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   27-MAR-2024, entry version 125.
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; Pseudomonadota; 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   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   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; cd04876; ACT_RelA-SpoT; 1.
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; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 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   NCBIfam; TIGR00691; spoT_relA; 1.
DR   PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF19296; RelA_AH_RIS; 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; ACT-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 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
//