ID A0A1W1XEZ7_9NEIS Unreviewed; 738 AA.
AC A0A1W1XEZ7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SMC22198.1};
GN ORFNames=SAMN02745857_01362 {ECO:0000313|EMBL:SMC22198.1};
OS Andreprevotia lacus DSM 23236.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Andreprevotia.
OX NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC22198.1, ECO:0000313|Proteomes:UP000192761};
RN [1] {ECO:0000313|EMBL:SMC22198.1, ECO:0000313|Proteomes:UP000192761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC22198.1,
RC ECO:0000313|Proteomes:UP000192761};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FWXD01000006; SMC22198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1XEZ7; -.
DR STRING; 1121001.SAMN02745857_01362; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000192761; Unassembled WGS sequence.
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; 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; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SMC22198.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192761};
KW Transferase {ECO:0000313|EMBL:SMC22198.1}.
FT DOMAIN 413..474
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 667..738
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 738 AA; 81591 MW; D42C0B6C6A958878 CRC64;
MVAVTRPLAL SIAEAADPTH WLAQLAERYP PAQVERLRTA LDWAADVYGD KTQTDICDPL
FTHAVAAASI VADLNLDADT VIASLLFAIP DFVPDAHAAV ESRLGKEVAQ LVDGVDKVRK
IRVLANIGAR DVTGKPQDAA AQVEAIRKML LAMVEDIRAV LIKLAWRTQT MHALGGAPAE
VQTSIARETL ELFAPLANRL GVWQIKWELE DLGFRYLHPD TYKKIAKLLD ERRIDREQFI
SNVLQTLHRE LETAGISGAN LMGRPKHIYS IWRKMQKKKL DFSELYDIRA VRVLVPELKD
CYTVLGIVHN LWQPIPGEFD DYIAHPKGNN YRSLHTAVIG PDDKAVEVQI RTFEMHEHAE
LGVAAHWRYK EGGKGDAKYE EKIAWLRQLL DWKSDLASDA QLADAFKAEL FEDTIYALTP
AGRVIALPKG STPVDFAYHL HTDLGHRCRG AKVNGQIVPL HTALENGQRV EIIAAKEGGP
SLDWLHQGYV KSTRAQQKLR AWIRQQNLDV AIENGRAIYD KEAARNGATQ ANQDAVAQRL
GYKGLDELLA GLGHGEVTLR ELADALTADA KPVVETTINP DDVIKRARAS GQGEGILIEG
VDKLMTLLAK CCKPVPPDAV VGFVTKGRGI SIHRTDCATL KRLAVASPER LISADWGKHA
GSVFSTDLLI EAHDRPSLLR DLSDVMSREK INVTGVNTLS RDTLAKMRFT VEIRSADDLA
RIRSRLTDVV GVLSVNRA
//
