RSH_BRUSU
ID RSH_BRUSU Reviewed; 750 AA.
AC Q8CY42; G0K7Z3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=GTP pyrophosphokinase rsh;
DE EC=2.7.6.5;
DE AltName: Full=(p)ppGpp synthase;
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase;
GN Name=rsh; OrderedLocusNames=BR0652, BS1330_I0648;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP FUNCTION IN STRINGENT RESPONSE, AND DISRUPTION PHENOTYPE.
RC STRAIN=1330;
RX PubMed=16803581; DOI=10.1111/j.1462-5822.2006.00749.x;
RA Dozot M., Boigegrain R.-A., Delrue R.-M., Hallez R., Ouahrani-Bettache S.,
RA Danese I., Letesson J.-J., De Bolle X., Koehler S.;
RT "The stringent response mediator Rsh is required for Brucella melitensis
RT and Brucella suis virulence, and for expression of the type IV secretion
RT system virB.";
RL Cell. Microbiol. 8:1791-1802(2006).
CC -!- FUNCTION: Functions as a (p)ppGpp synthase. In eubacteria ppGpp
CC (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the
CC stringent response that coordinates a variety of cellular activities in
CC response to changes in nutritional abundance. It is necessary for
CC persistence in mice, essential for intracellular growth of Brucella and
CC required for expression of the type IV secretion system VirB and
CC therefore plays a role in adaptation of Brucella to its intracellular
CC host environment. {ECO:0000269|PubMed:16803581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC -!- DISRUPTION PHENOTYPE: Cells show morphological abnormalities such as
CC branching and swelling forms during vegetative growth. It is unable to
CC persist during stationary phase, presumably because of nutrient
CC limitation occurring during this growth phase. It shows an important
CC growth defect in human HeLa cells and in ovine macrophages MOCL3. At
CC four weeks post infection the number of viable bacteria (deletion
CC mutant) in mouse spleen is markedly reduced compared to the wild-type.
CC The deletion mutant shows very low levels or absence of VirB at all
CC time points of growth. {ECO:0000269|PubMed:16803581}.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; AE014291; AAN29581.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM17998.1; -; Genomic_DNA.
DR RefSeq; WP_004690700.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8CY42; -.
DR SMR; Q8CY42; -.
DR EnsemblBacteria; AEM17998; AEM17998; BS1330_I0648.
DR GeneID; 45051735; -.
DR KEGG; bms:BR0652; -.
DR KEGG; bsi:BS1330_I0648; -.
DR PATRIC; fig|204722.21.peg.1526; -.
DR HOGENOM; CLU_012300_3_0_5; -.
DR OMA; YKTIHTT; -.
DR PhylomeDB; Q8CY42; -.
DR PRO; PR:Q8CY42; -.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF19296; DUF5913; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00691; spoT_relA; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; GTP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..750
FT /note="GTP pyrophosphokinase rsh"
FT /id="PRO_0000322560"
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 390..451
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 676..750
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 587..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 83860 MW; 195B752C18594104 CRC64;
MMRQYELVER VQRYKPDVNE ALLNKAYVYA MQKHGSQKRA SGDPYFSHPL EVAAILTDMH
LDEATIAIAL LHDTIEDTTA TRQEIDQLFG PEIGKLVEGL TKLKKLDLVS KKAVQAENLR
KLLLAISEDV RVLLVKLADR LHNMRTLGVM CEDKRLRIAE ETMDIYAPLA GRMGMQDMRE
ELEELAFRYI NPDAWRAVTD RLAELLEKNR GLLQKIETDL SEIFEKNGIK ASVKSRQKKP
WSVFRKMETK GLSFEQLSDI FGFRVMVDTV QDCYRALGLI HTTWSMVPGR FKDYISTPKQ
NDYRSIHTTI IGPSRQRIEL QIRTREMDEI AEFGVAAHSI YKDRGSANNP HKISTETNAY
AWLRQTIEQL SEGDNPEEFL EHTKLELFQD QVFCFTPKGR LIALPRGATP IDFAYAVHTD
IGDSCVGAKV NGRIMPLMTE LKNGDEVDII RSKAQVPPAA WESLVATGKA RAAIRRATRS
AVRKQYSGLG MRILERAFER AGKPFSKDIL KPGLPRLARK DVEDVLAAVG RGELPSTDVV
KAVYPDYQDT RVTTQNNPAK AGEKGWFNIQ NAAGMIFKVP EGGEGAAAKV DPAATTPKPG
KRALPIRGTN PDLPVRFAPE GAVPGDRIVG ILQPGAGITI YPIQSPALTA YDDQPERWID
VRWDIDDQMS ERFPARISVS AINSPGSLAK IAQIAAANDA NIHNLSMVRT APDFTEMIID
VEVWDLKHLN RIISQLKESA SVSSAKRVNG
