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Database: UniProt
Entry: A0A1Y3G530_9PROT
LinkDB: A0A1Y3G530_9PROT
Original site: A0A1Y3G530_9PROT 
ID   A0A1Y3G530_9PROT        Unreviewed;       747 AA.
AC   A0A1Y3G530;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE   AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN   ORFNames=HK11_09790 {ECO:0000313|EMBL:OUI89617.1};
OS   Acetobacter sp. DmW_043.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=1670658 {ECO:0000313|EMBL:OUI89617.1, ECO:0000313|Proteomes:UP000196359};
RN   [1] {ECO:0000313|EMBL:OUI89617.1, ECO:0000313|Proteomes:UP000196359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DmW_043 {ECO:0000313|EMBL:OUI89617.1,
RC   ECO:0000313|Proteomes:UP000196359};
RA   Ju J., Zhang J.;
RL   Submitted (JUN-2014) 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}.
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:OUI89617.1}.
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DR   EMBL; JOMN01000003; OUI89617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3G530; -.
DR   Proteomes; UP000196359; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase 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; 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; 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:OUI89617.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196359};
KW   Transferase {ECO:0000313|EMBL:OUI89617.1}.
FT   DOMAIN          52..151
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          395..460
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          673..747
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   747 AA;  82541 MW;  8243BBBB98254826 CRC64;
     MSVKDAKPVT CDKLLSVVRG YAPDADLESI RRAFDVAQKA HEGQLRDNGD PYITHPLAVA
     MILAGFRLDV SSVITALLHD TVEDTGVTQE QLRAEFGDTV SELVDGVTKL TRLELQSDRT
     KQAENFRKLV LAMSKDIRVL LVKLADRLHN MRTLHFVERV DRRQRIARET LDIYAPLAER
     IGMDRVKTEL QNLSFAQIEP EVDATLRARL NYLRGQGADV IEDVRRELLR LCHDAGLKNV
     HVAGREKSPY SIWDKMQRRN VAFEQLSDIM AFRVIVDTRE DCYMALGAVH AAYSVIAGRF
     KDYISTPKVN GYQSIHTGVT LRSPRNQKIE VQIRTAAMHD IAENGVAAHW AYKDGSGENT
     EGSPGFRRPR WVQDLLEILE ASSAPDEFLE NTKLELYQDQ VFCFSPKGQL ISLPRGATPV
     DFAYAVHSQI GDSCVGARVN GRLMPLRYEL QNGDQVEIMT ARGGAPSPSW ERFVVTGKAR
     ARIRRYVAAQ QRQTYLDAGR SALAKAFRQE GVDGSEKILE PVLKTLKQNS LHDLYVAVGN
     NSIGARDVVY ATYPELRRAV RAPRMVPGLP GVLGTAGPRL MAGTSGNQKK RADGNIPLVG
     LGAGIAVHFA ACCHPLPGDR IVGVVATGRG VTVHTKVCQT LENFAATPER FLDVDWDYDA
     MDRGGASTMR VGRISLIAEN VSSVLATVTN TVSKYDASIV NLKIVNRQLD FMEILVDVEV
     RDLRHLSSVI GGLRAASGVT QADRARS
//
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