Heat shock 70 kDa protein 6 (Heat shock 70 kDa protein B')
1_MQAPR 6_ ELAVG 11_ IDLGT 16_ TYSCV 21_ GVFQQ 26_ GRVEI 31_ LANDQ 36_ GNRTT 41_ PSYVA 46_ FTDTE 51_ RLVGD 56_ AAKSQ 61_ AALNP 66_ HNTVF 71_ DAKRL 76_ IGRKF 81_ ADTTV 86_ QSDMK 91_ HWPFR 96_ VVSEG 101_ GKPKV 106_ RVCYR 111_ GEDKT 116_ FYPEE 121_ ISSMV 126_ LSKMK 131_ ETAEA 136_ YLGQP 141_ VKHAV 146_ ITVPA 151_ YFNDS 156_ QRQAT 161_ KDAGA 166_ IAGLN 171_ VLRII 176_ NEPTA 181_ AAIAY 186_ GLDRR 191_ GAGER 196_ NVLIF 201_ DLGGG 206_ TFDVS 211_ VLSID 216_ AGVFE 221_ VKATA 226_ GDTHL 231_ GGEDF 236_ DNRLV 241_ NHFME 246_ EFRRK 251_ HGKDL 256_ SGNKR 261_ ALRRL 266_ RTACE 271_ RAKRT 276_ LSSST 281_ QATLE 286_ IDSLF 291_ EGVDF 296_ YTSIT 301_ RARFE 306_ ELCSD 311_ LFRST 316_ LEPVE 321_ KALRD 326_ AKLDK 331_ AQIHD 336_ VVLVG 341_ GSTRI 346_ PKVQK 351_ LLQDF 356_ FNGKE 361_ LNKSI 366_ NPDEA 371_ VAYGA 376_ AVQAA 381_ VLMGD 386_ KCEKV 391_ QDLLL 396_ LDVAP 401_ LSLGL 406_ ETAGG 411_ VMTTL 416_ IQRNA 421_ TIPTK 426_ QTQTF 431_ TTYSD 436_ NQPGV 441_ FIQVY 446_ EGERA 451_ MTKDN 456_ NLLGR 461_ FELSG 466_ IPPAP 471_ RGVPQ 476_ IEVTF 481_ DIDAN 486_ GILSV 491_ TATDR 496_ STGKA 501_ NKITI 506_ TNDKG 511_ RLSKE 516_ EVERM 521_ VHEAE 526_ QYKAE 531_ DEAQR 536_ DRVAA 541_ KNSLE 546_ AHVFH 551_ VKGSL 556_ QEESL 561_ RDKIP 566_ EEDRR 571_ KMQDK 576_ CREVL 581_ AWLEH 586_ NQLAE 591_ KEEYE 596_ HQKRE 601_ LEQIC 606_ RPIFS 611_ RLYGG 616_ PGVPG 621_ GSSCG 626_ TQARQ 631_ GDPST 636_GPIIE
1: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365)