SubmitCancel

Skip Header

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

Q57E90

- RSH_BRUAB

UniProt

Q57E90 - RSH_BRUAB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

GTP pyrophosphokinase rsh

Gene
rsh, spoT, BruAb1_0669
Organism
Brucella abortus biovar 1 (strain 9-941)
Status
Reviewed - Annotation score: 4 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. 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

BioCyciBABO262698:GJC2-676-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
Synonyms:spoT
Ordered Locus Names:BruAb1_0669
OrganismiBrucella abortus biovar 1 (strain 9-941)
Taxonomic identifieri262698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000540: Chromosome I

Pathology & Biotechi

Disruption phenotypei

Cells show morphological abnormalities such as branching and swelling forms. It does not grow in RPMI-1640 with or without 10% FBS. It shows decreased growth until 48 hours in RPMI-1640 and stationary growth until 48 hours in RPMI-1640 with 10% FBS. It has the same ability as the wild-type to internalize at 0 minute but a lower rate of internalization at 30 minutes. It shows a lower rate of intracellular replication within macrophages than the wild-type. Its adherence is four times higher than that of the wild-type. It shows lower MICs than the wild-type for several antimicrobial agents such as penicillin G, methicillin, erythromycin and doxycycline. At ten days post infection the number of viable bacteria (disruption mutant) is markedly reduced compared to the wild-type.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 750750GTP pyrophosphokinase rshPRO_0000322563Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi262698.BruAb1_0669.

Structurei

3D structure databases

ProteinModelPortaliQ57E90.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 144100HDAdd
BLAST
Domaini676 – 75075ACTAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0317.
HOGENOMiHOG000018299.
KOiK01139.
OMAiESNAYSW.
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.

Q57E90-1 [UniParc]FASTAAdd to Basket

« Hide

MMRQYELVER VQRYKPDVNE ALLNKAYVYA MQKHGSQKRA SGDPYFSHPL    50
EVAAILTDMH LDEATIAIAL LHDTIEDTTA TRQEIDQLFG PEIGKLVEGL 100
TKLKKLDLVS KKAVQAENLR KLLLAISEDV RVLLVKLADR LHNMRTLGVM 150
REDKRLRIAE ETMDIYAPLA GRMGMQDMRE ELEELAFRYI NPDAWRAVTD 200
RLAELLEKNR GLLQKIETDL SEIFEKNGIK ASVKSRQKKP WSVFRKMETK 250
GLSFEQLSDI FGFRVMVDTV QDCYRALGLI HTTWSMVPGR FKDYISTPKQ 300
NDYRSIHTTI IGPSRQRIEL QIRTREMDEI AEFGVAAHSI YKDRGSANNP 350
HKISTETNAY AWLRQTIEQL SEGDNPEEFL EHTKLELFQD QVFCFTPKGR 400
LIALPRGATP IDFAYAVHTD IGDSCVGAKV NGRIMPLMTE LKNGDEVDII 450
RSKAQVPPAA WESLVATGKA RAAIRRATRS AVRKQYSGLG MRILERAFER 500
AGKPFSKDIL KPGLPRLARK DVEDVLAAVG RGELPSADVV KAVYPDYQDT 550
RVTTQNNPAK AGEKGWFNIQ NAAGMIFKVP EGGEGAAAKV DPAATTPKPG 600
KRALPIRGTN PDLPVRFAPE GAVPGDRIVG ILQPGAGITI YPIQSPALTA 650
YDDQPERWID VRWDIDDQMS ERFPARISVS AINSPGSLAE IAQIAAANDA 700
NIHNLSMART APDFTEMIID VEVWDLKHLN RIISQLKESA SVSSAKRVNG 750
Length:750
Mass (Da):83,856
Last modified:May 10, 2005 - v1
Checksum:i4836EEECB0E52495
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017223 Genomic DNA. Translation: AAX74044.1.
RefSeqiYP_221405.1. NC_006932.1.

Genome annotation databases

EnsemblBacteriaiAAX74044; AAX74044; BruAb1_0669.
GeneIDi3339865.
KEGGibmb:BruAb1_0669.
PATRICi17822939. VBIBruAbo15061_0705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017223 Genomic DNA. Translation: AAX74044.1 .
RefSeqi YP_221405.1. NC_006932.1.

3D structure databases

ProteinModelPortali Q57E90.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262698.BruAb1_0669.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAX74044 ; AAX74044 ; BruAb1_0669 .
GeneIDi 3339865.
KEGGi bmb:BruAb1_0669.
PATRICi 17822939. VBIBruAbo15061_0705.

Phylogenomic databases

eggNOGi COG0317.
HOGENOMi HOG000018299.
KOi K01139.
OMAi ESNAYSW.
OrthoDBi EOG6SV551.

Enzyme and pathway databases

BioCyci BABO262698:GJC2-676-MONOMER.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR003607. HD/PDEase_dom.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view ]
Pfami 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

« Hide 'large scale' publications
  1. "Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
    Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
    J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 9-941.
  2. "Roles of Brucella abortus SpoT in morphological differentiation and intramacrophagic replication."
    Kim S., Watanabe K., Suzuki H., Watarai M.
    Microbiology 151:1607-1617(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADAPTATION TO INTRACELLULAR REPLICATION, DISRUPTION PHENOTYPE.
    Strain: 544 / Biovar 1.

Entry informationi

Entry nameiRSH_BRUAB
AccessioniPrimary (citable) accession number: Q57E90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 10, 2005
Last modified: June 11, 2014
This is version 71 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

Complete proteome

Documents

  1. Brucella abortus strain 9-941
    Brucella abortus (strain 9-941): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi