| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Chaperone protein DnaK |
Protein Synonyms/Alias | |
Gene Name | dnaK |
Gene Synonyms/Alias | SPD_0460 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | | 244 | EKAKKDLSGVTSTQI | S | HTP | [1] | | 247 | KKDLSGVTSTQISLP | T | HTP | [1] | | 248 | KDLSGVTSTQISLPF | 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: Acts as a chaperone (By similarity) |
| MOD_RES 173 173 Phosphothreonine; by autocatalysis (By |
| ATP-binding; Chaperone; Completeproteome; Nucleotide-binding; Phosphoprotein; Stressresponse |
Protein Sequence | MSKIIGIDLG TTNSAVAVLE GTESKIIANP EGNRTTPSVV SFKNGEIIVG DAAKRQAVTN 60
PDTVISIKSK MGTSEKVSAN GKEYTPQEIS AMILQYLKGY AEDYLGEKVT KAVITVPAYF 120
NDAQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGLDKTDK EEKILVFDLG GGTFDVSILE 180
LGDGVFDVLS TAGDNKLGGD DFDQKIIDHL VAEFKKENGI DLSTDKMAMQ RLKDAAEKAK 240
KDLSGVTSTQ ISLPFITAGE AGPLHLEMTL TRAKFDDLTR DLVERTKVPV RQALSDAGLS 300
LSEIDEVILV GGSTRIPAVV EAVKAETGKE PNKSVNPDEV VAMGAAIQGG VITGDVKDVV 360
LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMAAD 420
NKTLGRFQLT DIPAAPRGIP QIEVTFDIDK NGIVSVKAKD LGTQKEQTIV IQSNSGLTDE 480
EIDRMMKDAE ANAEADKKRK EEVDLRNEVD QAIFATEKTI KETEGKGFDA ERDAAQAALD 540
DLKKAQEDNN LDDMKAKLEA LNEKAQGLAV KLYEQAAAAQ QAQEGAEGAQ ATGNAGDDVV 600
DGEFTEK 607 |
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