ID RSH_BRUO2 Reviewed; 750 AA.
AC A5VPI9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=BOV_0645;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(2009).
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. Plays a role in
CC adaptation of Brucella to its intracellular host environment (By
CC similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000708; ABQ60728.1; -; Genomic_DNA.
DR RefSeq; WP_004688165.1; NC_009505.1.
DR AlphaFoldDB; A5VPI9; -.
DR SMR; A5VPI9; -.
DR GeneID; 58776213; -.
DR KEGG; bov:BOV_0645; -.
DR HOGENOM; CLU_012300_3_0_5; -.
DR PhylomeDB; A5VPI9; -.
DR Proteomes; UP000006383; 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 3: Inferred from homology;
KW ATP-binding; GTP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..750
FT /note="GTP pyrophosphokinase rsh"
FT /id="PRO_0000322564"
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; 83914 MW; D717A5F11B802A6E CRC64;
MMRQYELVER VQRYKPDVNE ALLNKAYVYA MQKHGSQKRA SGDPYFSHPL EVAAILTDMH
LDEATIAIAL LHDTIEDTTA TRQEIDQLFG PEIGKLVEGL TKLKKLDLVS KKAVQAENLR
KLLLAISEDV RVLLVKLADR LHNMRTLGVM REDKRLRIAE 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 AINSPGSLAE IAQIAAANDA NIHNLSMVRT APDFTEMIID
VEVWDLKHLN RIISQLKESA SVSSAKRVNG
//
