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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ismej.2007.46; PubMed=18059494 [NCBI, ExPASy, EBI, Israel, Japan]
Bhaya D.,
Grossman A.R.,
Steunou A.-S.,
Khuri N.,
Cohan F.M.,
Hamamura N.,
Melendrez M.C.,
Bateson M.M.,
Ward D.M.,
Heidelberg J.F.;
"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses.";
ISME J. 1:703-713(2007).
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- FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
- SIMILARITY: Belongs to the peptidase S14 family [view classification].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 203 AA [This is the length of the unprocessed precursor] |
Molecular weight: 22566 Da [This is the MW of the unprocessed precursor] |
CRC64: 5E8DB5E780A11436 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MPIGVPRVPY RLPGEPYSQW ISLDDRLYQE RILFIGEPID DSLANTIVGV MLYLNSQDPQ
70 80 90 100 110 120
KDIVMYINSP GGSVTAGMAI YDTMNHIKPD IVTVCVGQAA SMGAFLLAAG TKGKRFALPH
130 140 150 160 170 180
SRIMLHQPSL GTIQGQASDI EIRARETLRV KRRMNEILAQ TTGQPLEKIE RDVERDFYLS
190 200
ATEAQAYGIV DRVIQERSEA MAS
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Q2JHM1 in FASTA format |
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