ID A0A1M5JXN7_9BURK Unreviewed; 745 AA.
AC A0A1M5JXN7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SHG45342.1};
GN ORFNames=SAMN05428948_0550 {ECO:0000313|EMBL:SHG45342.1};
OS Massilia sp. CF038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1881045 {ECO:0000313|EMBL:SHG45342.1, ECO:0000313|Proteomes:UP000184361};
RN [1] {ECO:0000313|EMBL:SHG45342.1, ECO:0000313|Proteomes:UP000184361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF038 {ECO:0000313|EMBL:SHG45342.1,
RC ECO:0000313|Proteomes:UP000184361};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQWU01000001; SHG45342.1; -; Genomic_DNA.
DR RefSeq; WP_073212540.1; NZ_FQWU01000001.1.
DR AlphaFoldDB; A0A1M5JXN7; -.
DR STRING; 1881045.SAMN05428948_0550; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000184361; 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; 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:SF36; 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:SHG45342.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000184361};
KW Transferase {ECO:0000313|EMBL:SHG45342.1}.
FT DOMAIN 78..177
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 419..480
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 670..745
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 83309 MW; 091EEAFB7215193C CRC64;
MNLTTPDTTL PGTPKTRTPR ASKPDATPAI APGVASVTQL TAKLAEYLSP TELKKVKEAY
RFSDEMHLGQ VRKSGEPYIS HPIAVAEICA DWKLDAQAIM AALLHDVMED QDVKKDELIE
RFGAQVATLV DGLSKLEKIE FQSLIEAQAE NFRKMLLAMA SDVRVILIKL ADRLHNMRTL
EHMTDAKKRR IASETMEVYV PIAHRLGLNN IYRELQDLAF SHLYPVRYRT LAKAVKAARG
NRREVVKKIL ESVKGTLANA GLEAEVYGRE KTLYGIYKKM RSKRLSFSQV LDVYGFRVVV
DNFANCYVAL GTLHGLYKPM PGKFKDYIAI RKLNGYQSLH TTLIGPYGTP VEFQIRTQEM
HRTAESGVAA HWLYKNGDSN LSDLQQRTHA WLQSLLDIQQ QTGDSAEFLE HVKVDLFPDS
VYVFTPKSKI IALPRGATAL DFAYTIHTGI GDHTVAVKIN HEAATLRTEL RNGDIIEIVT
DPNSRPSPTW LAFVRTGKAR SAIRHHLRTI NLNESVELGQ ELLAQALTAL NIRPDLPAPT
IEKLLNESSA NTMDELYADI GIGKRMAALV ARHIFGLIDD ELVSVPSTQH ASPGELDPVT
IYGAEGVAVQ LAPCCLPIPG DQVIGQLRRD QGLIVHTHDC VAAKRTRAKE PDRWIPVQWG
QEVNRRFDCR IRLLINNEKG ILARVAAEIG ESDANISYVG MDEDDEHVMT QLRFTIQVKD
RVHLAHLIRN LRGVAGVTRV ERERN
//