| Tag | Content |
|---|
| CPLM ID | CPLM-003581 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional (p)ppGpp synthase/hydrolase SpoT |
Protein Synonyms/Alias | 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 |
Gene Synonyms/Alias | b3650; JW3625 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 102 | ELVEGVSKLDKLKFR | acetylation | [1] | | 136 | DIRVILIKLADRTHN | acetylation | [1] | | 154 | LGSLRPDKRRRIARE | acetylation | [1] | | 179 | RLGIHHIKTELEELG | acetylation | [1] | | 215 | NRKEMIQKILSEIEG | acetylation | [1, 2] | | 285 | GQMHSLYKPRPGRVK | acetylation | [1] | | 611 | GYQKEPEKFMAVEWD | acetylation | [1] | | 662 | QSLNTEEKDGRVYSA | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 45 144 HD.
DOMAIN 628 702 ACT. |
Keyword | Complete proteome; Cytoplasm; Hydrolase; Kinase; Manganese; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 702 AA |
Protein Sequence | MYLFESLNQL IQTYLPEDQI KRLRQAYLVA RDAHEGQTRS SGEPYITHPV AVACILAEMK 60
LDYETLMAAL LHDVIEDTPA TYQDMEQLFG KSVAELVEGV SKLDKLKFRD KKEAQAENFR 120
KMIMAMVQDI RVILIKLADR THNMRTLGSL RPDKRRRIAR ETLEIYSPLA HRLGIHHIKT 180
ELEELGFEAL YPNRYRVIKE VVKAARGNRK EMIQKILSEI EGRLQEAGIP CRVSGREKHL 240
YSIYCKMVLK EQRFHSIMDI YAFRVIVNDS DTCYRVLGQM HSLYKPRPGR VKDYIAIPKA 300
NGYQSLHTSM IGPHGVPVEV QIRTEDMDQM AEMGVAAHWA YKEHGETSTT AQIRAQRWMQ 360
SLLELQQSAG SSFEFIESVK SDLFPDEIYV FTPEGRIVEL PAGATPVDFA YAVHTDIGHA 420
CVGARVDRQP YPLSQPLTSG QTVEIITAPG ARPNAAWLNF VVSSKARAKI RQLLKNLKRD 480
DSVSLGRRLL NHALGGSRKL NEIPQENIQR ELDRMKLATL DDLLAEIGLG NAMSVVVAKN 540
LQHGDASIPP ATQSHGHLPI KGADGVLITF AKCCRPIPGD PIIAHVSPGK GLVIHHESCR 600
NIRGYQKEPE KFMAVEWDKE TAQEFITEIK VEMFNHQGAL ANLTAAINTT TSNIQSLNTE 660
EKDGRVYSAF IRLTARDRVH LANIMRKIRV MPDVIKVTRN RN 702 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0008728; F:GTP diphosphokinase activity; IEA:EC. GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IDA:EcoCyc. GO:0016301; F:kinase activity; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:InterPro. GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro. GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway. GO:0015949; P:nucleobase-containing small molecule interconversion; IMP:EcoCyc. |
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