Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 60 kDa chaperonin 1 |
Protein Synonyms/Alias | |
Gene Name | groL1 |
Gene Synonyms/Alias | groEL1; OrderedLocusNames=SCO4762 |
Created Date | 3-June-2014 |
Organism | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
NCBI Taxa ID | 100226 |
Phosphorylation | Position | Peptide | Code | Type | References | 88 | NDIAGDGTTTATVLA | T | HTP | [1] | 80 | VKEVATKTNDIAGDG | T | HTP | [1] | 89 | DIAGDGTTTATVLAQ | T | HTP | [1] | 438 | GKTGDEATGVAVVRR | T | HTP | [1] | 482 | GQGFNAATGEYGDLV | T | HTP | [1] | 500 | VIDPVKVTRSALENA | T | HTP | [1] | 485 | FNAATGEYGDLVKAG | Y | HTP | [1] | 90 | IAGDGTTTATVLAQA | T | HTP | [1] | |
Reference | [1]Phosphoproteome analysis of Streptomyces development reveals extensive protein phosphorylation accompanying bacterial differentiation. Manteca A,Ye J,Sánchez J,Jensen ON J. Proteome Res. 2011, Dec, 2;10(12):5481-92. [ PMID:21999169] |
Functional Description From UniProt | FUNCTION: Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity) |
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| ATP-binding; Chaperone; Completeproteome; Cytoplasm; Nucleotide-binding; Referenceproteome |
Protein Sequence | MAKILKFDED ARRALERGVN KLADTVKVTI GPKGRNVVID KKFGAPTITN DGVTIAREVE 60 VEDPYENLGA QLVKEVATKT NDIAGDGTTT ATVLAQALVR EGLKNVAAGA SPALLKKGID 120 AAVAAVSEDL LATARPIDEK SDIAAVAALS AQDQQVGELI AEAMDKVGKD GVITVEESNT 180 FGLELDFTEG MAFDKGYLSP YFVTDQERME AVLDDPYILI NQGKISSIAD LLPLLEKVIQ 240 ANASKPLLII AEDLEGEALS TLVVNKIRGT FNAVAVKAPG FGDRRKAMLQ DMAVLTGATV 300 ISEEVGLKLD QVGLEVLGTA RRITVTKDDT TIVDGAGKRD EVQGRIAQIK AEIENTDSDW 360 DREKLQERLA KLAGGVCVIK VGAATEVELK ERKHRLEDAI SATRAAVEEG IVSGGGSALV 420 HAVKVLEGNL GKTGDEATGV AVVRRAAVEP LRWIAENAGL EGYVITSKVA DLDKGQGFNA 480 ATGEYGDLVK AGVIDPVKVT RSALENAASI ASLLLTTETL VVEKKEEEEP AAGGHSHGHS 540 H 541 |
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