Bifunctional (p)ppGpp synthase/hydrolase SpoT (P0AG24)

Identification
Name:Bifunctional (p)ppGpp synthase/hydrolase SpoT
Synonyms:
  • GTP pyrophosphokinase
  • (p)ppGpp synthase
  • ATP:GTP 3'-pyrophosphotransferase
  • Stringent response-like protein
  • ppGpp synthase II
  • Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase
  • Penta-phosphate guanosine-3'-pyrophosphohydrolase
  • (ppGpp)ase
Gene Name:spoT
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
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 synthesis and degradation of ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c- di-GMP induces it
Cellular Location:Cytoplasm.
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Guanosine triphosphate ↔ 1.0Adenosine monophosphate + 1.0Guanosine 3'-diphosphate 5'-triphosphate + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.0Guanosine 3',5'-bis(diphosphate) ↔ 1.0Guanosine diphosphate + 1.0Pyrophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Guanosine diphosphate → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Guanosine 3',5'-bis(diphosphate)
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Guanosine triphosphate ↔ 1.0Adenosine monophosphate + 1.0Guanosine 3'-diphosphate 5'-triphosphate + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.0Guanosine 3',5'-bis(diphosphate) ↔ 1.0Guanosine diphosphate + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Guanosine 3'-diphosphate 5'-triphosphate + 1.0Water → 1.0Guanosine triphosphate + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Guanosine diphosphate → 1.0Adenosine monophosphate + 1.0Guanosine 3',5'-bis(diphosphate)
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine 3',5'-bis(diphosphate) + 1.0Water → 1.0Hydrogen ion + 1.0Pyrophosphate + 1.0Guanosine diphosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine 3'-diphosphate 5'-triphosphate + 1.0Water → 1.0Hydrogen ion + 1.0Guanosine triphosphate + 1.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Guanosine 3',5'-bis(diphosphate) + 1.0Water → 1.0Guanosine diphosphate + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB20158Guanosine 3',5'-bis(diphosphate)MetaboCard
ECMDB20156Guanosine 3'-diphosphate 5'-triphosphateMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
Process
cellular nitrogen compound metabolic process
guanosine metabolic process
guanosine tetraphosphate metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside metabolic process
purine ribonucleoside metabolic process
ribonucleoside metabolic process
Gene Properties
Blattner:b3650
Gene OrientationClockwise
Centisome Percentage:82.34
Left Sequence End3820423
Right Sequence End3822531
Gene Sequence:
>2109 bp
ATGAATTCTCTGTTTGCCAGTACGGCCCGTGGGCTGGAAGAGCTGTTAAAAACTGAACTG
GAAAACCTGGGGGCCGTTGAATGCCAGGTGGTTCAGGGTGGGGTCCATTTCAAGGGCGAC
ACACGGCTTGTTTACCAGAGCCTGATGTGGAGCCGCCTGGCCTCGCGTATTATGTTGCCG
CTGGGCGAGTGTAAGGTTTACAGCGATTTAGACCTCTATCTCGGTGTTCAGGCGATCAAC
TGGACAGAGATGTTTAATCCTGGCGCGACCTTCGCTGTCCACTTCAGTGGTTTGAATGAC
ACCATCCGCAACAGTCAGTACGGCGCGATGAAAGTGAAAGACGCGATCGTCGATGCTTTC
ACGCGGAAAAATCTGCCGCGTCCAAATGTTGATCGCGATGCGCCGGATATCCGCGTTAAC
GTCTGGCTGCATAAAGAAACCGCCAGTATCGCTCTTGATCTGAGTGGTGATGGTTTACAT
CTGCGTGGCTATCGCGATCGTGCTGGTATTGCGCCGATCAAAGAAACCCTGGCAGCCGCT
ATTGTGATGCGATCCGGCTGGCAGCCAGGAACACCGCTGCTCGATCCGATGTGTGGTTCC
GGTACGTTGCTGATTGAAGCAGCGATGCTGGCGACCGATCGCGCACCAGGCTTGCACCGT
GGGCGTTGGGGCTTTAGCGGCTGGGCGCAGCATGATGAAGCTATCTGGCAGGAAGTGAAA
GCGGAAGCGCAAACTCGCGCCCGTAAAGGCCTGGCTGAGTATAGCTCTCATTTTTACGGT
TCGGACAGCGACGCACGGGTGATTCAACGTGCACGCACTAACGCCCGTCTTGCGGGGATT
GGTGAACTGATCACCTTTGAGGTGAAAGATGTCGCGCAACTGACCAATCCGCTGCCGAAA
GGGCCGTACGGCACAGTGTTGAGCAACCCGCCATACGGGGAACGTCTGGACAGCGAACCG
GCGCTGATTGCGCTGCATAGCCTGCTGGGTCGGATCATGAAAAACCAGTTTGGTGGCTGG
AATCTCTCTTTGTTTAGTGCCTCGCCGGATCTGCTAAGCTGCTTGCAGCTGCGTGCAGAC
AAACAGTACAAGGCGAAAAACGGCCCGCTGGACTGCGTACAGAAAAATTACCACGTTGCC
GAAAGCACTCCAGACAGCAAACCGGCGATGGTAGCGGAAGACTACACCAACCGCCTGCGT
AAGAACCTCAAAAAATTCGAGAAGTGGGCTCGCCAGGAAGGGATTGAATGTTACCGCCTG
TATGACGCCGATCTGCCAGAATATAACGTTGCCGTTGACCGTTATGCCGACTGGGTGGTG
GTGCAGGAGTATGCGCCGCCAAAAACTATTGATGCTCACAAAGCGCGTCAGCGTCTGTTC
GATATTATCGCTGCAACCATTTCGGTACTGGGGATTGCGCCAAACAAACTGGTGCTGAAA
ACCCGTGAACGCCAGAAGGGCAAAAACCAATACCAGAAACTGGGCGAGAAGGGCGAGTTT
CTTGAAGTTACCGAATATAACGCTCACTTGTGGGTGAACCTGACGGATTATCTCGATACT
GGTCTGTTCCTCGATCACCGCATCGCCCGTCGTATGCTCGGTCAGATGAGCAAAGGCAAA
GATTTCCTCAACCTGTTCTCTTATACCGGCAGCGCCACCGTGCATGCGGGATTAGGCGGT
GCACGCAGCACCACCACCGTGGATATGTCGCGTACTTATCTGGAATGGGCAGAACGCAAC
CTGCGTCTGAATGGCCTGACCGGGCGTGCGCATCGCCTGATTCAGGCCGATTGCCTGGCG
TGGCTGCGTGAGGCAAATGAACAGTTCGATCTGATCTTTATCGATCCGCCAACCTTCTCT
AACTCAAAACGAATGGAAGATGCGTTTGATGTTCAGCGCGATCATCTGGCGCTGATGAAA
GATTTGAAACGTCTGCTGCGTGCAGGTGGGACGATCATGTTCTCGAACAACAAACGTGGC
TTCCGTATGGATCTCGACGGCCTGGCAAAACTGGGACTGAAAGCACAAGAAATTACGCAA
AAAACGCTCTCCCAGGATTTCGCCCGTAACCGCCAGATCCACAACTGCTGGCTGATTACC
GCAGCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:702
Protein Molecular Weight:79342
Protein Theoretical pI:9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Bifunctional (p)ppGpp synthase/hydrolase SpoT
MYLFESLNQLIQTYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMK
LDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKFRDKKEAQAENFR
KMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKT
ELEELGFEALYPNRYRVIKEVVKAARGNRKEMIQKILSEIEGRLQEAGIPCRVSGREKHL
YSIYCKMVLKEQRFHSIMDIYAFRVIVNDSDTCYRVLGQMHSLYKPRPGRVKDYIAIPKA
NGYQSLHTSMIGPHGVPVEVQIRTEDMDQMAEMGVAAHWAYKEHGETSTTAQIRAQRWMQ
SLLELQQSAGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGHA
CVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAAWLNFVVSSKARAKIRQLLKNLKRD
DSVSLGRRLLNHALGGSRKLNEIPQENIQRELDRMKLATLDDLLAEIGLGNAMSVVVAKN
LQHGDASIPPATQSHGHLPIKGADGVLITFAKCCRPIPGDPIIAHVSPGKGLVIHHESCR
NIRGYQKEPEKFMAVEWDKETAQEFITEIKVEMFNHQGALANLTAAINTTTSNIQSLNTE
EKDGRVYSAFIRLTARDRVHLANIMRKIRVMPDVIKVTRNRN
References
External Links:
ResourceLink
Uniprot ID:P0AG24
Uniprot Name:SPOT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062515
Ecogene ID:EG10966
Ecocyc:EG10966
ColiBase:b3650
Kegg Gene:b3650
EchoBASE ID:EB0959
CCDB:SPOT_ECOLI
BacMap:16131521
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Boehm, A., Steiner, S., Zaehringer, F., Casanova, A., Hamburger, F., Ritz, D., Keck, W., Ackermann, M., Schirmer, T., Jenal, U. (2009). "Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress." Mol Microbiol 72:1500-1516. Pubmed: 19460094
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Fujita, C., Maeda, M., Fujii, T., Iwamoto, R., Ikehara, K. (2002). "Identification of an indispensable amino acid for ppGpp synthesis of Escherichia coli SpoT protein." Biosci Biotechnol Biochem 66:2735-2738. Pubmed: 12596879
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jiang, M., Sullivan, S. M., Wout, P. K., Maddock, J. R. (2007). "G-protein control of the ribosome-associated stress response protein SpoT." J Bacteriol 189:6140-6147. Pubmed: 17616600
  • Sarubbi, E., Rudd, K. E., Xiao, H., Ikehara, K., Kalman, M., Cashel, M. (1989). "Characterization of the spoT gene of Escherichia coli." J Biol Chem 264:15074-15082. Pubmed: 2549050
  • Wout, P., Pu, K., Sullivan, S. M., Reese, V., Zhou, S., Lin, B., Maddock, J. R. (2004). "The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase." J Bacteriol 186:5249-5257. Pubmed: 15292126
  • Xiao, H., Kalman, M., Ikehara, K., Zemel, S., Glaser, G., Cashel, M. (1991). "Residual guanosine 3',5'-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations." J Biol Chem 266:5980-5990. Pubmed: 2005134