RSH_BRUA2
ID RSH_BRUA2 Reviewed; 750 AA.
AC Q2YN11;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=BAB1_0672;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ10628.1; -; Genomic_DNA.
DR RefSeq; WP_002963796.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YN11; -.
DR SMR; Q2YN11; -.
DR STRING; 359391.BAB1_0672; -.
DR EnsemblBacteria; CAJ10628; CAJ10628; BAB1_0672.
DR GeneID; 3787392; -.
DR KEGG; bmf:BAB1_0672; -.
DR PATRIC; fig|359391.11.peg.2986; -.
DR HOGENOM; CLU_012300_3_0_5; -.
DR OMA; YKTIHTT; -.
DR PhylomeDB; Q2YN11; -.
DR Proteomes; UP000002719; 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 3: Inferred from homology;
KW ATP-binding; GTP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..750
FT /note="GTP pyrophosphokinase rsh"
FT /id="PRO_0000322562"
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; 83856 MW; 4836EEECB0E52495 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 RGELPSADVV
KAVYPDYQDT RVTTQNNPAK AGEKGWFNIQ NAAGMIFKVP EGGEGAAAKV DPAATTPKPG
KRALPIRGTN PDLPVRFAPE GAVPGDRIVG ILQPGAGITI YPIQSPALTA YDDQPERWID
VRWDIDDQMS ERFPARISVS AINSPGSLAE IAQIAAANDA NIHNLSMART APDFTEMIID
VEVWDLKHLN RIISQLKESA SVSSAKRVNG