60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein)
1_MLRLP 6_ TVFRQ 11_ MRPVS 16_ RVLAP 21_ HLTRA 26_ YAKDV 31_ KFGAD 36_ ARALM 41_ LQGVD 46_ LLADA 51_ VAVTM 56_ GPKGR 61_ TVIIE 66_ QSWGS 71_ PKVTK 76_ DGVTV 81_ AKSID 86_ LKDKY 91_ KNIGA 96_ KLVQD 101_ VANNT 106_ NEEAG 111_ DGTTT 116_ ATVLA 121_ RSIAK 126_ EGFEK 131_ ISKGA 136_ NPVEI 141_ RRGVM 146_ LAVDA 151_ VIAEL 156_ KKQSK 161_ PVTTP 166_ EEIAQ 171_ VATIS 176_ ANGDK 181_ EIGNI 186_ ISDAM 191_ KKVGR 196_ KGVIT 201_ VKDGK 206_ TLNDE 211_ LEIIE 216_ GMKFD 221_ RGYIS 226_ PYFIN 231_ TSKGQ 236_ KCEFQ 241_ DAYVL 246_ LSEKK 251_ ISSIQ 256_ SIVPA 261_ LEIAN 266_ AHRKP 271_ LVIIA 276_ EDVDG 281_ EALST 286_ LVLNR 291_ LKVGL 296_ QVVAV 301_ KAPGF 306_ GDNRK 311_ NQLKD 316_ MAIAT 321_ GGAVF 326_ GEEGL 331_ TLNLE 336_ DVQPH 341_ DLGKV 346_ GEVIV 351_ TKDDA 356_ MLLKG 361_ KGDKA 366_ QIEKR 371_ IQEII 376_ EQLDV 381_ TTSEY 386_ EKEKL 391_ NERLA 396_ KLSDG 401_ VAVLK 406_ VGGTS 411_ DVEVN 416_ EKKDR 421_ VTDAL 426_ NATRA 431_ AVEEG 436_ IVLGG 441_ GCALL 446_ RCIPA 451_ LDSLT 456_ PANED 461_ QKIGI 466_ EIIKR 471_ TLKIP 476_ AMTIA 481_ KNAGV 486_ EGSLI 491_ VEKIM 496_ QSSSE 501_ VGYDA 506_ MAGDF 511_ VNMVE 516_ KGIID 521_ PTKVV 526_ RTALL 531_ DAAGV 536_ ASLLT 541_ TAEVV 546_ VTEIP 551_ KEEKD 556_ PGMGA 561_ MGGMG 566_GGMGG
1: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable)