| Tag | Content |
|---|
| CPLM ID | CPLM-026693 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Lon protease |
Protein Synonyms/Alias | ATP-dependent protease La |
Gene Name | lon |
Gene Synonyms/Alias | RPA2959 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 335 | SDHYGLEKVKERIVE | acetylation | [1] | | 640 | GNLRDVMKESIQAAA | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity). |
Sequence Annotation | DOMAIN 18 208 Lon (By similarity).
NP_BIND 362 369 ATP (By similarity).
ACT_SITE 684 684 By similarity.
ACT_SITE 727 727 By similarity. |
Keyword | ATP-binding; Complete proteome; Cytoplasm; Hydrolase; Nucleotide-binding; Protease; Serine protease; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 810 AA |
Protein Sequence | MTATKPRPSI TYGESHSYPV LPLRDIVVFP HMIVPLFVGR EKSIRALEEV MKNDALIMLA 60
TQKNASDDDP APDAIYEIGT LASVLQLLKL PDGTVKVLVE GLARAKVDKY TDRADYYEAD 120
AVALEDSDAT SVEAEALGRS VVSDFESYVK LNKKISAEVV GVVQSITDFA KLADTVASHL 180
AVKIADRQGI LETLSVTQRL EKVLGLMESE ISVLQVEKRI RSRVKRQMEK TQREYYLNEQ 240
MKAIQKELGD EDGRDELAEL EEKIAKTKLS KEAREKAQHE LKKLRQMSPM SAEATVVRNY 300
LDWLLSIPWN KKSKVKKDLE AAQAVLDSDH YGLEKVKERI VEYLAVQSRA NKLSGPILCL 360
VGPPGVGKTS LGKSIAKATG REFVRVSLGG VRDEAEIRGH RRTYIGSMPG KIIQSMRKAK 420
TSNPLFLLDE IDKMGADFRG DPSSALLEVL DPEQNGTFND HYLEVDYDLS NVMFITTANT 480
LNIPGPLMDR MEIIRIAGYT ETEKVEIARK HLIPLALTKH GLEPKEWSID DNALLLVIRR 540
YTREAGVRNL EREISTLARK VVKDLMLSKK KSVHIDEKQI EEYLGVPKFR FGEIEKDDQV 600
GVVTGLAWTD VGGELLTIES VMMPGKGRMT VTGNLRDVMK ESIQAAASYV RSRAITFGIE 660
PPFFEKRDIH VHVPEGATPK DGPSAGVAMA TTIVSVLTGI PIRRDIAMTG EITLRGRVLP 720
IGGLKEKLLA AARGGIKTVL IPEDNAKDLT EISDAIKGGL NIIPVARMDE VIANALTRAP 780
VPIVWEEETK LPGTPDSAEA DEAGGGLTAH 810 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0004176; F:ATP-dependent peptidase activity; IEA:HAMAP. GO:0043565; F:sequence-specific DNA binding; IEA:HAMAP. GO:0004252; F:serine-type endopeptidase activity; IEA:HAMAP. GO:0006200; P:ATP catabolic process; IEA:GOC. GO:0033554; P:cellular response to stress; IEA:HAMAP. GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IEA:HAMAP. |
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