ID A0A175RHR1_9MICO Unreviewed; 750 AA.
AC A0A175RHR1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:KTR02921.1};
GN ORFNames=NS184_14800 {ECO:0000313|EMBL:KTR02921.1};
OS Curtobacterium luteum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=33881 {ECO:0000313|EMBL:KTR02921.1, ECO:0000313|Proteomes:UP000078252};
RN [1] {ECO:0000313|EMBL:KTR02921.1, ECO:0000313|Proteomes:UP000078252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS184 {ECO:0000313|EMBL:KTR02921.1,
RC ECO:0000313|Proteomes:UP000078252};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTR02921.1}.
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DR EMBL; LDQC01000095; KTR02921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175RHR1; -.
DR STRING; 33881.NS184_14800; -.
DR PATRIC; fig|33881.3.peg.3493; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000078252; 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:KTR02921.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KTR02921.1}.
FT DOMAIN 70..167
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 413..474
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 675..749
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 750 AA; 83529 MW; 8534181C1C6CB27D CRC64;
MGPNTTGNLG SLRSLLPRLF SRAQPAGAVD TLIRTVRSHH PKADVTLIER AYSVAEQAHD
GQKRKSGEPY ITHPVAVAQI LADLGIGTIT IASALLHDTV EDTDYQLDQL RADFGDEIAM
LVDGVTKLDK VKYGDSAQAE TVRKMVIAMS KDIRVLVIKL ADRLHNARTW GFVESASATR
KAKETLEIYA PLAHRLGIQM IKLELEDLSF AVLHPKLYVE IDSLVKERQP KREQFVQNVI
GTLKKDLKAA KIRGDVMGRP KQYYSIYQKM IVRGREFDEI YDLVGIRVLV PTVRDCYAML
GSVHARWTPL PGRFKDYIAT PKFNLYQSLH TTVLGPQGRA VEIQIRTHEM HQRAEFGVAA
HWKYKQRVTG RDVDSSSQND QDMAWLAHIT DWQAETSDPG EFLDSLRYEI GAKETYVFTP
QGKVIGLPSG ATPVDFAYAV HTEIGHRTMG AKVNGRLVPL ESTLSSGDVV EIFTSKNPDS
GPSQDWLTFV RSPRARNKIK QWFTKERREE AIEQGRDAIA RAMRKQNLPL QRILSQDTIA
EVASSMRYED VSALYAAIGE GHVSTQSVIE KVLGSVQTEA ETDEPELAFP RQITSRQLRN
SDSGVLVRGA PDILVKLAKC CTPVPGDQIV GFITRGQGVS VHQASCSNVK SLMNEPDRMI
EVEWAPSSKS VFLVQIQIEA LDRSGLLSDV TRVLTDHHVN ILSATVSTSS DRLALSRFVF
EMGDTTHLDR VLNAVRRIDA VYDVYRVSAG
//
