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Database: UniProt
Entry: A0A160JFF6_9PROT
LinkDB: A0A160JFF6_9PROT
Original site: A0A160JFF6_9PROT 
ID   A0A160JFF6_9PROT        Unreviewed;       719 AA.
AC   A0A160JFF6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE            EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE   AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN   ORFNames=A6A40_06430 {ECO:0000313|EMBL:ANC91566.1};
OS   Azospirillum humicireducens.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC91566.1, ECO:0000313|Proteomes:UP000077405};
RN   [1] {ECO:0000313|EMBL:ANC91566.1, ECO:0000313|Proteomes:UP000077405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC91566.1,
RC   ECO:0000313|Proteomes:UP000077405};
RX   PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA   Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT   "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT   from a microbial fuel cell.";
RL   Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
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; CP015285; ANC91566.1; -; Genomic_DNA.
DR   RefSeq; WP_063634663.1; NZ_CP015285.1.
DR   AlphaFoldDB; A0A160JFF6; -.
DR   STRING; 1226968.A6A40_06430; -.
DR   KEGG; ahu:A6A40_06430; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000077405; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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   Hydrolase {ECO:0000313|EMBL:ANC91566.1}.
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          386..447
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          644..718
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   719 AA;  80794 MW;  3CCB5E2F02C26919 CRC64;
     MIRQYELVER VKAYDPNADE DLLNRAYVYS MKAHGSQTRA SGDPYFLHPL EVAGILTQMK
     LDAGTIATAL LHDTVEDTVA TLEDIERVFG KEIARLVDGV TKLSRLELNS EQAKQAENFR
     KLVLAMSEDI RVLLVKLADR LHNMRTLFHL KKPEKRKRIA RETIEIYSPL AERIGMHKIK
     DELDDLAFAE LNPDARDSIL AQLARLRSEG ENRVQTIITE LRELLASEGL PDATVSGREK
     SAYSIWRKLQ RKNVSFEQLS DIMAFRITVG SVGECYQALG VVHAHYPVVP GRFKDYISTP
     KPNGYRSLHT GVIGPGRNRI EVQIRTQDMH EIAELGVAAH WAYKQDHQPR PNGGEYRWLR
     ELLDILEHAQ KPEEFLEHTK LELFQDQVFC FTPKGDLIAL PRGATPVDFA YAVHSQVGDH
     CVGAKINGRM LPLRTQLQNG DQVDIVTSKA QTPVPGWERF VVTGKARARI RKFLRTQQRA
     QYMELGRGML MRQFKAEGYE FTEKALEAAT KIFQQPTVDD LMAGVGSGLH SVREVFHAVF
     PGHKAQAAPA VREMEESAPK QKAKARKESA LPIRGLIPGM AVHYARCCHP LPGDRIVGIV
     TTGKGVTIHT IDCETLESFH ESPERWIDVS WETGPDSPEE HVGRISVVIA NEQGSLGTLF
     TVIGKNQGNV IHQKITNRST DHFELLIDID VKDAKHLTNI MAALRATPAI HSVERARGR
//
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