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Functional Status	Green (experimental evidence, uncurated)
EC number	3.4.21.92 (See reaction via BRENDA) (Source: BRENDA) 3.4.21.92 (See reaction via BRENDA) (Source: NCBI RefSeq)
GO terms	MF: GO:0008236 : serine-type peptidase activity : IEA MF: GO:0005524 : ATP binding : IEA CC: GO:0005829 : cytosol : IDA BP: GO:0006515 : misfolded or incompletely synthesized protein catabolic process : IDA CC: GO:0005624 : membrane fraction : IDA BP: GO:0006508 : proteolysis : IEA MF: GO:0004252 : serine-type endopeptidase activity : IEA CC: GO:0016020 : membrane : IDA BP: GO:0009408 : response to heat : IEP MF: GO:0000166 : nucleotide binding : IEA CC: GO:0005737 : cytoplasm : IEA MF: GO:0008233 : peptidase activity : IEA MF: GO:0016787 : hydrolase activity : IEA BP: GO:0006950 : response to stress : IEA
Domain Structure from CDD	S14_ClpP_2: 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..... (More) See domain structure on NCBI Conserved Domain Database
Domain structure from Pfam	CLP_protease H See domain structure on Pfam Database
Based on the function of this gene, COMBREX predictions were made to the following related genes (mouse over gene symbol for details)	[Download ] CKO_02723 , clpP (63) , clpP2 , ESA_02861 , NT01EI_1078 , SARI_02486 , SPAB_03130 , Spro_1095

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The table at right lists genes that may be "functionally linked to" (i.e., participate in a common biological process, or form a protein complex with) the subject gene of this page, as determined by two sequence-independent methods, including phylogenetic profiling and operon membership (determined by OperonDB). (Info.) These linkages may also be viewed graphically using the program VisANT, by clicking on the headers of the table. Note: VisANT requires Java. To install the latest version of Java, see www.java.com

clpX ATPase and specificity subunit of ClpX-ClpP ATP-de     tig peptidyl-prolyl cis/trans isomerase (trigger facto     rluE 23S rRNA U2457 pseudouridine synthase     mrdA transpeptidase involved in peptidoglycan synthesis     hemN coproporphyrinogen III oxidase, SAM and NAD(P)H de     murG N-acetylglucosaminyl transferase     cusR DNA-binding response regulator in two-component re     miaA delta(2)-isopentenylpyrophosphate tRNA-adenosine t     mrdB cell wall shape-determining protein     rstA multicopy supressor of yjeE, yeaZ or ygjD deletion     phoB DNA-binding response regulator in two-component re     ompR DNA-binding response regulator in two-component re     murD UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase     cca fused tRNA nucleotidyl transferase/2'3'-cyclic pho     rimM 16S rRNA processing protein     qseB quorum sensing DNA-binding response regulator in t     prfB peptide chain release factor RF-2     baeR DNA-binding response regulator in two-component re     ftsW integral membrane protein involved in stabilizing     pnp polynucleotide phosphorylase/polyadenylase     polA fused DNA polymerase I 5'->3' polymerase/3'->5' ex     recG ATP-dependent DNA helicase     glmU fused N-acetyl glucosamine-1-phosphate uridyltrans     torR DNA-binding response regulator in two-component re     murE UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-dia     rluF 23S rRNA U2604 pseudouridine synthase     rsmD 16S rRNA m(2)G966 methyltransferase, SAM-dependent     yajC SecYEG protein translocase auxillary subunit     ddlA D-alanine-D-alanine ligase A     yedW predicted DNA-binding response regulator in two-co     yggW predicted oxidoreductase, HemN family     nlpD novel lipoprotein, function unknown     murB UDP-N-acetylenolpyruvoylglucosamine reductase, FAD     pcnB poly(A) polymerase I     priA Primosome factor n' (replication factor Y)     secG preprotein translocase membrane subunit     yaeJ conserved protein     murC UDP-N-acetylmuramate:L-alanine ligase     radA DNA repair protein     rluB 23S rRNA pseudouridylate synthase     ygeR novel lipoprotein, function unknown     basR DNA-binding response regulator in two-component re     phoP DNA-binding response regulator in two-component re     mfd transcription-repair coupling factor     yebA predicted peptidase     murA UDP-N-acetylglucosamine 1-carboxyvinyltransferase     creB DNA-binding response regulator in two-component re     ftsI transpeptidase involved in septal peptidoglycan sy     rsuA 16S rRNA U516 pseudouridine synthase     ddlB D-alanine:D-alanine ligase     arcA DNA-binding response regulator in two-component re     rpsA 30S ribosomal subunit protein S1     kdpE DNA-binding response regulator in two-component re     mpl UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-mes     cpxR DNA-binding response regulator in two-component re