Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 33 kDa chaperonin |
Protein Synonyms/Alias | HSP33 |
Gene Name | hslO |
Gene Synonyms/Alias | SPD_2015 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | 49 | LGRTLIASQILAANE | S | 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: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress (By similarity) |
| DISULFID 235 237 Redox-active (By similarity) DISULFID 268 271 Redox-active (By similarity) |
| Chaperone; Completeproteome; Cytoplasm; Disulfidebond; Redox-activecenter; Zinc |
Protein Sequence | MDKIIKTISE SGAFRAFVLD STETVRTAQE KHQTQASSTV ALGRTLIASQ ILAANEKGNT 60 KLTVKVLGSS SLGAIITVAD TKGNVKGYVQ NPGVDIKKTA TGEVLVGPFV GNGQFLVITD 120 YGTGNPYNSI TPLISGEIGE DLAFYLTESQ QTPSAVGLNV LLDEEDKVKV AGGFLVQVLP 180 GAKKEEIARF EKRIQEMPAI STLLESDDHI EALLKAIYGD EAYKRLSEEE IRFQCDCSHE 240 RFMNALASLP SSDLQEMKEE DHGAEITCQF CQTTYNFDEK DLEELIRDKS 290 |
| |
| |
| |
| |
| |
| |