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GTP pyrophosphokinase rsh (EC 2.7.6.5) ((p)ppGpp synthase) (ATP:GTP 3'-pyrophosphotransferase)

 RSH_BRUAB               Reviewed;         750 AA.
Q57E90;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
22-NOV-2017, entry version 87.
RecName: Full=GTP pyrophosphokinase rsh;
EC=2.7.6.5;
AltName: Full=(p)ppGpp synthase;
AltName: Full=ATP:GTP 3'-pyrophosphotransferase;
Name=rsh; Synonyms=spoT; OrderedLocusNames=BruAb1_0669;
Brucella abortus biovar 1 (strain 9-941).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Brucellaceae; Brucella.
NCBI_TaxID=262698;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=9-941;
PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L.,
Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
"Completion of the genome sequence of Brucella abortus and comparison
to the highly similar genomes of Brucella melitensis and Brucella
suis.";
J. Bacteriol. 187:2715-2726(2005).
[2]
FUNCTION IN ADAPTATION TO INTRACELLULAR REPLICATION, AND DISRUPTION
PHENOTYPE.
STRAIN=544 / Biovar 1;
PubMed=15870469; DOI=10.1099/mic.0.27782-0;
Kim S., Watanabe K., Suzuki H., Watarai M.;
"Roles of Brucella abortus SpoT in morphological differentiation and
intramacrophagic replication.";
Microbiology 151:1607-1617(2005).
-!- FUNCTION: Functions as a (p)ppGpp synthase. In eubacteria ppGpp
(guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the
stringent response that coordinates a variety of cellular
activities in response to changes in nutritional abundance. Plays
a role in adaptation of Brucella to its intracellular host
environment. {ECO:0000269|PubMed:15870469}.
-!- CATALYTIC ACTIVITY: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-
triphosphate.
-!- DISRUPTION PHENOTYPE: Cells show morphological abnormalities such
as branching and swelling forms. It does not grow in RPMI-1640
with or without 10% FBS. It shows decreased growth until 48 hours
in RPMI-1640 and stationary growth until 48 hours in RPMI-1640
with 10% FBS. It has the same ability as the wild-type to
internalize at 0 minute but a lower rate of internalization at 30
minutes. It shows a lower rate of intracellular replication within
macrophages than the wild-type. Its adherence is four times higher
than that of the wild-type. It shows lower MICs than the wild-type
for several antimicrobial agents such as penicillin G,
methicillin, erythromycin and doxycycline. At ten days post
infection the number of viable bacteria (disruption mutant) is
markedly reduced compared to the wild-type.
{ECO:0000269|PubMed:15870469}.
-!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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EMBL; AE017223; AAX74044.1; -; Genomic_DNA.
RefSeq; WP_002963796.1; NC_006932.1.
ProteinModelPortal; Q57E90; -.
EnsemblBacteria; AAX74044; AAX74044; BruAb1_0669.
KEGG; bmb:BruAb1_0669; -.
HOGENOM; HOG000018299; -.
KO; K01139; -.
OMA; TIHTTIF; -.
Proteomes; UP000000540; Chromosome I.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
CDD; cd00077; HDc; 1.
CDD; cd05399; NT_Rel-Spo_like; 1.
CDD; cd01668; TGS_RelA_SpoT; 1.
Gene3D; 3.10.20.30; -; 1.
InterPro; IPR002912; ACT_dom.
InterPro; IPR012675; Beta-grasp_dom_sf.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR004811; RelA/Spo_fam.
InterPro; IPR007685; RelA_SpoT.
InterPro; IPR004095; TGS.
InterPro; IPR012676; TGS-like.
InterPro; IPR033655; TGS_RelA.
Pfam; PF13291; ACT_4; 1.
Pfam; PF13328; HD_4; 1.
Pfam; PF04607; RelA_SpoT; 1.
Pfam; PF02824; TGS; 1.
SMART; SM00471; HDc; 1.
SMART; SM00954; RelA_SpoT; 1.
SUPFAM; SSF81271; SSF81271; 1.
TIGRFAMs; TIGR00691; spoT_relA; 1.
PROSITE; PS51671; ACT; 1.
PROSITE; PS51831; HD; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; GTP-binding; Kinase;
Nucleotide-binding; Transferase.
CHAIN 1 750 GTP pyrophosphokinase rsh.
/FTId=PRO_0000322563.
DOMAIN 45 144 HD. {ECO:0000255|PROSITE-
ProRule:PRU01175}.
DOMAIN 676 750 ACT. {ECO:0000255|PROSITE-
ProRule:PRU01007}.
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


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