Tag | Content |
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CPLM ID | CPLM-003186 |
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 | capR; deg; lopA; muc; b0439; JW0429 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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89 | KLPDGTVKVLVEGLQ | acetylation | [1, 2] | 113 | NGEHFSAKAEYLESP | acetylation | [2] | 143 | SQFEGYIKLNKKIPP | acetylation | [2] | 176 | IAAHMPLKLADKQSV | acetylation | [2] | 235 | YYLNEQMKAIQKELG | acetylation | [2] | 239 | EQMKAIQKELGEMDD | acetylation | [2] | 255 | PDENEALKRKIDAAK | acetylation | [2] | 405 | YIGSMPGKLIQKMAK | acetylation | [2] | 409 | MPGKLIQKMAKVGVK | acetylation | [1, 2] | 412 | KLIQKMAKVGVKNPL | acetylation | [2] | 416 | KMAKVGVKNPLFLLD | acetylation | [2] | 427 | FLLDEIDKMSSDMRG | acetylation | [2] | 509 | AKRHLLPKQIERNAL | acetylation | [1] | 550 | GLEREISKLCRKAVK | acetylation | [2] | 557 | KLCRKAVKQLLLDKS | acetylation | [2] | 563 | VKQLLLDKSLKHIEI | acetylation | [2] | 566 | LLLDKSLKHIEINGD | acetylation | [1, 2] | 623 | ACVPGKGKLTYTGSL | acetylation | [1] | 651 | VVRARAEKLGINPDF | acetylation | [1, 2] | 661 | INPDFYEKRDIHVHV | acetylation | [2] | 720 | VLPIGGLKEKLLAAH | acetylation | [2] | 722 | PIGGLKEKLLAAHRG | acetylation | [2] | 741 | VLIPFENKRDLEEIP | acetylation | [2] | 761 | DLDIHPVKRIEEVLT | acetylation | [2] |
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Reference | [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. 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. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system. |
Sequence Annotation | DOMAIN 10 201 Lon. NP_BIND 356 363 ATP (By similarity). ACT_SITE 679 679 ACT_SITE 722 722 |
Keyword | 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleotide-binding; Protease; Reference proteome; Serine protease; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 784 AA |
Protein Sequence | MNPERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSIRCL EAAMDHDKKI MLVAQKEAST 60 DEPGVNDLFT VGTVASILQM LKLPDGTVKV LVEGLQRARI SALSDNGEHF SAKAEYLESP 120 TIDEREQEVL VRTAISQFEG YIKLNKKIPP EVLTSLNSID DPARLADTIA AHMPLKLADK 180 QSVLEMSDVN ERLEYLMAMM ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE 240 LGEMDDAPDE NEALKRKIDA AKMPKEAKEK AEAELQKLKM MSPMSAEATV VRGYIDWMVQ 300 VPWNARSKVK KDLRQAQEIL DTDHYGLERV KDRILEYLAV QSRVNKIKGP ILCLVGPPGV 360 GKTSLGQSIA KATGRKYVRM ALGGVRDEAE IRGHRRTYIG SMPGKLIQKM AKVGVKNPLF 420 LLDEIDKMSS DMRGDPASAL LEVLDPEQNV AFSDHYLEVD YDLSDVMFVA TSNSMNIPAP 480 LLDRMEVIRL SGYTEDEKLN IAKRHLLPKQ IERNALKKGE LTVDDSAIIG IIRYYTREAG 540 VRGLEREISK LCRKAVKQLL LDKSLKHIEI NGDNLHDYLG VQRFDYGRAD NENRVGQVTG 600 LAWTEVGGDL LTIETACVPG KGKLTYTGSL GEVMQESIQA ALTVVRARAE KLGINPDFYE 660 KRDIHVHVPE GATPKDGPSA GIAMCTALVS CLTGNPVRAD VAMTGEITLR GQVLPIGGLK 720 EKLLAAHRGG IKTVLIPFEN KRDLEEIPDN VIADLDIHPV KRIEEVLTLA LQNEPSGMQV 780 VTAK 784 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:EcoliWiki. GO:0009295; C:nucleoid; IBA:RefGenome. GO:0005524; F:ATP binding; IBA:RefGenome. GO:0004176; F:ATP-dependent peptidase activity; IDA:EcoliWiki. GO:0043565; F:sequence-specific DNA binding; IBA:RefGenome. GO:0004252; F:serine-type endopeptidase activity; IMP:EcoliWiki. GO:0033554; P:cellular response to stress; IEA:HAMAP. GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IBA:RefGenome. GO:0009408; P:response to heat; IEP:EcoliWiki. |
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