ID A0A347WLH6_9LACT Unreviewed; 732 AA.
AC A0A347WLH6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=CL176_07940 {ECO:0000313|EMBL:AXY25933.1};
OS Suicoccus acidiformans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Suicoccus.
OX NCBI_TaxID=2036206 {ECO:0000313|EMBL:AXY25933.1, ECO:0000313|Proteomes:UP000263232};
RN [1] {ECO:0000313|EMBL:AXY25933.1, ECO:0000313|Proteomes:UP000263232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY16052 {ECO:0000313|EMBL:AXY25933.1,
RC ECO:0000313|Proteomes:UP000263232};
RA Li F.;
RT "Complete genome sequence of Oxytococcus suis strain ZY16052.";
RL Submitted (SEP-2017) 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 -!- 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}.
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DR EMBL; CP023434; AXY25933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347WLH6; -.
DR KEGG; abae:CL176_07940; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000263232; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; 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; PS51831; HD; 1.
DR PROSITE; PS50889; S4; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AXY25933.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000263232};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AXY25933.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 394..455
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT REGION 560..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 83422 MW; 78D44E5AAA2F984C CRC64;
MTQNIDYTAQ EVLDLCATYM NETGVAKVEK ALNVATQAHE GQMRMSGEPY IIHPIQVAGI
LAELKMDPDT VATGFLHDVV EDTDYTLEDI ESAFSETIAF LVDGVTKLGK FRFQSKQEAL
AENHRKMLMA MAKDIRVIIV KLADRLHNMR TMRFQKPEKQ VEKSEEALEI YAPLADRIGM
SNIKWELEDI SLRYINPDAY YNIVNQMDSK REEREAYIQA TAEEIQASLQ ELDIEAEVYG
RPKHIYSIYR KMTDQKKEFD DIYDLLALRV ITESIKDCYA VVGAVHTKWR PMPGRFKDYI
AMPKANMYQS LHTTVIGSDG RPVEIQIRTK EMHEVAENGI AAHWAYKQGK TDGVNPDDNL
QKQLQWFRDL VELQDETEDA KEFMDSVKQD LFKDQVYIFT PQGDVIELPV GSGPIDFAYH
IHTEVGNKTV GAKVNGEIVS LDYQLKNGDI VQILTNPNSN GPSRDWLKHT HTSKARNRIK
RYFKHLEREE KAAQGEQIMD RELREAGRSL KFIERRKVED ALKERFNFNE MTDFYAAIGY
GELNPSTVLN FLDVHKPKDA TKETSEAEVN RTATKPKSRT VHESGVVVEG ADNLMIRLSR
CCNPVPGDEI IGYITRGRGI SVHRKDCPNL KGESDLQNRT IDVHWDTMDT IEKDFVCEIR
IIGFERSGLI NDILHVVNHS VENLLSVQGK QDENSGALVT VKVGVSDTQQ IDQLLTKLKS
IPDVEDAFRK VS
//