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
Functions
amino acid binding / ATP binding / GTP binding / GTP diphosphokinase activity / guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity / kinase activity / metal ion binding
Processes
guanosine 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
ResourceLink
UniProtKB IDQ54089
UniProtKB Entry NameRELA_STREQ
GenBank Protein ID407881
GenBank Gene IDX72832
General References
  1. 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. [PubMed:8232196]
  2. 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. [PubMed:12003927]
  3. 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. [PubMed:15066282]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02836Guanosine 5'-diphosphate 2':3'-cyclic monophosphateexperimentalunknownDetails
DB04315Guanosine-5'-DiphosphateexperimentalunknownDetails