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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
Nakagawa S.;
"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan]
Kalinowski J.,
Bathe B.,
Bartels D.,
Bischoff N.,
Bott M.,
Burkovski A.,
Dusch N.,
Eggeling L.,
Eikmanns B.J.,
Gaigalat L.,
Goesmann A.,
Hartmann M.,
Huthmacher K.,
Kraemer R.,
Linke B.,
McHardy A.C.,
Meyer F.,
Moeckel B.,
Pfefferle W., ![]()
Puehler A.,
Rey D.A.,
Rueckert C.,
Rupp O.,
Sahm H.,
Wendisch V.F.,
Wiegraebe I.,
Tauch A.;
"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins.";
J. Biotechnol. 104:5-25(2003).
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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: 208 AA [This is the length of the unprocessed precursor] |
Molecular weight: 23037 Da [This is the MW of the unprocessed precursor] |
CRC64: 4972B7CBF0344AA7 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSNGFQMPTS RYVLPSFIEQ SAYGTKETNP YAKLFEERII FLGTQVDDTS ANDIMAQLLV
70 80 90 100 110 120
LEGMDPDRDI TLYINSPGGS FTALMAIYDT MQYVRPDVQT VCLGQAASAA AVLLAAGAPG
130 140 150 160 170 180
KRAVLPNSRV LIHQPATQGT QGQVSDLEIQ AAEIERMRRL METTLAEHTG KTAEQIRIDT
190 200
DRDKILTAEE ALEYGIVDQV FDYRKLKR
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Q8NN02 in FASTA format |
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