1725:
26:
477:
family. The family is usually broken into two parts, one being the ClpA/B family with two ATPase domains, and the other being ClpX and friends with only one such domain. ClpA through E is put into the first group along with Hsp78/104, and ClpX and HSIU is put into the second group.
567:
Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S (July 1990). "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of
Escherichia coli".
711:
Gille C, Goede A, Schlöetelburg C, Preissner R, Kloetzel PM, Göbel UB, Frömmel C (March 2003). "A comprehensive view on proteasomal sequences: implications for the evolution of the proteasome".
302:
ClpXP is presented in almost all bacteria while ClpA is found in the Gram-negative bacteria, ClpC in Gram-Positive bacteria and cyanobacteria. ClpAP, ClpXP and ClpYQ coexist in
473:
family of eukaryotic heat shock proteins is homologous to the ATPase-active chaperon subunits found in the Clp complex; as such the entire group is often referred to as the
175:
403:
540:
Gottesman S, Clark WP, Maurizi MR (May 1990). "The ATP-dependent Clp protease of
Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate".
1379:
1239:
979:
520:
194:
497:) pore, thereby giving each client protein a second chance to fold. A member of the ClpA/B family termed ClpV is used in the bacterial
746:
Schirmer EC, Glover JR, Singer MA, Lindquist S (August 1996). "HSP100/Clp proteins: a common mechanism explains diverse functions".
287:
A fully assembled Clp protease complex has a barrel-shaped structure in which two stacked heptameric ring of proteolytic subunits (
187:
999:
668:
Hamon MP, Bulteau AL, Friguet B (September 2015). "Mitochondrial proteases and protein quality control in ageing and longevity".
288:
239:
154:
901:
Schlieker C, Zentgraf H, Dersch P, Mogk A (November 2005). "ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria".
423:
972:
862:"Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB"
1444:
957:
148:
965:
481:
Many of the proteins are not associated with a protease and have functions other than proteolysis. ClpB (human
130:
411:
135:
1600:
1199:
199:
123:
291:
or ClpQ) are either sandwiched between two rings or single-caped by one ring of hexameric ATPase-active
1715:
628:"Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome"
407:
58:
306:
while only ClpXP complex in present in humans as mitochondrial enzymes. ClpYQ is another name for the
1701:
1688:
1675:
1662:
1649:
1636:
1623:
1585:
1114:
1099:
151:
1595:
1549:
1492:
996:
951:
215:
75:
41:
1497:
1389:
1354:
1349:
1518:
1437:
1344:
1194:
947:
860:
Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, et al. (November 2004).
111:
1590:
1334:
390:
87:
8:
1554:
1234:
1224:
1041:
1036:
515:
292:
270:
53:
46:
784:
Doyle SM, Wickner S (January 2009). "Hsp104 and ClpB: protein disaggregating machines".
1745:
1487:
926:
693:
311:
987:
759:
724:
1216:
918:
883:
842:
801:
763:
728:
697:
685:
647:
608:
604:
577:
549:
398:
252:
142:
930:
493:. They are thought to function by threading client proteins through a small 20 Ă… (2
352:
1533:
1528:
1502:
1430:
1008:
910:
873:
832:
793:
755:
720:
677:
639:
600:
386:
1580:
1564:
1477:
1249:
1244:
1016:
992:
626:
Kessel M, Maurizi MR, Kim B, Kocsis E, Trus BL, Singh SK, Steven AC (July 1995).
461:
364:
1729:
1618:
1559:
878:
861:
837:
820:
797:
170:
681:
1739:
1523:
1482:
1394:
1267:
1256:
988:
510:
1472:
1290:
1184:
1026:
922:
887:
846:
821:"Chaperoned protein disaggregation--the ClpB ring uses its central channel"
805:
732:
689:
643:
767:
651:
612:
581:
553:
1696:
1631:
1467:
1409:
1404:
1053:
218:
99:
30:
ATP-dependent Clp protease (fragment) homo14mer, Streptococcus pneumoniae
914:
1371:
1313:
1094:
1089:
1069:
315:
258:
1670:
1644:
1399:
1385:
1204:
1084:
1074:
494:
274:
248:
627:
1724:
1285:
1280:
1229:
1079:
1064:
1031:
597:
Endopeptidase Clp: ATP-dependent Clp protease from
Escherichia coli
456:
359:
1339:
1329:
1275:
1189:
1021:
489:) break up insoluble protein aggregates in conjunction with DnaK/
262:
118:
710:
1683:
1453:
1366:
1308:
486:
418:
281:
182:
94:
82:
70:
1657:
1375:
1361:
1300:
1174:
1169:
1164:
1159:
1154:
1149:
859:
745:
490:
314:
complex thought to resemble the hypothetical ancestor of the
307:
278:
566:
1144:
1139:
1134:
1129:
1124:
1119:
1109:
1104:
900:
498:
482:
380:
347:
296:
106:
1422:
599:. Methods in Enzymology. Vol. 244. pp. 314–31.
284:
activity. ClpP and ClpA are not evolutionarily related.
594:
25:
625:
269:
This bacterial enzyme contains subunits of two types,
1713:
539:
667:
595:Maurizi MR, Thompson MW, Singh SK, Kim SH (1994).
1737:
521:ATP-dependent Clp protease proteolytic subunit
1438:
973:
853:
783:
812:
1445:
1431:
980:
966:
950:at the U.S. National Library of Medicine
877:
836:
779:
777:
818:
663:
661:
1738:
993:serine proteases/serine endopeptidases
774:
1426:
961:
739:
277:activity, and the protein ClpA, with
704:
658:
570:The Journal of Biological Chemistry
542:The Journal of Biological Chemistry
13:
14:
1757:
941:
1723:
24:
894:
786:Trends in Biochemical Sciences
748:Trends in Biochemical Sciences
619:
588:
560:
533:
265:in the presence of ATP and Mg.
1:
1205:Urinary plasminogen activator
760:10.1016/S0968-0004(96)10038-4
725:10.1016/s0022-2836(02)01470-5
526:
375:Available protein structures:
1200:Tissue plasminogen activator
819:Horwich AL (November 2004).
713:Journal of Molecular Biology
632:Journal of Molecular Biology
605:10.1016/0076-6879(94)44025-5
295:subunits (ClpA, ClpC, ClpE,
7:
1452:
504:
10:
1762:
879:10.1016/j.cell.2004.11.027
838:10.1016/j.cell.2004.11.018
798:10.1016/j.tibs.2008.09.010
235:ATP-dependent Clp protease
1609:
1601:Michaelis–Menten kinetics
1573:
1542:
1511:
1460:
1322:
1299:
1291:Proteinase 3/Myeloblastin
1265:
1215:
1052:
1007:
682:10.1016/j.arr.2014.12.010
455:
447:
442:
437:
417:
397:
379:
374:
370:
358:
346:
338:
333:
328:
321:
193:
181:
169:
164:
160:
141:
129:
117:
105:
93:
81:
69:
64:
52:
40:
35:
23:
18:
1493:Diffusion-limited enzyme
952:Medical Subject Headings
670:Ageing Research Reviews
1345:Proprotein convertases
644:10.1006/jmbi.1995.0400
1586:Eadie–Hofstee diagram
1519:Allosteric regulation
1195:Plasminogen activator
261:of proteins to small
227:caseinolytic protease
1596:Lineweaver–Burk plot
1335:Prolyl endopeptidase
903:Biological Chemistry
299:, ClpY, or others).
915:10.1515/BC.2005.128
516:CLP protease family
1555:Enzyme superfamily
1488:Enzyme promiscuity
312:heat shock protein
1711:
1710:
1420:
1419:
1217:Complement system
1009:Digestive enzymes
948:Endopeptidase+Clp
467:
466:
433:
432:
429:
428:
424:structure summary
253:chemical reaction
212:Endopeptidase Clp
209:
208:
205:
204:
124:metabolic pathway
19:Endopeptidase Clp
1753:
1728:
1727:
1719:
1591:Hanes–Woolf plot
1534:Enzyme activator
1529:Enzyme inhibitor
1503:Enzyme catalysis
1447:
1440:
1433:
1424:
1423:
982:
975:
968:
959:
958:
935:
934:
898:
892:
891:
881:
857:
851:
850:
840:
816:
810:
809:
781:
772:
771:
743:
737:
736:
708:
702:
701:
665:
656:
655:
623:
617:
616:
592:
586:
585:
576:(21): 12536–45.
564:
558:
557:
537:
435:
434:
372:
371:
326:
325:
223:endopeptidase Ti
162:
161:
28:
16:
15:
1761:
1760:
1756:
1755:
1754:
1752:
1751:
1750:
1736:
1735:
1734:
1722:
1714:
1712:
1707:
1619:Oxidoreductases
1605:
1581:Enzyme kinetics
1569:
1565:List of enzymes
1538:
1507:
1478:Catalytic triad
1456:
1451:
1421:
1416:
1318:
1295:
1261:
1211:
1048:
1017:Enteropeptidase
1003:
986:
944:
939:
938:
909:(11): 1115–27.
899:
895:
858:
854:
817:
813:
782:
775:
744:
740:
709:
705:
676:(Pt A): 56–66.
666:
659:
624:
620:
593:
589:
565:
561:
548:(14): 7886–93.
538:
534:
529:
507:
485:"Hsp78", yeast
324:
247:). This enzyme
31:
12:
11:
5:
1759:
1749:
1748:
1733:
1732:
1709:
1708:
1706:
1705:
1692:
1679:
1666:
1653:
1640:
1627:
1613:
1611:
1607:
1606:
1604:
1603:
1598:
1593:
1588:
1583:
1577:
1575:
1571:
1570:
1568:
1567:
1562:
1557:
1552:
1546:
1544:
1543:Classification
1540:
1539:
1537:
1536:
1531:
1526:
1521:
1515:
1513:
1509:
1508:
1506:
1505:
1500:
1495:
1490:
1485:
1480:
1475:
1470:
1464:
1462:
1458:
1457:
1450:
1449:
1442:
1435:
1427:
1418:
1417:
1415:
1414:
1413:
1412:
1407:
1397:
1392:
1383:
1369:
1364:
1359:
1358:
1357:
1352:
1342:
1337:
1332:
1326:
1324:
1320:
1319:
1317:
1316:
1311:
1305:
1303:
1297:
1296:
1294:
1293:
1288:
1283:
1278:
1272:
1270:
1263:
1262:
1260:
1259:
1254:
1253:
1252:
1247:
1237:
1232:
1227:
1221:
1219:
1213:
1212:
1210:
1209:
1208:
1207:
1202:
1192:
1180:
1179:
1178:
1177:
1172:
1167:
1162:
1157:
1152:
1147:
1142:
1137:
1132:
1127:
1122:
1117:
1112:
1107:
1102:
1092:
1087:
1082:
1077:
1072:
1067:
1058:
1056:
1050:
1049:
1047:
1046:
1045:
1044:
1039:
1029:
1024:
1019:
1013:
1011:
1005:
1004:
989:Endopeptidases
985:
984:
977:
970:
962:
956:
955:
943:
942:External links
940:
937:
936:
893:
852:
811:
773:
738:
719:(5): 1437–48.
703:
657:
618:
587:
559:
531:
530:
528:
525:
524:
523:
518:
513:
506:
503:
465:
464:
459:
453:
452:
449:
445:
444:
440:
439:
431:
430:
427:
426:
421:
415:
414:
401:
395:
394:
384:
377:
376:
368:
367:
362:
356:
355:
350:
344:
343:
340:
336:
335:
331:
330:
323:
320:
267:
266:
251:the following
207:
206:
203:
202:
197:
191:
190:
185:
179:
178:
173:
167:
166:
158:
157:
146:
139:
138:
133:
127:
126:
121:
115:
114:
109:
103:
102:
97:
91:
90:
85:
79:
78:
73:
67:
66:
62:
61:
56:
50:
49:
44:
38:
37:
33:
32:
29:
21:
20:
9:
6:
4:
3:
2:
1758:
1747:
1744:
1743:
1741:
1731:
1726:
1721:
1720:
1717:
1703:
1699:
1698:
1693:
1690:
1686:
1685:
1680:
1677:
1673:
1672:
1667:
1664:
1660:
1659:
1654:
1651:
1647:
1646:
1641:
1638:
1634:
1633:
1628:
1625:
1621:
1620:
1615:
1614:
1612:
1608:
1602:
1599:
1597:
1594:
1592:
1589:
1587:
1584:
1582:
1579:
1578:
1576:
1572:
1566:
1563:
1561:
1560:Enzyme family
1558:
1556:
1553:
1551:
1548:
1547:
1545:
1541:
1535:
1532:
1530:
1527:
1525:
1524:Cooperativity
1522:
1520:
1517:
1516:
1514:
1510:
1504:
1501:
1499:
1496:
1494:
1491:
1489:
1486:
1484:
1483:Oxyanion hole
1481:
1479:
1476:
1474:
1471:
1469:
1466:
1465:
1463:
1459:
1455:
1448:
1443:
1441:
1436:
1434:
1429:
1428:
1425:
1411:
1408:
1406:
1403:
1402:
1401:
1398:
1396:
1395:Streptokinase
1393:
1391:
1387:
1384:
1381:
1377:
1373:
1370:
1368:
1365:
1363:
1360:
1356:
1353:
1351:
1348:
1347:
1346:
1343:
1341:
1338:
1336:
1333:
1331:
1328:
1327:
1325:
1321:
1315:
1312:
1310:
1307:
1306:
1304:
1302:
1298:
1292:
1289:
1287:
1284:
1282:
1279:
1277:
1274:
1273:
1271:
1269:
1268:immune system
1264:
1258:
1257:C3-convertase
1255:
1251:
1248:
1246:
1243:
1242:
1241:
1238:
1236:
1233:
1231:
1228:
1226:
1223:
1222:
1220:
1218:
1214:
1206:
1203:
1201:
1198:
1197:
1196:
1193:
1191:
1188:
1186:
1182:
1181:
1176:
1173:
1171:
1168:
1166:
1163:
1161:
1158:
1156:
1153:
1151:
1148:
1146:
1143:
1141:
1138:
1136:
1133:
1131:
1128:
1126:
1123:
1121:
1118:
1116:
1113:
1111:
1108:
1106:
1103:
1101:
1098:
1097:
1096:
1093:
1091:
1088:
1086:
1083:
1081:
1078:
1076:
1073:
1071:
1068:
1066:
1063:
1060:
1059:
1057:
1055:
1051:
1043:
1040:
1038:
1035:
1034:
1033:
1030:
1028:
1025:
1023:
1020:
1018:
1015:
1014:
1012:
1010:
1006:
1001:
998:
994:
990:
983:
978:
976:
971:
969:
964:
963:
960:
953:
949:
946:
945:
932:
928:
924:
920:
916:
912:
908:
904:
897:
889:
885:
880:
875:
872:(5): 653–65.
871:
867:
863:
856:
848:
844:
839:
834:
831:(5): 579–81.
830:
826:
822:
815:
807:
803:
799:
795:
791:
787:
780:
778:
769:
765:
761:
757:
754:(8): 289–96.
753:
749:
742:
734:
730:
726:
722:
718:
714:
707:
699:
695:
691:
687:
683:
679:
675:
671:
664:
662:
653:
649:
645:
641:
638:(5): 587–94.
637:
633:
629:
622:
614:
610:
606:
602:
598:
591:
583:
579:
575:
571:
563:
555:
551:
547:
543:
536:
532:
522:
519:
517:
514:
512:
511:Endopeptidase
509:
508:
502:
500:
496:
492:
488:
484:
479:
476:
472:
463:
460:
458:
454:
450:
446:
441:
436:
425:
422:
420:
416:
413:
409:
405:
402:
400:
396:
392:
388:
385:
382:
378:
373:
369:
366:
363:
361:
357:
354:
351:
349:
345:
341:
337:
332:
327:
319:
317:
313:
309:
305:
300:
298:
294:
290:
285:
283:
280:
276:
272:
264:
260:
257:
256:
255:
254:
250:
246:
242:
241:
236:
232:
228:
224:
220:
217:
213:
201:
198:
196:
192:
189:
186:
184:
180:
177:
174:
172:
168:
163:
159:
156:
153:
150:
147:
144:
140:
137:
134:
132:
128:
125:
122:
120:
116:
113:
110:
108:
104:
101:
100:NiceZyme view
98:
96:
92:
89:
86:
84:
80:
77:
74:
72:
68:
63:
60:
57:
55:
51:
48:
45:
43:
39:
34:
27:
22:
17:
1697:Translocases
1694:
1681:
1668:
1655:
1642:
1632:Transferases
1629:
1616:
1473:Binding site
1185:fibrinolysis
1183:
1061:
1027:Chymotrypsin
906:
902:
896:
869:
865:
855:
828:
824:
814:
789:
785:
751:
747:
741:
716:
712:
706:
673:
669:
635:
631:
621:
596:
590:
573:
569:
562:
545:
541:
535:
480:
474:
470:
468:
303:
301:
286:
268:
245:Clp protease
244:
238:
234:
230:
226:
222:
211:
210:
88:BRENDA entry
59:110910-59-3
1468:Active site
1090:Factor XIIa
1070:Factor VIIa
1054:Coagulation
792:(1): 40–8.
443:Identifiers
334:Identifiers
310:complex, a
231:protease Ti
76:IntEnz view
36:Identifiers
1671:Isomerases
1645:Hydrolases
1512:Regulation
1372:Subtilisin
1314:Batroxobin
1095:Kallikrein
1085:Factor XIa
1075:Factor IXa
1042:Pancreatic
1037:Neutrophil
527:References
475:HSP100/Clp
387:structures
316:proteasome
259:Hydrolysis
145:structures
112:KEGG entry
1746:EC 3.4.21
1550:EC number
1400:Cathepsin
1386:Sedolisin
1362:Prostasin
1080:Factor Xa
698:205667759
462:IPR004487
365:IPR001270
275:peptidase
249:catalyses
219:3.4.21.92
65:Databases
47:3.4.21.92
1740:Category
1574:Kinetics
1498:Cofactor
1461:Activity
1301:Venombin
1286:Tryptase
1281:Granzyme
1235:Factor I
1230:Factor D
1225:Factor B
1065:Thrombin
1062:factors:
1032:Elastase
931:34095247
923:16307477
888:15550247
847:15550237
806:19008106
733:12595256
690:25578288
505:See also
457:InterPro
404:RCSB PDB
360:InterPro
293:chaperon
263:peptides
200:proteins
188:articles
176:articles
149:RCSB PDB
1730:Biology
1684:Ligases
1454:Enzymes
1340:Pronase
1330:Acrosin
1276:Chymase
1190:Plasmin
1022:Trypsin
768:8772382
652:7623377
613:7845217
582:2197275
554:2186030
353:PF02861
304:E. coli
273:, with
136:profile
119:MetaCyc
54:CAS no.
1716:Portal
1658:Lyases
1367:Reelin
1309:Ancrod
1266:Other
1000:3.4.21
954:(MeSH)
929:
921:
886:
845:
804:
766:
731:
696:
688:
650:
611:
580:
552:
487:Hsp104
471:Hsp100
448:Symbol
419:PDBsum
393:
383:
342:ClpA/B
339:Symbol
329:ClpA/B
322:ATPase
282:ATPase
183:PubMed
165:Search
155:PDBsum
95:ExPASy
83:BRENDA
71:IntEnz
42:EC no.
1610:Types
1376:Furin
1323:Other
1250:MASP2
1245:MASP1
1175:KLK15
1170:KLK14
1165:KLK13
1160:KLK12
1155:KLK11
1150:KLK10
927:S2CID
694:S2CID
491:Hsp70
308:HslVU
131:PRIAM
1702:list
1695:EC7
1689:list
1682:EC6
1676:list
1669:EC5
1663:list
1656:EC4
1650:list
1643:EC3
1637:list
1630:EC2
1624:list
1617:EC1
1390:TPP1
1240:MASP
1145:KLK9
1140:KLK8
1135:KLK7
1130:KLK6
1125:KLK5
1120:KLK4
1115:KLK3
1110:KLK2
1105:KLK1
919:PMID
884:PMID
866:Cell
843:PMID
825:Cell
802:PMID
764:PMID
729:PMID
686:PMID
648:PMID
609:PMID
578:PMID
550:PMID
499:T6SS
483:CLPB
469:The
451:ClpX
438:ClpX
412:PDBj
408:PDBe
391:ECOD
381:Pfam
348:Pfam
297:ClpX
289:ClpP
279:AAA+
271:ClpP
240:ClpP
195:NCBI
152:PDBe
107:KEGG
1380:S1P
1100:PSA
911:doi
907:386
874:doi
870:119
833:doi
829:119
794:doi
756:doi
721:doi
717:326
678:doi
640:doi
636:250
601:doi
574:265
546:265
399:PDB
171:PMC
143:PDB
1742::
997:EC
991::
925:.
917:.
905:.
882:.
868:.
864:.
841:.
827:.
823:.
800:.
790:34
788:.
776:^
762:.
752:21
750:.
727:.
715:.
692:.
684:.
674:23
672:.
660:^
646:.
634:.
630:.
607:.
572:.
544:.
501:.
495:nm
410:;
406:;
389:/
318:.
243:,
237:,
233:,
229:,
225:,
221:,
216:EC
1718::
1704:)
1700:(
1691:)
1687:(
1678:)
1674:(
1665:)
1661:(
1652:)
1648:(
1639:)
1635:(
1626:)
1622:(
1446:e
1439:t
1432:v
1410:G
1405:A
1388:/
1382:4
1378:/
1374:/
1355:2
1350:1
1187::
1002:)
995:(
981:e
974:t
967:v
933:.
913::
890:.
876::
849:.
835::
808:.
796::
770:.
758::
735:.
723::
700:.
680::
654:.
642::
615:.
603::
584:.
556:.
214:(
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
