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Q54089

- RELA_STREQ

UniProt

Q54089 - RELA_STREQ

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Protein

Bifunctional (p)ppGpp synthase/hydrolase RelA

Gene
relA, rel
Organism
Streptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
Guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.

Cofactori

Binds 1 Mg2+ per subunit Reviewed prediction.1 Publication
Binds 1 Mn2+ per subunit.1 Publication

Enzyme regulationi

Alpha-beta methylenyl ATP, an ATP-analog inhibitor of the synthase activity also reduces the hydrolase activity about 4-fold.2 Publications

Kineticsi

  1. KM=2 mM for GTP1 Publication
  2. KM=5 mM for ATP

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Manganese
Metal bindingi77 – 771Manganese
Active sitei81 – 811Nucleophile, for hydrolase activity Reviewed prediction
Active sitei82 – 821Nucleophile, for hydrolase activity Reviewed prediction
Metal bindingi144 – 1441Manganese
Metal bindingi264 – 2641Magnesium Reviewed prediction

GO - Molecular functioni

  1. amino acid binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. GTP binding Source: UniProtKB-KW
  4. GTP diphosphokinase activity Source: UniProtKB-EC
  5. guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity Source: UniProtKB-EC
  6. kinase activity Source: UniProtKB-KW
  7. metal ion binding Source: UniProtKB-KW
  8. phosphoric diester hydrolase activity Source: InterPro

GO - Biological processi

  1. guanosine tetraphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, GTP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKQ54089.
UniPathwayiUPA00908; UER00884.
UPA00908; UER00886.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional (p)ppGpp synthase/hydrolase RelA
Including the following 2 domains:
GTP pyrophosphokinase (EC:2.7.6.5)
Alternative name(s):
(p)ppGpp synthase
ATP:GTP 3'-pyrophosphotransferase
Stringent response-like protein
ppGpp synthase I
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase (EC:3.1.7.2)
Alternative name(s):
Penta-phosphate guanosine-3'-pyrophosphohydrolase
Short name:
(ppGpp)ase
Gene namesi
Name:relA
Synonyms:rel
OrganismiStreptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis)
Taxonomic identifieri119602 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441R → Q: No hydrolase activity. 1 Publication
Mutagenesisi78 – 781D → A: No hydrolase activity. 1 Publication
Mutagenesisi81 – 811E → G: No hydrolase activity. 1 Publication
Mutagenesisi82 – 821D → V: No hydrolase activity. 1 Publication
Mutagenesisi151 – 1511T → A or P: No hydrolase activity. 1 Publication
Mutagenesisi264 – 2641D → G: No synthase activity. 1 Publication
Mutagenesisi323 – 3231E → Q: No synthase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 739739Bifunctional (p)ppGpp synthase/hydrolase RelAPRO_0000166565Add
BLAST

Structurei

Secondary structure

1
739
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911
Helixi22 – 3817
Turni39 – 413
Helixi52 – 6312
Helixi68 – 769
Helixi79 – 824
Helixi87 – 948
Helixi96 – 10813
Turni128 – 1303
Helixi135 – 15016
Helixi160 – 16910
Helixi171 – 1777
Helixi181 – 19515
Helixi197 – 20913
Helixi211 – 23020
Turni231 – 2333
Beta strandi237 – 2404
Helixi245 – 25511
Helixi256 – 2583
Helixi263 – 2653
Beta strandi267 – 2748
Helixi275 – 28814
Turni299 – 3013
Beta strandi311 – 3166
Beta strandi318 – 32811
Helixi329 – 3379
Helixi364 – 3707

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VJ7X-ray2.10A/B1-385[»]
ProteinModelPortaliQ54089.
SMRiQ54089. Positions 5-371.

Miscellaneous databases

EvolutionaryTraceiQ54089.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 149100HDAdd
BLAST
Domaini664 – 73976ACTAdd
BLAST

Domaini

Based on a random mutagenesis study of the catalytic fragment (residues 1-385), the (p)ppGpp phosphohydrolase domain seems to encompass approximately the first 225 residues, while the (p)ppGpp synthase domain seems to be found between residues 226 and 385.

Sequence similaritiesi

Belongs to the RelA/SpoT family.
Contains 1 ACT domain.
Contains 1 HD domain.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF01966. HD. 1 hit.
PF04607. RelA_SpoT. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
SM00954. RelA_SpoT. 1 hit.
[Graphical view]
SUPFAMiSSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00691. spoT_relA. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q54089-1 [UniParc]FASTAAdd to Basket

« Hide

MAKEINLTGE EVVALAAKYM NETDAAFVKK ALDYATAAHF YQVRKSGEPY    50
IVHPIQVAGI LADLHLDAVT VACGFLHDVV EDTDITLDNI EFDFGKDVRD 100
IVDGVTKLGK VEYKSHEEQL AENHRKMLMA MSKDIRVILV KLADRLHNMR 150
TLKHLRKDKQ ERISRETMEI YAPLAHRLGI SRIKWELEDL AFRYLNETEF 200
YKISHMMNEK RREREALVDD IVTKIKSYTT EQGLFGDVYG RPKHIYSIYR 250
KMRDKKKRFD QIFDLIAIRC VMETQSDVYA MVGYIHELWR PMPGRFKDYI 300
AAPKANGYQS IHTTVYGPKG PIEIQIRTKE MHQVAEYGVA AHWAYKKGVR 350
GKVNQAEQKV GMNWIKELVE LQDASNGDAV DFVDSVKEDI FSERIYVFTP 400
TGAVQELPKD SGPIDFAYAI HTQVGEKAIG AKVNGRMVPL TAKLKTGDVV 450
EIVTNPNSFG PSRDWIKLVK TNKARNKIRQ FFKNQDKELS VNKGRDMLVS 500
YFQEQGYVAN KYLDKKRIEA ILPKVSVKSE ESLYAAVGFG DISPVSVFNK 550
LTEKERREEE RAKAKAEAEE LVNGGEIKHE NKDVLKVRSE NGVIIQGASG 600
LLMRIAKCCN PVPGDPIEGY ITKGRGIAIH RADCNNIKSQ DGYQERLIEV 650
EWDLDNSSKD YQAEIDIYGL NRRGLLNDVL QILSNSTKSI STVNAQPTKD 700
MKFANIHVSF GIPNLTHLTT VVEKIKAVPD VYSVKRTNG 739
Length:739
Mass (Da):83,913
Last modified:November 1, 1997 - v1
Checksum:iE65CBEF99103D171
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X72832 Genomic DNA. Translation: CAA51353.1.
PIRiS39975.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X72832 Genomic DNA. Translation: CAA51353.1 .
PIRi S39975.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VJ7 X-ray 2.10 A/B 1-385 [» ]
ProteinModelPortali Q54089.
SMRi Q54089. Positions 5-371.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL1163118.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00908 ; UER00884 .
UPA00908 ; UER00886 .
SABIO-RK Q54089.

Miscellaneous databases

EvolutionaryTracei Q54089.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view ]
Pfami PF01842. ACT. 1 hit.
PF01966. HD. 1 hit.
PF04607. RelA_SpoT. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view ]
SMARTi SM00471. HDc. 1 hit.
SM00954. RelA_SpoT. 1 hit.
[Graphical view ]
SUPFAMi SSF81271. SSF81271. 1 hit.
TIGRFAMsi TIGR00691. spoT_relA. 1 hit.
PROSITEi PS51671. ACT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genetic organization of the streptokinase region of the Streptococcus equisimilis H46A chromosome."
    Mechold U., Steiner K., Vettermann S., Malke H.
    Mol. Gen. Genet. 241:129-140(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: H46A.
  2. "Intramolecular regulation of the opposing (p)ppGpp catalytic activities of Rel(Seq), the Rel/Spo enzyme from Streptococcus equisimilis."
    Mechold U., Murphy H., Brown L., Cashel M.
    J. Bacteriol. 184:2878-2888(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  3. "Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response."
    Hogg T., Mechold U., Malke H., Cashel M., Hilgenfeld R.
    Cell 117:57-68(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-385 BOUND TO GUANOSINE-NUCLEOTIDE DERIVATIVES, HYDROLASE AND SYNTHASE ACTIVITIES, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF ARG-44; ASP-78; GLU-81; ASP-82; THR-151; ASP-264 AND GLU-323.
    Strain: H46A.

Entry informationi

Entry nameiRELA_STREQ
AccessioniPrimary (citable) accession number: Q54089
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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