEAKEYGLI 208


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:PRK12552  209 DRVLESR 215
S14_ClpP cd07013
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 1-83 1.83e-29

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: 102.73  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:cd07013    80 GAKGKRFILPNAMMMIHQPWGGTLGDATDMRIYADLLLKVEGNLVSAYAHKTGQSEEELHADLERDTWLSAREAVEYGFA 159


                  ...
gi 2427919573  81 DKI 83
Cdd:cd07013   160 DTI 162
PRK14512 PRK14512
ATP-dependent Clp protease proteolytic subunit; Provisional
 3-87 3.48e-26

ATP-dependent Clp protease proteolytic subunit; Provisional


Pssm-ID: 237741  Cd Length: 197  Bit Score: 95.25  E-value: 3.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   3 KGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLIDK 82
Cdd:PRK14512  105 KESRFSLPNARYLLHQPLSGFKGVATDIEIYANELNKVKSELNDIIAKETGQELDKVEKDTDRDFWLDSSSAVKYGLVFE 184


                  ....*
gi 2427919573  83 IFTNR 87
Cdd:PRK14512  185 VVETR 189
PRK14513 PRK14513
ATP-dependent Clp protease proteolytic subunit; Provisional
 1-87 1.73e-25

ATP-dependent Clp protease proteolytic subunit; Provisional


Pssm-ID: 237742 [Multi-domain]  Cd Length: 201  Bit Score: 93.46  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   1 GEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLI 80
Cdd:PRK14513  107 GDKGKRMALPNSRIMIHQGSAGFRGNTPDLEVQAKEVLFLRDTLVDIYHRHTDLPHEKLLRDMERDYFMSPEEAKAYGLI 186


                  ....*..
gi 2427919573  81 DKIFTNR 87
Cdd:PRK14513  187 DSVIEPT 193
Clp_protease_like cd00394
Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ...
 5-83 3.59e-18

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: 73.58  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427919573   5 KRYALPNSEVMIHQPLGGAQGQA--TEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLIDK 82
Cdd:cd00394    81 KIVMAPGTRVGSHGPIGGYGGNGnpTAQEADQRIILYFIARFISLVAENRGQTTEKLEEDIEKDLVLTAQEALEYGLVDA 160


                  .
gi 2427919573  83 I 83
Cdd:cd00394   161 L 161
S14_ClpP_1 cd07016
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 10-83 3.38e-15

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: 66.02  E-value: 3.38e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2427919573  10 PNSEVMIHQPLGGAQGQATEIEIAAKRILFLREKLNQILADRTGQPLEVLQRDTDRDNFMTAEKALEYGLIDKI 83
Cdd:cd07016    87 PNAMLMIHNPSTGAAGNADDLRKAADLLDKIDESIANAYAEKTGLSEEEISALMDAETWLTAQEAVELGFADEI 160
 
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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