※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lon protease
Protein Synonyms/Alias
 
Gene Name
 lon
Gene Synonyms/Alias
 Z0545
Created Date
 3-June-2014
Organism
 Escherichia coli O157:H7
NCBI Taxa ID
 83334
Phosphorylation
Position
Peptide
Code
Type
References
243 MEKSQREYYLNEQMK Y HTP [1]
Reference
 [1]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence.
 Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A
 PLoS Pathog. 2013;9(6):e1003403. [PMID:23785281]
Functional Description From UniProt
 FUNCTION: 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 Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overproduction specifically inhibits translation trough at least two different pathways, one of them being the YoeB-YefM toxin- antitoxin system (By similarity)
Sequence Annotation From UniProt
 
Key Word From UniProt
 ATP-binding; Completeproteome; Cytoplasm; DNA-binding; Hydrolase; Nucleotide-binding; Protease; Serineprotease; Stressresponse
Protein Sequence
 MSSDYLAEIK LRESSMNPER SERIEIPVLP LRDVVVYPHM VIPLFVGREK SIRCLEAAMD 60
 HDKKIMLVAQ KEASTDEPGV NDLFTVGTVA SILQMLKLPD GTVKVLVEGL QRARISALSD 120
 NGEHFSAKAE YLESPTIDER EQEVLVRTAI SQFEGYIKLN KKIPPEVLTS LNSIDDPARL 180
 ADTIAAHMPL KLADKQSVLE MSDVNERLEY LMAMMESEID LLQVEKRIRN RVKKQMEKSQ 240
 REYYLNEQMK AIQKELGEMD DAPDENEALK RKIDAAKMPK EAKEKAEAEL QKLKMMSPMS 300
 AEATVVRGYI DWMVQVPWNA RSKVKKDLRQ AQEILNTDHY GLERVKDRIL EYLAVQSRVN 360
 KIKGPILCLV XPPGVGKTSL GQSIAKATGR KYVRMALGGV RDEAEIRGHR RTYIGSMPGK 420
 LIQKMAKVGV KNPLFLLDEI DKMSSDMRGD PASALLEVLD PEQNVAFSDH YLEVDYDLSD 480
 VMFVATSNSM NIPAPLLDRM EVIRLSGYTE DEKLNIAKRH LLPKQIERNA LKKGELTVDD 540
 SAIIGIIRYY TREAGVRGLE REISKLCRKA VKQLLLDKSL KHIEINGDNL HDYLGVQRFD 600
 YGRADNENRV GQVTGLAWTE VGGDLLTIET ACVPGKGKLT YTGSLGEVMQ ESIQAALTVV 660
 RARAEKLGIN PDFYEKRDIH VHVPEGATPK DGPSAGIAMC TALVSCLTGN PVRADVAMTG 720
 EITLRGQVLP IGGLKEKLLA AHRGGIKTVL IPFENKRDLE EIPDNVIADL DIHPVKRIEE 780
 VLTLALQNEP SGMQVVTAK 799
  GO:0005737   C:cytoplasm IEA:UniProtKB-SubCell
  GO:0005524   F:ATP binding IEA:UniProtKB-HAMAP
  GO:0004176   F:ATP-dependent peptidase activity IEA:UniProtKB-HAMAP
  GO:0043565   F:sequence-specific DNA binding IEA:UniProtKB-HAMAP
  GO:0004252   F:serine-type endopeptidase activity IEA:UniProtKB-HAMAP
  GO:0033554   P:cellular response to stress IEA:UniProtKB-HAMAP
  GO:0006515   P:misfolded or incompletely synthesized protein catabolic process IEA:UniProtKB-HAMAP
  IPR003593   AAA+_ATPase.
  IPR003959   ATPase_AAA_core.
  IPR027543   Lon_bac.
  IPR004815   Lon_bac/euk-typ.
  IPR027065   Lon_Prtase.
  IPR027417   P-loop_NTPase.
  IPR008269   Pept_S16_C.
  IPR003111   Pept_S16_N.
  IPR008268   Peptidase_S16_AS.
  IPR015947   PUA-like_domain.
  IPR020568   Ribosomal_S5_D2-typ_fold.
  IPR014721   Ribosomal_S5_D2-typ_fold_subgr.
  PF00004   AAA.
  PF02190   LON.
  PF05362   Lon_C.
  SM00382   AAA.
  SM00464   LON.
  PS01046   LON_SER.