Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GTP pyrophosphokinase rsh

Gene

rsh

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

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. kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. guanosine tetraphosphate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBMEL224914:GCJ0-1336-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP pyrophosphokinase rsh (EC:2.7.6.5)
Alternative name(s):
(p)ppGpp synthase
ATP:GTP 3'-pyrophosphotransferase
Gene namesi
Name:rsh
Ordered Locus Names:BMEI1296
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000419: Chromosome I

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 750750GTP pyrophosphokinase rshPRO_0000322561Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224914.BMEI1296.

Structurei

3D structure databases

ProteinModelPortaliQ8YG65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 144100HDAdd
BLAST
Domaini676 – 75075ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000018299.
KOiK01139.
OrthoDBiEOG6SV551.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR003607. HD/PDEase_dom.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamiPF04607. 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.

Q8YG65-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMRQYELVER VQRYKPDVNE ALLNKAYVYA MQKHRSQKRA SGDPYFSHPL
60 70 80 90 100
EVAAILTDMH LDEATIAIAL LHDTIEDTTA TRQEIDQLFG PEIGKLVEGL
110 120 130 140 150
TKLKKLDLVS KKAVQAENLR KLLLAISEDV RVLLVKLADR LHNMRTLGVM
160 170 180 190 200
REDKRLRIAE ETMDIYAPLA GRMGMQDMRE ELEELAFRYI NPDAWRAVTD
210 220 230 240 250
RLAELLEKNR GLLQKIETDL SEIFEKNGIK ASVKSRQKKP WSVFRKMESK
260 270 280 290 300
GLSFEQLSDI FGFRVMVDTV QDCYRALGLI HTTWSMVPGR FKDYISTPKQ
310 320 330 340 350
NDYRSIHTTI IGPSRQRIEL QIRTREMDEI AEFGVAAHSI YKDRGSANNP
360 370 380 390 400
HKISTETNAY AWLRQTIEQL SEGDNPEEFL EHTKLELFQD QVFCFTPKGR
410 420 430 440 450
LIALPRGATP IDFAYAVHTD IGDSCVGAKV NGRIMPLMTE LKNGDEVDII
460 470 480 490 500
RSKAQVPPAA WESLVATGKA RAAIRRATRS AVRKQYSGLG MRILERAFER
510 520 530 540 550
AGKPFSKDIL KPGLPRLARK DVEDVLAAVG RGELPSTDVV KAVYPDYQDT
560 570 580 590 600
RVTTQNNPAK AGEKGWFNIQ NAAGMIFKVP EGGEGAAAKV DPAATTPKPG
610 620 630 640 650
KRALPIRGTN PDLPVRFAPE GAVPGDRIVG ILQPGAGITI YPIQSPALTA
660 670 680 690 700
YDDQPERWID VRWDIDDQMS ERFPARISVS AINSPGSLAE IAQIAAANDA
710 720 730 740 750
NIHNLSMVRT APDFTEMIID VEVWDLKHLN RIISQLKESA SVSSAKRVNG
Length:750
Mass (Da):83,999
Last modified:February 26, 2008 - v2
Checksum:i1BF6850C0FA147C7
GO

Sequence cautioni

The sequence AAL52477.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52477.1. Different initiation.
PIRiAB3414.
RefSeqiNP_540213.1. NC_003317.1.

Genome annotation databases

EnsemblBacteriaiAAL52477; AAL52477; BMEI1296.
GeneIDi1197007.
KEGGibme:BMEI1296.
PATRICi17852919. VBIBruMel92729_1451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52477.1. Different initiation.
PIRiAB3414.
RefSeqiNP_540213.1. NC_003317.1.

3D structure databases

ProteinModelPortaliQ8YG65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224914.BMEI1296.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL52477; AAL52477; BMEI1296.
GeneIDi1197007.
KEGGibme:BMEI1296.
PATRICi17852919. VBIBruMel92729_1451.

Phylogenomic databases

HOGENOMiHOG000018299.
KOiK01139.
OrthoDBiEOG6SV551.

Enzyme and pathway databases

BioCyciBMEL224914:GCJ0-1336-MONOMER.

Miscellaneous databases

PROiQ8YG65.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR003607. HD/PDEase_dom.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamiPF04607. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiRSH_BRUME
AccessioniPrimary (citable) accession number: Q8YG65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: January 7, 2015
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  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.