ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial
1_MPSCG 6_ ACTCG 11_ AAAVR 16_ LITSS 21_ LASAQ 26_ RGISG 31_ GRIHM 36_ SVLGR 41_ LGTFE 46_ TQILQ 51_ RAPLR 56_ SFTET 61_ PAYFA 66_ SKDGI 71_ SKDGS 76_ GDGNK 81_ KSASE 86_ GSSKK 91_ SGSGN 96_ SGKGG 101_ NQLRC 106_ PKCGD 111_ LCTHV 116_ ETFVS 121_ STRFV 126_ KCEKC 131_ HHFFV 136_ VLSEA 141_ DSKKS 146_ IIKEP 151_ ESAAE 156_ AVKLA 161_ FQQKP 166_ PPPPK 171_ KIYNY 176_ LDKYV 181_ VGQSF 186_ AKKVL 191_ SVAVY 196_ NHYKR 201_ IYNNI 206_ PANLR 211_ QQAEV 216_ EKQTS 221_ LTPRE 226_ LEIRR 231_ REDEY 236_ RFTKL 241_ LQIAG 246_ ISPHG 251_ NALGA 256_ SMQQQ 261_ VNQQI 266_ PQEKR 271_ GGEVL 276_ DSSHD 281_ DIKLE 286_ KSNIL 291_ LLGPT 296_ GSGKT 301_ LLAQT 306_ LAKCL 311_ DVPFA 316_ ICDCT 321_ TLTQA 326_ GYVGE 331_ DIESV 336_ IAKLL 341_ QDANY 346_ NVEKA 351_ QQGIV 356_ FLDEV 361_ DKIGS 366_ VPGIH 371_ QLRDV 376_ GGEGV 381_ QQGLL 386_ KLLEG 391_ TIVNV 396_ PEKNS 401_ RKLRG 406_ ETVQV 411_ DTTNI 416_ LFVAS 421_ GAFNG 426_ LDRII 431_ SRRKN 436_ EKYLG 441_ FGTPS 446_ NLGKG 451_ RRAAA 456_ AADLA 461_ NRSGE 466_ SNTHQ 471_ DIEEK 476_ DRLLR 481_ HVEAR 486_ DLIEF 491_ GMIPE 496_ FVGRL 501_ PVVVP 506_ LHSLD 511_ EKTLV 516_ QILTE 521_ PRNAV 526_ IPQYQ 531_ ALFSM 536_ DKCEL 541_ NVTED 546_ ALKAI 551_ ARLAL 556_ ERKTG 561_ ARGLR 566_ SIMEK 571_ LLLEP 576_ MFEVP 581_ NSDIV 586_ CVEVD 591_ KEVVE 596_ GKKEP 601_ GYIRA 606_ PTKES 611_ SEEEY 616_ DSGVE 621_ EEGWP 626_RQADA
1: ATP-dependent chaperone that functions as an unfoldase. As part of the ClpXP protease complex, it recognizes specific protein substrates, unfolds them using energy derived from ATP hydrolysis, and then translocates them to the proteolytic subunit (CLPP) of the ClpXP complex for degradation (PubMed:11923310, PubMed:22710082, PubMed:28874591). Thanks to its chaperone activity, it also functions in the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis (PubMed:28874591). This chaperone is also involved in the control of mtDNA nucleoid distribution, by regulating mitochondrial transcription factor A (TFAM) activity (PubMed:22841477)