| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 60 kDa chaperonin |
Protein Synonyms/Alias | |
Gene Name | groL |
Gene Synonyms/Alias | groEL, mopA; OrderedLocusNames=BSU06030 |
Created Date | 3-June-2014 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Phosphorylation | Position | Peptide | Code | Type | References | | 283 | APGFGDRRKAMLEDI | R | HTP | [1] | | 282 | KAPGFGDRRKAMLED | R | HTP | [1] | | 35 | VTLGPKGRNVVLEKK | R | HTP | [1] | | 116 | GANPVGVRKGMEQAV | R | HTP | [1] | |
Reference | [1]Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Elsholz AK,Turgay K,Michalik S,Hessling B,Gronau K,Oertel D,Mäder U,Bernhardt J,Becher D,Hecker M,Gerth U Proc. Natl. Acad. Sci. U.S.A. 2012, May, 8;109(19):7451-6. [ PMID:22517742] |
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; Directproteinsequencing; Nucleotide-binding; Referenceproteome; Stressresponse |
Protein Sequence | MAKEIKFSEE ARRAMLRGVD ALADAVKVTL GPKGRNVVLE KKFGSPLITN DGVTIAKEIE 60
LEDAFENMGA KLVAEVASKT NDVAGDGTTT ATVLAQAMIR EGLKNVTAGA NPVGVRKGME 120
QAVAVAIENL KEISKPIEGK ESIAQVAAIS AADEEVGSLI AEAMERVGND GVITIEESKG 180
FTTELEVVEG MQFDRGYASP YMVTDSDKME AVLDNPYILI TDKKITNIQE ILPVLEQVVQ 240
QGKPLLLIAE DVEGEALATL VVNKLRGTFN AVAVKAPGFG DRRKAMLEDI AVLTGGEVIT 300
EDLGLDLKST QIAQLGRASK VVVTKENTTI VEGAGETDKI SARVTQIRAQ VEETTSEFDR 360
EKLQERLAKL AGGVAVIKVG AATETELKER KLRIEDALNS TRAAVEEGIV SGGGTALVNV 420
YNKVAAVEAE GDAQTGINIV LRALEEPIRQ IAHNAGLEGS VIVERLKNEE IGVGFNAATG 480
EWVNMIEKGI VDPTKVTRSA LQNAASVAAM FLTTEAVVAD KPEENGGGAG MPDMGGMGGM 540
GGMM 544 |
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