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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1;
DOI=10.1073/pnas.1431443100; PubMed=12835416 [NCBI, ExPASy, EBI, Israel, Japan]
Gloeckner F.O.,
Kube M.,
Bauer M.,
Teeling H.,
Lombardot T.,
Ludwig W.,
Gade D.,
Beck A.,
Borzym K.,
Heitmann K.,
Rabus R.,
Schlesner H.,
Amann R.,
Reinhardt R.;
"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1.";
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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: 227 AA [This is the length of the unprocessed precursor] |
Molecular weight: 25139 Da [This is the MW of the unprocessed precursor] |
CRC64: 16CA525C877762AD [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSDPFGSPFP SLHDQNLNAQ HAMASDHRLA NAASYQSYQR QRQMTLGDLL LENRIVFMQG
70 80 90 100 110 120
EIHYANANEI VMKLLYLQSE NRRKDIHLYI NSPGGSVTAT LAIYDTMQML SCPVATYCVG
130 140 150 160 170 180
EACSGAAVLL IGGAKGKRFC LPNSRVMMHQ PLGGVSGQVS DIEIQAAEMF RYRDKLNEII
190 200 210 220
SSHCGKSVEQ IAKDTDRDFF LDAQQAKEYG LVDDLLLGTP ASEEDED
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Q7UK67 in FASTA format |
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