ID A0A095DIV7_9SPHN Unreviewed; 697 AA.
AC A0A095DIV7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN ORFNames=FG95_00136 {ECO:0000313|EMBL:KGB59228.1};
OS Sphingopyxis sp. LC363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB59228.1, ECO:0000313|Proteomes:UP000029625};
RN [1] {ECO:0000313|EMBL:KGB59228.1, ECO:0000313|Proteomes:UP000029625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC363 {ECO:0000313|EMBL:KGB59228.1,
RC ECO:0000313|Proteomes:UP000029625};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (MAY-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 -!- 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:KGB59228.1}.
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DR EMBL; JNFC01000001; KGB59228.1; -; Genomic_DNA.
DR RefSeq; WP_037553257.1; NZ_JNFC01000001.1.
DR AlphaFoldDB; A0A095DIV7; -.
DR STRING; 1120705.FG95_00136; -.
DR PATRIC; fig|1120705.3.peg.137; -.
DR eggNOG; COG0317; Bacteria.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000029625; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000029625}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 383..444
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 625..697
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 697 AA; 77768 MW; 9CC9D170BFAE99A0 CRC64;
MLRQYELVER VRAYDPDVDE ALLNRAYVFT VQKHGSQKRA SGDPYFSHPV EVAGILTDLH
LDSETIVTAL LHDTLEDTLT TPEEIERLFG SDVGRLVDGV TKLSKIEAQT ENERAAENLR
KFLLAMSDDI RVLLVKLADR LHNMRTLHFI KNPDKRRRIA KETMDIYAPL AERIGMYEYM
REMQLLAFRE LEPEAYATIT GRLAKLTAGG KDKVAAITRE FKELLAAAGI EAEVSGREKH
PYSIWRKMQE RHVSFEQVTD IIAFRIVTPT DADCYAALGL IHRKWKMVPG RFKDYISTPK
RNGYKSLHTT IMHQQNMRIE IQLRSLGMHQ QSEFGLAAHW AYKQGGSTPD GQAGWIRDLI
EILEQTHDPE EFLENTRIAM YQDRIFAFTP KGSLHQLPKG ATPVDFAYAV HTGLGDRTVG
AKVNGRLVPL RTQLSNGDTV EILSSDKQTP QPAWLGFAVT GKARAAIRRH VRSKEKVELA
ALGRTMYDEI VARLPNKVGD KARAAARERL KLDDDSALYV AIAKQRLTDN AVLEALVPGI
TAEMKTKPGK LVQGAAVSIA GLTPGVAFQL ADCCHPVPGD RIVGLSRPGE GIEVHVIDCP
SLADGVDADW IDLRWQEDSE GGNARLCIVI RNEPGTLAEM SGILAANMAN ITNLRLSNRE
GGFHTYDVVV EVRDVQHVMR ILSALRASDS VVQAERL
//
