Q8YG65 (RSH_BRUME) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 82.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: GTP pyrophosphokinase rsh EC=2.7.6.5 Alternative name(s): (p)ppGpp synthase ATP:GTP 3'-pyrophosphotransferase | ||||
| Gene names |
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| Organism | Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 224914 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › ![]() |
Protein attributes
| Sequence length | 750 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Functions as a (p)ppGpp synthase. 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. It is necessary for persistence in mice, essential for intracellular growth of Brucella and required for expression of the type IV secretion system VirB and therefore plays a role in adaptation of Brucella to its intracellular host environment. Ref.2 |
| Catalytic activity | ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. |
| Disruption phenotype | Cells show morphological abnormalities such as branching and swelling forms during vegetative growth. It is unable to persist during stationary phase, presumably because of nutrient limitation occurring during this growth phase. It shows an important growth defect in human HeLa cells and in ovine macrophages MOCL3. At four weeks post infection the number of viable bacteria (deletion mutant) in mouse spleen is markedly reduced compared to the wild-type. The deletion mutant shows very low levels or absence of VirB at all time points of growth. Ref.2 |
| Sequence similarities | Belongs to the RelA/SpoT family. Contains 1 ACT domain. Contains 1 HD domain. |
| Sequence caution | The sequence AAL52477.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding GTP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | guanosine tetraphosphate metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP bindingInferred from electronic annotation. Source: UniProtKB-KW GTP diphosphokinase activityInferred from electronic annotation. Source: EC kinase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. Overbeek R.Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094. |
| [2] | "The stringent response mediator Rsh is required for Brucella melitensis and Brucella suis virulence, and for expression of the type IV secretion system virB." Dozot M., Boigegrain R.-A., Delrue R.-M., Hallez R., Ouahrani-Bettache S., Danese I., Letesson J.-J., De Bolle X., Koehler S. Cell. Microbiol. 8:1791-1802(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN STRINGENT RESPONSE, DISRUPTION PHENOTYPE. Strain: 16M / ATCC 23456 / NCTC 10094. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE008917 Genomic DNA. Translation: AAL52477.1. Different initiation. |
| PIR | AB3414. |
| RefSeq | NP_540213.1. NC_003317.1. |
3D structure databases | |
| ProteinModelPortal | Q8YG65. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224914.BMEI1296. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAL52477; AAL52477; BMEI1296. |
| GeneID | 1197007. |
| KEGG | bme:BMEI1296. |
| PATRIC | 17852919. VBIBruMel92729_1451. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000018299. |
| KO | K01139. |
| ProtClustDB | CLSK2754108. |
Enzyme and pathway databases | |
| BioCyc | BMEL224914:GCJ0-1336-MONOMER. |
Family and domain databases | |
| Gene3D | 3.10.20.30. 1 hit. |
| InterPro | IPR026020. (p)ppGpp_Synthase. IPR012675. Beta-grasp_dom. IPR003607. HD/PDEase_dom. IPR004811. RelA/Spo_fam. IPR007685. RelA_SpoT. IPR004095. TGS. IPR012676. TGS-like. [Graphical view] |
| PANTHER | PTHR21262. PTHR21262. 1 hit. |
| Pfam | PF04607. RelA_SpoT. 1 hit. PF02824. TGS. 1 hit. [Graphical view] |
| SMART | SM00471. HDc. 1 hit. SM00954. RelA_SpoT. 1 hit. [Graphical view] |
| SUPFAM | SSF81271. TGS-like. 1 hit. |
| TIGRFAMs | TIGR00691. spoT_relA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RSH_BRUME | ||||||||
| Accession | Primary (citable) accession number: Q8YG65 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella melitensis Brucella melitensis (strain 16M): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
