Bifunctional (p)ppGpp synthase/hydrolase RelA
Details
- Name
- Bifunctional (p)ppGpp synthase/hydrolase RelA
- Synonyms
- rel
- Gene Name
- relA
- Organism
- Streptococcus dysgalactiae subsp. equisimilis
- Amino acid sequence
>lcl|BSEQ0016525|Bifunctional (p)ppGpp synthase/hydrolase RelA MAKEINLTGEEVVALAAKYMNETDAAFVKKALDYATAAHFYQVRKSGEPYIVHPIQVAGI LADLHLDAVTVACGFLHDVVEDTDITLDNIEFDFGKDVRDIVDGVTKLGKVEYKSHEEQL AENHRKMLMAMSKDIRVILVKLADRLHNMRTLKHLRKDKQERISRETMEIYAPLAHRLGI SRIKWELEDLAFRYLNETEFYKISHMMNEKRREREALVDDIVTKIKSYTTEQGLFGDVYG RPKHIYSIYRKMRDKKKRFDQIFDLIAIRCVMETQSDVYAMVGYIHELWRPMPGRFKDYI AAPKANGYQSIHTTVYGPKGPIEIQIRTKEMHQVAEYGVAAHWAYKKGVRGKVNQAEQKV GMNWIKELVELQDASNGDAVDFVDSVKEDIFSERIYVFTPTGAVQELPKDSGPIDFAYAI HTQVGEKAIGAKVNGRMVPLTAKLKTGDVVEIVTNPNSFGPSRDWIKLVKTNKARNKIRQ FFKNQDKELSVNKGRDMLVSYFQEQGYVANKYLDKKRIEAILPKVSVKSEESLYAAVGFG DISPVSVFNKLTEKERREEERAKAKAEAEELVNGGEIKHENKDVLKVRSENGVIIQGASG LLMRIAKCCNPVPGDPIEGYITKGRGIAIHRADCNNIKSQDGYQERLIEVEWDLDNSSKD YQAEIDIYGLNRRGLLNDVLQILSNSTKSISTVNAQPTKDMKFANIHVSFGIPNLTHLTT VVEKIKAVPDVYSVKRTNG
- Number of residues
- 739
- Molecular Weight
- 83912.61
- Theoretical pI
- 8.8
- GO Classification
- Functionsamino acid binding / ATP binding / GTP binding / GTP diphosphokinase activity / guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity / kinase activity / metal ion bindingProcessesguanosine tetraphosphate biosynthetic process
- General Function
- Metal ion binding
- Specific Function
- In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the formation of pppGpp which is then hydrolyzed to form ppGpp, and the hydrolysis of ppGpp. The enzyme does not simultaneously display both synthase and hydrolase activities. In the structure of residues 1-385 there are 2 conformations seen, the hydrolase-OFF/synthase-ON and hydrolase-ON/synthase-OFF, suggesting there is ligand-induced signal transmission between the 2 active sites.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0003382|2220 bp TTAGCCATTGGTCCGCTTCACGCTATAAACATCTGGAACTGCCTTAATTTTTTCGACAAC AGTTGTCAGATGCGTCAGATTTGGAATGCCAAAGCTCACGTGAATATTCGCAAACTTCAT GTCCTTGGTTGGCTGGGCATTAACGGTGGAAATACTCTTGGTAGAATTAGACAAAATCTG GAGGACGTCATTGAGAAGGCCTCTACGATTGAGCCCATAAATATCAATTTCAGCTTGGTA ATCTTTGCTGGAGTTATCCAAATCCCATTCCACCTCGATGAGACGCTCTTGGTAGCCATC TTGACTCTTGATGTTATTACAATCCGCACGGTGGATGGCAATGCCTCGACCCTTGGTAAT ATAGCCTTCAATGGGATCCCCAGGTACAGGATTACAACATTTAGCAATCCGCATCAAGAG TCCTGAAGCCCCTTGGATAATAACCCCATTTTCACTGCGAACCTTGAGAACATCCTTGTT TTCGTGCTTGATTTCGCCACCGTTAACCAATTCTTCTGCTTCTGCCTTAGCCTTGGCTCT TTCCTCTTCACGGCGTTCTTTTTCAGTTAATTTATTAAAGACACTAACAGGACTAATGTC GCCAAAACCGACCGCTGCGTAGAGAGATTCTTCGCTCTTCACACTGACTTTTGGAAGAAT AGCTTCTATGCGTTTTTTATCAAGGTATTTATTGGCAACATAGCCCTGCTCTTGGAAATA AGAAACCAGCATGTCACGGCCTTTATTCACTGACAACTCTTTGTCTTGGTTTTTAAAGAA CTGACGAATCTTGTTGCGAGCTTTATTGGTTTTTACCAACTTAATCCAGTCACGGCTTGG CCCAAAAGAGTTAGGGTTGGTGACGATTTCCACCACATCTCCTGTTTTTAATTTGGCTGT TAGGGGAACCATACGGCCATTAACCTTGGCCCCTATCGCTTTTTCACCCACTTGCGTGTG GATGGCATAGGCAAAGTCAATTGGTCCCGAGTCCTTTGGCAATTCCTGCACAGCACCTGT CGGTGTAAAGACGTAAATACGTTCTGAGAAAATGTCTTCTTTGACCGAGTCCACAAAGTC CACTGCATCGCCATTTGACGCATCTTGTAACTCCACAAGCTCTTTGATCCAGTTCATGCC AACCTTTTGTTCGGCCTGATTAACCTTGCCGCGGACGCCTTTTTTATAAGCCCAGTGAGC AGCTACCCCGTACTCAGCCACTTGGTGCATTTCCTTGGTGCGGATTTGAATCTCAATCGG ACCTTTAGGGCCATACACGGTGGTATGAATAGACTGGTAACCATTAGCTTTAGGCGCGGC AATATAATCTTTGAAGCGGCCTGGCATTGGACGCCACAACTCGTGAATGTAACCGACCAT AGCATAAACATCGCTCTGCGTTTCCATGACACAACGGATAGCAATCAAATCAAAAATCTG ATCAAAGCGTTTTTTCTTGTCCCGCATTTTCCGATAAATGGAATAAATGTGTTTTGGTCG ACCATAAACATCACCAAACAAGCCTTGCTCAGTGGTATAAGACTTGATTTTGGTAACAAT ATCATCCACCAAAGCTTCACGCTCGCGACGTTTTTCATTCATCATATGGGAAATCTTATA AAACTCCGTTTCGTTCAGGTAACGGAAAGCCAGATCTTCTAATTCCCATTTGATACGACT AATCCCCAAGCGGTGCGCCAAGGGAGCATAAATTTCCATGGTTTCGCGCGAAATACGCTC TTGCTTATCCTTACGCAGATGCTTGAGGGTCCGCATATTATGTAAACGGTCCGCCAATTT CACCAAAATCACTCGAATGTCTTTGGACATGGCCATCAACATTTTACGGTGATTTTCAGC TAACTGTTCTTCGTGCGATTTGTACTCTACCTTACCTAACTTGGTTACCCCATCAACAAT ATCACGGACATCTTTGCCAAAATCAAATTCAATGTTATCTAGAGTAATATCAGTATCTTC TACCACGTCATGCAAAAAACCACAGGCAACCGTCACAGCATCCAAATGCAAATCTGCCAG AATCCCCGCCACTTGAATCGGATGCACAATGTAAGGCTCTCCTGACTTTCGCACTTGATA AAAATGAGCAGCCGTTGCATAATCCAAAGCTTTTTTCACAAAGGCCGCATCGGTCTCATT CATGTATTTGGCTGCTAAGGCAACAACTTCTTCTCCTGTTAAATTGATTTCTTTTGCCAT
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q54089 UniProtKB Entry Name RELA_STREQ GenBank Protein ID 407881 GenBank Gene ID X72832 - General References
- Mechold U, Steiner K, Vettermann S, Malke H: Genetic organization of the streptokinase region of the Streptococcus equisimilis H46A chromosome. Mol Gen Genet. 1993 Oct;241(1-2):129-40. [Article]
- Mechold U, Murphy H, Brown L, Cashel M: Intramolecular regulation of the opposing (p)ppGpp catalytic activities of Rel(Seq), the Rel/Spo enzyme from Streptococcus equisimilis. J Bacteriol. 2002 Jun;184(11):2878-88. [Article]
- Hogg T, Mechold U, Malke H, Cashel M, Hilgenfeld R: Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response [corrected]. Cell. 2004 Apr 2;117(1):57-68. [Article]