ID A0A0G3XMM2_9SPHN Unreviewed; 696 AA.
AC A0A0G3XMM2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AB433_09810 {ECO:0000313|EMBL:AKM11723.1};
OS Croceicoccus naphthovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM11723.1, ECO:0000313|Proteomes:UP000035287};
RN [1] {ECO:0000313|EMBL:AKM11723.1, ECO:0000313|Proteomes:UP000035287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PQ-2 {ECO:0000313|EMBL:AKM11723.1,
RC ECO:0000313|Proteomes:UP000035287};
RA Zeng Y., Huang Y.;
RL Submitted (JUN-2015) 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 ---------------------------------------------------------------------------
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; CP011770; AKM11723.1; -; Genomic_DNA.
DR RefSeq; WP_047823799.1; NZ_JACIEL010000010.1.
DR AlphaFoldDB; A0A0G3XMM2; -.
DR STRING; 1348774.AB433_09810; -.
DR KEGG; cna:AB433_09810; -.
DR PATRIC; fig|1348774.3.peg.2055; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000035287; Chromosome.
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; 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; 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; 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 Kinase {ECO:0000313|EMBL:AKM11723.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035287};
KW Transferase {ECO:0000313|EMBL:AKM11723.1}.
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 624..696
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 696 AA; 78267 MW; A70C56295431A032 CRC64;
MLRQYELVER VKAYDPDADE ALLNRAYVYT VQKHGTQKRA SGDPYFSHPV EVAGLMTDLK
LDQETIITAL LHDTVEDTLA TIEDVEKNFG SDVARLVDGV TKLSKIEQMP ENERAAENLR
KLFLAMSEDL RVLLVKLADR LHNMRTLHFI SNPDKRRRIA RETMDIYAPL AERVGMYEYM
REMQLLAFEQ LEPEAYATIT GRLAQIRSTE GGQVDEIALH IKQALAEGGV KVEVSGREKH
PYSIWRKMAE RHVSFEQITD IMAFRVLTDS TEDCYRALGV LHRTWSMIPG KFKDYISTPK
SNGYRSLHTS LIYENSMRVE VQIRTHDMHR TNEFGLAAHW AYKQRGDGPD GQVGWLRDLI
EILDTAADAE ELLEHAKLAI YQDRIFAFTP KGALYQLPKG ATPVDFAFSV HTDLGASAVG
CKINGRHMPL RTPLANGDIV EIIKGADSEP QLSWLSFVVT AKARAAIRRS VRQKEREETA
RIGQELYESI VARMPMKIGK KALNGALKRL DLDDDTALML AIGSAKLTEK DVMEALVPGS
AAELPDDSFW QAPARSVRLR GLPKNAEFTL SECCHPVPGD RIVGVKDGRR IEVHTIDCLT
LGEQDDRRWI DLSWDPRSDG ATGLLRVMLY NRLGTLSEMT GVFAANHANI TQLSLNSRDD
LFGTYEVGIE VRDLAHLTRM ISALRASDAV AQADRV
//
