UniProtKB - Q8YG65 (RSH_BRUME)
Protein
GTP pyrophosphokinase rsh
Gene
rsh
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
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
- EC:2.7.6.5
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- GTP binding Source: UniProtKB-KW
- GTP diphosphokinase activity Source: UniProtKB-EC
- kinase activity Source: UniProtKB-KW
GO - Biological processi
- guanosine tetraphosphate metabolic process Source: InterPro
Keywordsi
Molecular function | Kinase, Transferase |
Ligand | ATP-binding, GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | BMEL224914:G1FZL-1404-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 |
Organismi | Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) |
Taxonomic identifieri | 224914 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › |
Proteomesi |
|
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000322561 | 1 – 750 | GTP pyrophosphokinase rshAdd BLAST | 750 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 45 – 144 | HDPROSITE-ProRule annotationAdd BLAST | 100 | |
Domaini | 390 – 451 | TGSPROSITE-ProRule annotationAdd BLAST | 62 | |
Domaini | 676 – 750 | ACTPROSITE-ProRule annotationAdd BLAST | 75 |
Sequence similaritiesi
Belongs to the RelA/SpoT family.Curated
Phylogenomic databases
eggNOGi | COG0317, Bacteria |
Family and domain databases
CDDi | cd00077, HDc, 1 hit cd05399, NT_Rel-Spo_like, 1 hit cd01668, TGS_RSH, 1 hit |
Gene3Di | 3.10.20.30, 1 hit 3.30.460.10, 1 hit |
InterProi | View protein in InterPro IPR002912, ACT_dom IPR012675, Beta-grasp_dom_sf IPR003607, HD/PDEase_dom IPR043519, NT_sf IPR004811, RelA/Spo_fam IPR007685, RelA_SpoT IPR004095, TGS IPR012676, TGS-like IPR033655, TGS_RelA |
Pfami | View protein in Pfam PF13291, ACT_4, 1 hit PF04607, RelA_SpoT, 1 hit PF02824, TGS, 1 hit |
SMARTi | View protein in SMART SM00471, HDc, 1 hit SM00954, RelA_SpoT, 1 hit |
SUPFAMi | SSF81271, SSF81271, 1 hit SSF81301, SSF81301, 1 hit |
TIGRFAMsi | TIGR00691, spoT_relA, 1 hit |
PROSITEi | View protein in PROSITE PS51671, ACT, 1 hit PS51831, HD, 1 hit PS51880, TGS, 1 hit |
i Sequence
Sequence statusi: Complete.
Q8YG65-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence AAL52477 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. |
PIRi | AB3414 |
RefSeqi | WP_004683389.1, NZ_GG703778.1 |
Genome annotation databases
EnsemblBacteriai | AAL52477; AAL52477; BMEI1296 |
GeneIDi | 29594139 |
KEGGi | bme:BMEI1296 bmel:DK63_109 |
PATRICi | fig|224914.52.peg.114 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE008917 Genomic DNA Translation: AAL52477.1 Different initiation. |
PIRi | AB3414 |
RefSeqi | WP_004683389.1, NZ_GG703778.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
STRINGi | 224914.BMEI1296 |
Genome annotation databases
EnsemblBacteriai | AAL52477; AAL52477; BMEI1296 |
GeneIDi | 29594139 |
KEGGi | bme:BMEI1296 bmel:DK63_109 |
PATRICi | fig|224914.52.peg.114 |
Phylogenomic databases
eggNOGi | COG0317, Bacteria |
Enzyme and pathway databases
BioCyci | BMEL224914:G1FZL-1404-MONOMER |
Miscellaneous databases
PROi | PR:Q8YG65 |
Family and domain databases
CDDi | cd00077, HDc, 1 hit cd05399, NT_Rel-Spo_like, 1 hit cd01668, TGS_RSH, 1 hit |
Gene3Di | 3.10.20.30, 1 hit 3.30.460.10, 1 hit |
InterProi | View protein in InterPro IPR002912, ACT_dom IPR012675, Beta-grasp_dom_sf IPR003607, HD/PDEase_dom IPR043519, NT_sf IPR004811, RelA/Spo_fam IPR007685, RelA_SpoT IPR004095, TGS IPR012676, TGS-like IPR033655, TGS_RelA |
Pfami | View protein in Pfam PF13291, ACT_4, 1 hit PF04607, RelA_SpoT, 1 hit PF02824, TGS, 1 hit |
SMARTi | View protein in SMART SM00471, HDc, 1 hit SM00954, RelA_SpoT, 1 hit |
SUPFAMi | SSF81271, SSF81271, 1 hit SSF81301, SSF81301, 1 hit |
TIGRFAMsi | TIGR00691, spoT_relA, 1 hit |
PROSITEi | View protein in PROSITE PS51671, ACT, 1 hit PS51831, HD, 1 hit PS51880, TGS, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RSH_BRUME | |
Accessioni | Q8YG65Primary (citable) accession number: Q8YG65 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 26, 2008 |
Last sequence update: | February 26, 2008 | |
Last modified: | December 2, 2020 | |
This is version 119 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |