Rhomboid protease GlpG

Details

Name
Rhomboid protease GlpG
Synonyms
  • 3.4.21.105
  • Intramembrane serine protease
Gene Name
glpG
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0007473|Rhomboid protease GlpG
MLMITSFANPRVAQAFVDYMATQGVILTIQQHNQSDVWLADESQAERVRAELARFLENPA
DPRYLAASWQAGHTGSGLHYRRYPFFAALRERAGPVTWVMMIACVVVFIAMQILGDQEVM
LWLAWPFDPTLKFEFWRYFTHALMHFSLMHILFNLLWWWYLGGAVEKRLGSGKLIVITLI
SALLSGYVQQKFSGPWFGGLSGVVYALMGYVWLRGERDPQSGIYLQRGLIIFALIWIVAG
WFDLFGMSMANGAHIAGLAVGLAMAFVDSLNARKRK
Number of residues
276
Molecular Weight
31306.455
Theoretical pI
9.48
GO Classification
Functions
endopeptidase activity / serine-type endopeptidase activity
Processes
protein processing / proteolysis
Components
integral component of plasma membrane / plasma membrane
General Function
Serine-type endopeptidase activity
Specific Function
Rhomboid-type serine protease that catalyzes intramembrane proteolysis.
Pfam Domain Function
Transmembrane Regions
94-114 142-162 169-189 192-212 223-245 250-272
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0017260|Rhomboid protease GlpG (glpG)
ATGTTGATGATTACCTCTTTTGCTAACCCCCGCGTGGCGCAGGCGTTTGTTGATTACATG
GCGACGCAGGGTGTTATCCTCACGATTCAACAACATAACCAAAGCGATGTCTGGCTGGCG
GATGAGTCCCAGGCCGAGCGCGTACGGGCGGAGCTGGCGCGTTTTCTCGAAAACCCGGCA
GATCCGCGTTATCTGGCGGCGAGCTGGCAGGCAGGCCATACCGGCAGTGGCCTGCATTAT
CGCCGTTATCCTTTCTTTGCCGCCTTGCGTGAACGCGCAGGTCCGGTAACCTGGGTGATG
ATGATCGCCTGCGTGGTGGTGTTTATTGCCATGCAAATTCTCGGCGATCAGGAAGTGATG
TTATGGCTGGCCTGGCCATTCGATCCAACACTGAAATTTGAGTTCTGGCGTTACTTCACC
CACGCGTTAATGCACTTCTCGCTGATGCATATCCTCTTTAACCTGCTCTGGTGGTGGTAT
CTCGGCGGTGCGGTGGAAAAACGCCTCGGTAGCGGTAAGCTAATTGTCATTACGCTTATC
AGCGCCCTGTTAAGCGGCTATGTGCAGCAAAAATTCAGCGGGCCGTGGTTTGGCGGGCTT
TCTGGCGTGGTGTATGCGCTGATGGGCTACGTCTGGCTACGTGGCGAACGCGATCCGCAA
AGTGGCATTTACCTGCAACGTGGGTTAATTATCTTTGCGCTGATCTGGATTGTCGCCGGA
TGGTTTGATTTGTTTGGGATGTCGATGGCGAACGGAGCACACATCGCCGGGTTAGCCGTG
GGTTTAGCGATGGCTTTTGTTGATTCGCTCAATGCGCGAAAACGAAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP09391
UniProtKB Entry NameGLPG_ECOLI
GenBank Protein ID146191
GenBank Gene IDM54940
General References
  1. Choi YL, Kawase S, Nishida T, Sakai H, Komano T, Kawamukai M, Utsumi R, Kohara Y, Akiyama K: Nucleotide sequence of the glpR gene encoding the repressor for the glycerol-3-phosphate regulon of Escherichia coli K12. Nucleic Acids Res. 1988 Aug 11;16(15):7732. [Article]
  2. Zeng G, Ye S, Larson TJ: Repressor for the sn-glycerol 3-phosphate regulon of Escherichia coli K-12: primary structure and identification of the DNA-binding domain. J Bacteriol. 1996 Dec;178(24):7080-9. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G 3rd, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL: Escherichia coli K-12: a cooperatively developed annotation snapshot--2005. Nucleic Acids Res. 2006 Jan 5;34(1):1-9. Print 2006. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Wu Z, Yan N, Feng L, Oberstein A, Yan H, Baker RP, Gu L, Jeffrey PD, Urban S, Shi Y: Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry. Nat Struct Mol Biol. 2006 Dec;13(12):1084-91. Epub 2006 Nov 10. [Article]
  7. Maegawa S, Ito K, Akiyama Y: Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane. Biochemistry. 2005 Oct 18;44(41):13543-52. [Article]
  8. Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G: Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005 May 27;308(5726):1321-3. [Article]
  9. Clemmer KM, Sturgill GM, Veenstra A, Rather PN: Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii. J Bacteriol. 2006 May;188(9):3415-9. [Article]
  10. Maegawa S, Koide K, Ito K, Akiyama Y: The intramembrane active site of GlpG, an E. coli rhomboid protease, is accessible to water and hydrolyses an extramembrane peptide bond of substrates. Mol Microbiol. 2007 Apr;64(2):435-47. [Article]
  11. Wang Y, Zhang Y, Ha Y: Crystal structure of a rhomboid family intramembrane protease. Nature. 2006 Nov 9;444(7116):179-80. Epub 2006 Oct 11. [Article]
  12. Ben-Shem A, Fass D, Bibi E: Structural basis for intramembrane proteolysis by rhomboid serine proteases. Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):462-6. Epub 2006 Dec 26. [Article]
  13. Wang Y, Ha Y: Open-cap conformation of intramembrane protease GlpG. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2098-102. Epub 2007 Feb 2. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02451B-nonylglucosideexperimentalunknownDetails
DB04147Dodecyldimethylamine N-oxideexperimentalunknownDetails