ID A0A2S5SUK1_9BURK Unreviewed; 752 AA.
AC A0A2S5SUK1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:PPE66415.1};
GN ORFNames=C1704_08845 {ECO:0000313|EMBL:PPE66415.1};
OS Caldimonas caldifontis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=1452508 {ECO:0000313|EMBL:PPE66415.1, ECO:0000313|Proteomes:UP000238605};
RN [1] {ECO:0000313|EMBL:PPE66415.1, ECO:0000313|Proteomes:UP000238605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCRC 80649 {ECO:0000313|EMBL:PPE66415.1,
RC ECO:0000313|Proteomes:UP000238605};
RA Tang B.;
RT "Reclassifiation of [Polyangium] brachysporum DSM 7029 as Guopingzhaonella
RT breviflexa gen. nov., sp. nov., a member of the family Comamonadaceae.";
RL Submitted (FEB-2018) 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:PPE66415.1}.
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DR EMBL; PSNX01000007; PPE66415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5SUK1; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000238605; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase 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:PPE66415.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000238605};
KW Transferase {ECO:0000313|EMBL:PPE66415.1}.
FT DOMAIN 423..484
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 681..752
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 752 AA; 82790 MW; 1DF50C9CB6CB4DB6 CRC64;
MKTSHQDAAP QAAPIVQLAG GLDQPGRSAS MRGPGMAEAL AQEMARLERA RAFAEPLLAG
QRLDTGEDAL DHAAGVASIL RAIGASPSLL AAVYLVYVGE YLNKPEDVIG KAFGASYASL
VAATRKLVQI QRNARDALVD EDMRAEQTER VRKMLLAFSR DLRVVLVRLA SRLQTLRYYA
QSKRDCPLVL ARESLHVFAP LANRLGIWQI KWELEDLSFR FLEPEQYKAI ARMLDEKRIE
REQVVEQARQ RLSAQLREQG IPALVQGRPK HLYSIWKKMR GKQLDFSGVF DLRALRVIVP
TVPDCYAALG LVHERYRPLP EEFDDYIAKP KPNGYQSLHT VVYDEQGRSL EIQIRTQAMH
EHAEHGVAAH WAYKEAGTKG YAGVSAAGDF EAQVAEARKA VLRQLLAWER DFSGEASTTG
FDDRIYVFTP QAAIVELPAG ATPVDFAYTL HTDLGHRCRG ARVDGAMVPL NTALHSGQTV
EVVAAKEGGP SMDWLNPELG YLRSSRAKAK VRAWFNALAQ QQTIARGREL VEKLLQREGR
TAMKLEDLAS QLGFKSADAL FDVVGKDEYS LRNIEQLLRP ADTVPQPDDQ IALRKPRSEA
PTGKGGVLVV GVESLLTTLA RCCKPAPPDA IGGYVTKGKG VAVHRADCSS FRQIAGRHPE
RVISVAWGQP SGEKAPVYPV DVAVEALDRQ GLLRDISEVF AKEKTNVIGV NTQTVRGTAW
MTFTVEVSDS ARLSQVLAAV AQVPGVRAAR RR
//
