| 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; OrderedLocusNames=SPD_1709 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | | 383 | VIKVGAATETELKEM | T | HTP | [1] | | 385 | KVGAATETELKEMKL | T | HTP | [1] | |
Reference | [1]Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. Sun X,Ge F,Xiao CL,Yin XF,Ge R,Zhang LH,He QY J. Proteome Res. 2010, Jan;9(1):275-82. [ PMID:19894762] |
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 |
Protein Sequence | MSKEIKFSSD ARSAMVRGVD ILADTVKVTL GPKGRNVVLE KSFGSPLITN DGVTIAKEIE 60
LEDHFENMGA KLVSEVASKT NDIAGDGTTT ATVLTQAIVR EGIKNVTAGA NPIGIRRGIE 120
TAVAAAVEAL KNNAIPVANK EAIAQVAAVS SRSEKVGEYI SEAMEKVGKD GVITIEESRG 180
METELEVVEG MQFDRGYLSQ YMVTDSEKMV ADLENPYILI TDKKISNIQE ILPLLESILQ 240
SNRPLLIIAD DVDGEALPTL VLNKIRGTFN VVAVKAPGFG DRRKAMLEDI AILTGGTVIT 300
EDLGLELKDA TIEALGQAAR VTVDKDSTVI VEGAGNPEAI SHRVAVIKSQ IETTTSEFDR 360
EKLQERLAKL SGGVAVIKVG AATETELKEM KLRIEDALNA TRAAVEEGIV AGGGTALANV 420
IPAVATLELT GDEATGRNIV LRALEEPVRQ IAHNAGFEGS IVIDRLKNAE LGIGFNAATG 480
EWVNMIDQGI IDPVKVSRSA LQNAASVASL ILTTEAVVAN KPEPVAPAPA MDPSMMGGMM 540 |
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