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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T.,
Nakamura Y.,
Sato S.,
Minamisawa K.,
Uchiumi T.,
Sasamoto S.,
Watanabe A.,
Idesawa K.,
Iriguchi M.,
Kawashima K.,
Kohara M.,
Matsumoto M.,
Shimpo S.,
Tsuruoka H.,
Wada T.,
Yamada M.,
Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).
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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: 211 AA [This is the length of the unprocessed precursor] |
Molecular weight: 23510 Da [This is the MW of the unprocessed precursor] |
CRC64: DF7A75EC38AE48D6 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MRDPVETYMN LVPMVVEQTN RGERAYDIFS RLLKERIIFL TGPVEDGMST LVVAQLLFLE
70 80 90 100 110 120
AENPKKEISM YINSPGGVVT SGLAIYDTMQ FIRPPVSTLC TGQAASMGSL LLAAGEKDMR
130 140 150 160 170 180
FSLPNARIMV HQPSGGFQGQ ATDIMLHAQE ILNLKKRLNE IYVKHTGQTY KTIEDALERD
190 200 210
KFLTANDAKE FGLVDRVIDK RAEEPAAAKT Q
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Q89KG1 in FASTA format |
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