Protein Info for Psest_3989 in Pseudomonas stutzeri RCH2

Annotation: Disulfide bond chaperones of the HSP33 family

These analyses and tools can help you predict a protein's function, but be skeptical. For enzymes, over 10% of annotations from KEGG or SEED are probably incorrect. For other types of proteins, the error rates may be much higher. MetaCyc and Swiss-Prot have low error rates, but the best hits in these databases are often quite distant, so this protein's function may not be the same. TIGRFam has low error rates. Finally, many experimentally-characterized proteins are not in any of these databases. To find relevant papers, use PaperBLAST.

Protein Families and Features

1 50 100 150 200 250 295 transmembrane" amino acids 43 to 62 (20 residues), see Phobius details PF01430: HSP33" amino acids 3 to 274 (272 residues), 275.9 bits, see alignment E=1.9e-86

Best Hits

Swiss-Prot: 76% identical to HSLO_PSEA7: 33 kDa chaperonin (hslO) from Pseudomonas aeruginosa (strain PA7)

KEGG orthology group: K04083, molecular chaperone Hsp33 (inferred from 91% identity to psa:PST_0292)

Predicted SEED Role

"33 kDa chaperonin (Heat shock protein 33) (HSP33)"

Sequence Analysis Tools

PaperBLAST (search for papers about homologs of this protein)

Search CDD (the Conserved Domains Database, which includes COG and superfam)

Compare to protein structures

Predict protein localization: PSORTb (Gram-negative bacteria)

Predict transmembrane helices and signal peptides: Phobius

Check the current SEED with FIGfam search

Find homologs in fast.genomics or the ENIGMA genome browser

See L0GNZ4 at UniProt or InterPro

Protein Sequence (295 amino acids)

>Psest_3989 Disulfide bond chaperones of the HSP33 family (Pseudomonas stutzeri RCH2)
MSDQTQRFLFDDSDVRGEIATLDHSFQHVLAKHSYPEPVAQLLGELLAAAALLVGTLKFD
GLLILQARSSGAVPLLMVECSSARDVRGIARYHAEQIQAGATLGELMPEGMLAITVDPAN
GQRYQGIVDLDGINLAECLTNYFATSEQLPTRFWLNADSRRACGLLLQQLPADRIKDAEE
RDASWQHLRTLADTLTAEELLGLDGETVLHRLYHEEQLRLFDALPIRFRCSCSRERSARA
LISLGEEDAQQLVTEQGGAVTIDCQFCNEKYTYDAADVAQLFAGGGSDSPSDTRH