Rhomboid protease GlpG
Details
- Name
- Rhomboid protease GlpG
- Synonyms
- 3.4.21.105
- Intramembrane serine protease
- Gene Name
- glpG
- Organism
- Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
- Amino acid sequence
>lcl|BSEQ0012990|Rhomboid protease GlpG MKNFLAQQGKITLILTALCVLIYLAQQLGFEDDIMYLMHYPAYEEQDSEVWRYISHTLVH LSNLHILFNLSWFFIFGGMIERTFGSVKLLMLYVVASAITGYVQNYVSGPAFFGLSGVVY AVLGYVFIRDKLNHHLFDLPEGFFTMLLVGIALGFISPLFGVEMGNAAHISGLIVGLIWG FIDSKLRKNSLE
- Number of residues
- 192
- Molecular Weight
- 21657.295
- Theoretical pI
- 6.39
- GO Classification
- Functionsidentical protein binding / serine-type endopeptidase activityComponentsintegral component of membrane / plasma membrane
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Rhomboid-type serine protease that catalyzes intramembrane proteolysis.
- Pfam Domain Function
- Rhomboid (PF01694)
- Transmembrane Regions
- 11-31 58-78 83-103 108-128 142-162 164-184
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0012991|Rhomboid protease GlpG (glpG) ATGAAAAACTTTTTAGCTCAACAAGGAAAAATCACGCTAATTCTCACCGCACTTTGTGTG CTTATTTATCTTGCTCAACAGCTGGGTTTTGAAGACGATATTATGTATTTGATGCATTAC CCCGCTTACGAAGAGCAAGATAGTGAAGTGTGGCGTTATATCTCACATACATTGGTACAT TTATCTAATTTGCATATTTTGTTTAATCTGTCTTGGTTTTTTATTTTCGGTGGAATGATT GAGCGCACTTTTGGCTCGGTTAAATTATTGATGTTGTATGTTGTAGCATCTGCCATAACA GGATATGTGCAAAATTATGTGTCTGGCCCCGCTTTCTTTGGGCTTTCTGGTGTTGTATAT GCGGTTCTAGGTTATGTATTTATACGTGATAAATTGAATCATCATTTATTTGATCTGCCA GAAGGTTTTTTTACAATGTTATTGGTGGGGATCGCATTAGGTTTTATTAGCCCCTTATTT GGTGTTGAAATGGGAAATGCTGCACATATTTCAGGCTTGATTGTCGGCTTGATTTGGGGA TTTATTGATAGCAAATTGCGCAAAAATTCGCTAGAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P44783 UniProtKB Entry Name GLPG_HAEIN GenBank Protein ID 3212176 GenBank Gene ID L42023 - General References
- Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb JF, Dougherty BA, Merrick JM, et al.: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 1995 Jul 28;269(5223):496-512. [Article]
- Lemieux MJ, Fischer SJ, Cherney MM, Bateman KS, James MN: The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis. Proc Natl Acad Sci U S A. 2007 Jan 16;104(3):750-4. Epub 2007 Jan 8. [Article]