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Database: UniProt
Entry: A0A1M5JXN7_9BURK
LinkDB: A0A1M5JXN7_9BURK
Original site: A0A1M5JXN7_9BURK 
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
//
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