ID A0A0J5P679_9PAST Unreviewed; 734 AA.
AC A0A0J5P679;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN Name=relA {ECO:0000313|EMBL:KMK50984.1};
GN ORFNames=RO21_08790 {ECO:0000313|EMBL:KMK50984.1};
OS Muribacter muris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Muribacter.
OX NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK50984.1, ECO:0000313|Proteomes:UP000036270};
RN [1] {ECO:0000313|EMBL:KMK50984.1, ECO:0000313|Proteomes:UP000036270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK50984.1,
RC ECO:0000313|Proteomes:UP000036270};
RA Christensen H., Nicklas W., Bisgaard M.;
RT "Reclassification of Actinobacillus muris as Muribacter muris.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMK50984.1}.
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DR EMBL; JWIZ01000056; KMK50984.1; -; Genomic_DNA.
DR RefSeq; WP_047977416.1; NZ_JWIZ01000056.1.
DR AlphaFoldDB; A0A0J5P679; -.
DR STRING; 67855.RO21_08790; -.
DR PATRIC; fig|67855.3.peg.1833; -.
DR Proteomes; UP000036270; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 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; 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:SF40; GTP PYROPHOSPHOKINASE; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000036270};
KW Transferase {ECO:0000313|EMBL:KMK50984.1}.
FT DOMAIN 52..154
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 397..458
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 659..734
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 734 AA; 83997 MW; 2078CA5E143446EA CRC64;
MVAIRRSHLL EPTNFELASW SAALKMSPIT FEELQSAWQY AQEKLDTDQF HLMWYGIEMV
EILHGLNMDD DSLIAALLFP LVKQHIIDLV QVKEHFGNQV KNLVKGVLEM DNIRQLNASH
TSDLQIDNIR RMLLAMVDDF RCVVIKLAER IVYLRDVERC SEEDLVLAAK ECSHIYAPLA
NRLGIGQLKW ELEDYCFRAL HPKEYRQIAK YDLAERRLDR EKYIANFVAD LTACLKEELN
EVQVYGRPKH IYSIWKKMQK KHLTFNQLFD VRAVRVIVPT LEDCYTALGV VHTQYLHLAE
HFDDYISNPK PNGYQSIHTV VLGKGDKPIE VQIRTQKMHD DAELGVAAHW KYKEGAAAGR
SGYEEKIVWL RKLLDWQKDI ADSGDVLAEM RSQVFDDRVY VFTPKGDVVD LPNNATSLDF
AYTIHSEIGH RCIGAKVAGR IVPFTYILQM GDQVEIITQK NPNPSRDWLN PSQGFVNTAK
ARSKIIAWFK KLDREKHIPI GKEMLEAEMA KYQFNYKQIE EFALPRYNLK QLDDLYASIG
GGDIRLNQLM HYLQNKLVKT TAEQADEAVL KQVANKNQSP KPHKNGFIVV EGVGNLMHHI
ARCCQPIPGD DIVGYITQGR GISIHRADCE QLFDLQSNSP ERVVDAEWGE HYATGFSLTI
RVIANDRNGL LRDVSAIMAN EKINVLGVSS RTDTKRRIAT IDVEVELNNI QLLSKLTARI
VQLDDVIEAK RLSN
//
