UniProt UniProt http://www.uniprot.org kang-2004-3 in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined Kang SG., Maurizi MR., Thompson M., Mueser T., Ahvazi B. ahvazib@mail.nih.gov Journal of structural biology 2004 Only protein-protein interactions imex curation imex curation kang-2004-2 ecoli Escherichia coli (strain K12) x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Kang SG., Maurizi MR., Thompson M., Mueser T., Ahvazi B. ahvazib@mail.nih.gov Journal of structural biology 2004 Only protein-protein interactions imex curation imex curation kang-2004-4 in vitro In vitro filter binding filter binding Filter overlay assay Filter overlay assay weight by comassie molecular weight estimation by coomasie staining weight by comassie Kang SG., Maurizi MR., Thompson M., Mueser T., Ahvazi B. Interaction measured by retention upon ultrafiltration through Microcon 100 300 kDa cut-off membranes. ahvazib@mail.nih.gov Journal of structural biology 2004 Only protein-protein interactions imex curation imex curation clpx_human ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial CLPX protein protein human Homo sapiens Human MPSCGACTCGAAAVRLITSSLASAQRGISGGRIHMSVLGRLGTFETQILQRAPLRSFTETPAYFASKDGISKDGSGDGNKKSASEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEVEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQIPQEKRGGEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNILFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPTKESSEEEYDSGVEEEGWPRQADAANS faphmalvpv FAPHMALVPV peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) FAPHMALVPV q16740-pro_0000005516 ATP-dependent Clp protease proteolytic subunit, mitochondrial CLPP Endopeptidase Clp protein protein human Homo sapiens Human PLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLVQKEPVEAAPAAEPVPAST 57 277 clpx_ecoli ATP-dependent Clp protease ATP-binding subunit ClpX clpX lopC b0438 JW0428 ATP-dependent unfoldase ClpX protein protein ecoli Escherichia coli (strain K12) MTDKRKDGSGKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPHRERSALPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEEALIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSKPLLIYGKPEAQQASGE p0a6g7-pro_0000179551 ATP-dependent Clp protease proteolytic subunit clpP lopP b0437 JW0427 Caseinolytic protease Endopeptidase Clp Heat shock protein F21.5 Protease Ti protein protein ecoli Escherichia coli (strain K12) ALVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN 15 207 clpp-clpx-4 3730909 N/A 3730912 enzyme regulator enzyme regulator unspecified role unspecified role purified purified N/A 3730913 enzyme target enzyme target substrate substrate unspecified role unspecified role N/A 3730914 enzyme enzyme neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false Q16740-PRO_0000005516:p.Pro1Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q16740-PRO_0000005516:p.Pro1Cys mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) protein cleavage protein cleavage false false false Fig. 6A, Table 2 Removal of the 28 C-terminal amino-acid resiudes of CLPP increased reaction rate, which has been inferred to suggest increased the interaction with CLPP. clpp-faphmalvpv-1 3730909 N/A 3730913 enzyme target enzyme target substrate substrate unspecified role unspecified role N/A 3730914 enzyme enzyme neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) protein cleavage protein cleavage false false false Table 2 Removal of the 28 C-terminal amino-acid resiudes of CLPP increased reaction rate, which has been inferred to suggest increased the interaction with CLPP. clpp-clpx-5 3730909 N/A 3730915 enzyme regulator enzyme regulator unspecified role unspecified role purified purified N/A 3730913 enzyme target enzyme target substrate substrate unspecified role unspecified role N/A 3730914 enzyme enzyme neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) protein cleavage protein cleavage false false false Fig. 6B, Removal of the 28 C-terminal amino-acid resiudes of CLPP increased reaction rate, which has been inferred to suggest increased the interaction with CLPP. clpp-clpx-6 3730909 N/A 3730915 enzyme regulator enzyme regulator unspecified role unspecified role purified purified N/A 3730913 enzyme target enzyme target substrate substrate unspecified role unspecified role N/A 3730916 enzyme enzyme neutral component neutral component purified purified ecoli Escherichia coli (strain K12) protein cleavage protein cleavage false false false Fig. 6B, Removal of the 28 C-terminal amino-acid resiudes of CLPP increased reaction rate, which has been inferred to suggest increased the interaction with CLPP. clpp-11 3730910 N/A 3730914 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 7.0 direct interaction direct interaction false false false Table 1 clpp-clpx-7 3730911 N/A 3730912 unspecified role unspecified role neutral component neutral component purified purified N/A 3730914 unspecified role unspecified role neutral component neutral component purified purified Q16740-PRO_0000005516:p.Pro1Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain false Q16740-PRO_0000005516:p.Pro1Cys mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false Fig. 7 Removal of the 28 C-terminal amino-acid resiudes of CLPP increased reaction rate, which has been inferred to suggest increased the interaction with CLPP.