RSH_BRUAB
ID RSH_BRUAB Reviewed; 750 AA.
AC Q57E90;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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; Synonyms=spoT; OrderedLocusNames=BruAb1_0669;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
RN [2]
RP FUNCTION IN ADAPTATION TO INTRACELLULAR REPLICATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=544 / Biovar 1;
RX PubMed=15870469; DOI=10.1099/mic.0.27782-0;
RA Kim S., Watanabe K., Suzuki H., Watarai M.;
RT "Roles of Brucella abortus SpoT in morphological differentiation and
RT intramacrophagic replication.";
RL Microbiology 151:1607-1617(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.
CC {ECO:0000269|PubMed:15870469}.
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. It does not grow in RPMI-1640 with or
CC without 10% FBS. It shows decreased growth until 48 hours in RPMI-1640
CC and stationary growth until 48 hours in RPMI-1640 with 10% FBS. It has
CC the same ability as the wild-type to internalize at 0 minute but a
CC lower rate of internalization at 30 minutes. It shows a lower rate of
CC intracellular replication within macrophages than the wild-type. Its
CC adherence is four times higher than that of the wild-type. It shows
CC lower MICs than the wild-type for several antimicrobial agents such as
CC penicillin G, methicillin, erythromycin and doxycycline. At ten days
CC post infection the number of viable bacteria (disruption mutant) is
CC markedly reduced compared to the wild-type.
CC {ECO:0000269|PubMed:15870469}.
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; AE017223; AAX74044.1; -; Genomic_DNA.
DR RefSeq; WP_002963796.1; NC_006932.1.
DR AlphaFoldDB; Q57E90; -.
DR SMR; Q57E90; -.
DR EnsemblBacteria; AAX74044; AAX74044; BruAb1_0669.
DR GeneID; 3787392; -.
DR KEGG; bmb:BruAb1_0669; -.
DR HOGENOM; CLU_012300_3_0_5; -.
DR OMA; YKTIHTT; -.
DR Proteomes; UP000000540; 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_0000322563"
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
