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Protein

GTP pyrophosphokinase

Gene

relA

Organism
Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 / CCUG 15956))
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 the formation of pppGpp which is then hydrolyzed to form ppGpp. Plays also a role in the reductive division that occurs during the initial phase of nutrient starvation.

Catalytic activityi

ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.

Pathway: ppGpp biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes ppGpp from GTP.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. GTP pyrophosphokinase (relA), Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase (gppA)
  2. no protein annotated in this organism
This subpathway is part of the pathway ppGpp biosynthesis, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes ppGpp from GTP, the pathway ppGpp biosynthesis and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00908; UER00884.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP pyrophosphokinase (EC:2.7.6.5)
Alternative name(s):
(p)ppGpp synthase
ATP:GTP 3'-pyrophosphotransferase
ppGpp synthase I
Gene namesi
Name:relA
OrganismiPhotobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 / CCUG 15956))
Taxonomic identifieri314292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Pathology & Biotechi

Disruption phenotypei

Mutants remain rod shaped, and do not acquire the typical coccoid morphology usually seen during starvation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 744744GTP pyrophosphokinasePRO_0000166566Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi314292.VAS14_20411.

Structurei

3D structure databases

ProteinModelPortaliP55133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini669 – 74476ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RelA/SpoT family.Curated
Contains 1 ACT domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF04607. RelA_SpoT. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
SMARTiSM00954. 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.

P55133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAVRGAHLK ENTTFELVSW VESLRQDAKV SSRIEGTYQR CIELAAEQEN
60 70 80 90 100
GPLLLWRGRE LVEILVTLSM DADTLIAALL YPLVEGGCYS TDALKEEYSG
110 120 130 140 150
TILHLVQGVE QMCAISQLKS TAEETAQAAQ VDNIRRMLLS MVDDFRCVVI
160 170 180 190 200
KLAERICNLR EVKDQPDEVR RAAAQECANI YAPLANRLGI GQLKWEIEDY
210 220 230 240 250
AFRYQHPDTY KQIAKQLSER RIDREDYITH FVDDLSDAMK ASNIRAEVQG
260 270 280 290 300
RPKHIYSIWR KMQKKSLEFD ELFDVRAVRI VAEELQDCYA ALGVVHTKYR
310 320 330 340 350
HLPKEFDDYV ANPKPNGYQS IHTVVLGPEG KTIEIQIRTK QMHEESELGV
360 370 380 390 400
AAHWKYKEGT ASGGAQSAYD EKINWLRKLL AWQEEMSDSG EMLDELRSQV
410 420 430 440 450
FDDRVYAFTP KGDVVDLPSN ATPLDFAYHI HSEVGHRCIG AKVEGRIVPF
460 470 480 490 500
TYHLQMGDQV EIITQKEPNP SRDWLNPNLG FVTSSRARAK VHAWFRKQDR
510 520 530 540 550
DKNIIAGKEI LEAELVKIHA TLKDAQYYAA KRFNVKSPEE LYAGIGSGDL
560 570 580 590 600
RINQVINHIN ALVNKPTAEE EDQQLLEKLS EASNKQATSH KKPQRDAVVV
610 620 630 640 650
EGVDNLMTHL ARCCQPIPGD DIQGFVTQGR GISVHRMDCE QLEELRHHAP
660 670 680 690 700
ERIIDTVWGG GFVGNYTITV RVTASERNGL LKELTNTLMN EKVKVAGMKS
710 720 730 740
RVDYKKQMSI MDFELELTDL EVLGRVLKRI EQVKDVAEAK RLYG
Length:744
Mass (Da):84,546
Last modified:October 1, 1996 - v1
Checksum:iB7AC772C4D47A40C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13769 Genomic DNA. Translation: AAA62208.1.
RefSeqiWP_005371455.1. NZ_CH902602.1.

Genome annotation databases

PATRICi31352187. VBIPhoAng36222_3707.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13769 Genomic DNA. Translation: AAA62208.1.
RefSeqiWP_005371455.1. NZ_CH902602.1.

3D structure databases

ProteinModelPortaliP55133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi314292.VAS14_20411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICi31352187. VBIPhoAng36222_3707.

Enzyme and pathway databases

UniPathwayiUPA00908; UER00884.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF04607. RelA_SpoT. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
SMARTiSM00954. RelA_SpoT. 1 hit.
[Graphical view]
SUPFAMiSSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00691. spoT_relA. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Stringent control during carbon starvation of marine Vibrio sp. strain S14: molecular cloning, nucleotide sequence, and deletion of the relA gene."
    Flaerdh K., Axberg T., Albertson N.H., Kjelleberg S.
    J. Bacteriol. 176:5949-5957(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiRELA_PHOAS
AccessioniPrimary (citable) accession number: P55133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.