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
//