ID A0A3N1G9E3_9ACTN Unreviewed; 806 AA.
AC A0A3N1G9E3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:ROP26860.1};
GN ORFNames=EDC03_3097 {ECO:0000313|EMBL:ROP26860.1};
OS Pseudokineococcus lusitanus.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Pseudokineococcus.
OX NCBI_TaxID=763993 {ECO:0000313|EMBL:ROP26860.1, ECO:0000313|Proteomes:UP000276232};
RN [1] {ECO:0000313|EMBL:ROP26860.1, ECO:0000313|Proteomes:UP000276232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7306 {ECO:0000313|EMBL:ROP26860.1,
RC ECO:0000313|Proteomes:UP000276232};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
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:ROP26860.1}.
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DR EMBL; RJKN01000009; ROP26860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1G9E3; -.
DR InParanoid; A0A3N1G9E3; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000276232; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ROP26860.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000276232};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ROP26860.1}.
FT DOMAIN 104..201
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 455..518
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 721..795
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 17..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 87960 MW; D64E354103CA736D CRC64;
MGRPTGRCVE EVLVAEQTPG AVGTTTGPEP EQVPARGDDG GAGGLRARLA RLGSRPSTTS
PVLEPLLRSL RSNHPKADTA MVERAYVVAE RCHRGQRRKS GDAYITHPVA VTTILADLGM
TAPTLAAALL HDTVEDTAYS LAQLRSEFGD EVAMLVDGVT KLDKVQYGDA AQAETVRKMV
VAMARDIRVL VIKLADRLHN ARTWKYVSAA SAEKKARETL EIYAPLAHRL GMNTIKWELE
DLSFATLYPG VYEEIVRLVA AQAPAREEYL AVVRDQVAAD LRQAKVRATV TGRPKHYYSV
YQKMIVRGRE FADIYDLVGV RVLVDTVRDC YAVLGALHAR WTPVPGRFKD YIAMPKFNMY
QSLHTTVIGP NGRPVEIQIR THLMHRRAEL GVAAHWKYKD AGRSGGDPAD TGAKGSLPGG
SSNGTDMAWL RQLLDWQKET ADPGEFLESL RFEINAAEVY VFTPKGDAIA LPAGSTPVDF
AYAVHTDVGH RTMGARVNGR LVPLESELDN GDVVEVFTSR VEGAGPSRDW MTFVRSPRAR
SKIKQWFSKE RREEAIEQGK DAIAKAMRKQ HLPIQRLMSH DSLVAVARDL HHPDVSALYA
AVGDGHVSAA SVVQKLVAAL GGEGGAEEDL AEAVVPLTRT APRRRSGDPG VVVKGVDDVW
VKVARCCTPV PRDPVIGFVT RGHGVSVHRR DCGNVAGLMN EPERVVEVEW SVGTDSVFLV
QIQVEALDRA RLLSDITRVL SDNHVNILSA SVTTSRDRVA LSKFTFEMGD PSHLDHVLGA
VRRVDGVFDV YRAGGRAEQP TGSAEG
//
