ID A0A1Y0RPM7_9CYAN Unreviewed; 757 AA.
AC A0A1Y0RPM7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:ARV60480.1};
GN ORFNames=BZZ01_19225 {ECO:0000313|EMBL:ARV60480.1};
OS Nostocales cyanobacterium HT-58-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV60480.1, ECO:0000313|Proteomes:UP000196302};
RN [1] {ECO:0000313|EMBL:ARV60480.1, ECO:0000313|Proteomes:UP000196302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV60480.1,
RC ECO:0000313|Proteomes:UP000196302};
RA Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT "Genome sequences and microbial community composition of HT-58-2, a
RT tolyporphin-producing cyanobacterium-microbial holobiont.";
RL Submitted (FEB-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 -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; CP019636; ARV60480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0RPM7; -.
DR KEGG; ncn:BZZ01_19225; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000196302; Chromosome.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000196302}.
FT DOMAIN 66..165
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 411..472
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 680..754
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 757 AA; 86144 MW; 86DC9F3CFA5EC11F CRC64;
MISTLSTSRI DITLPEWLHT CLNGSSTERI SAEDDRRQSD RALIHGAFEF AYQLHQGQYR
KSGEPYICHP VAVAGILREL GGSAAMIAAG FLHDVVEDTE VTIEEIEQRF GKEVRLLVEG
VTKLSKINFK SKTESQAENF RRMFLAMAQD IRVIVVKLAD RLHNMRTLEH LPDEKRRRIA
LETREIFAPL ANRLGIWHMK WELEDLSFKY LEPESYRQIQ EYVAEKRAAR EERLTKVAEV
LRSRLMEAGI QCLDLSGRPK HLYSIYQKMQ KQNKEFHEIY DLAALRIIVN TNEECYRALA
IVHDACRPIP GRFKDYIGLP KPNRYQSLHT GVIGPWGRPL EVQIRTLEMH HVAEYGIAAH
WKYKETGGSH ATHLTAADEK FAWLRQLLEW QNDLKDAQEY LESVKDNLFE DDVYVFTPKG
DLVSLSPSST TIDFAYRIHT EVGNHCAGAK VNGRIVPLST RLQNGDIVEI LTQKNGHPSL
DWLNFVRTSA AKNRIKQWYK RSRREENVAR GRELLEKELG KPGVENLIKS QPMQIVAERC
NYHSMEDLLA ALGYGEVTLN LVLNRWREVV KAQQPVTTAS TVPTKELLPT TKALRDVPPA
SSRSTDSPIV GVEGLVHHLA KCCTPIPGES IIGVVTRGRG ISIHRQGCQN LETVEYERLV
PVHWNSAGEV QSRPQTYPVN IQIEALDRVG VLKDILSRLS DQGINVRHAQ VKTANGQPAL
IDLGIEIRDR PQLEQVFTQV KKLSDILNIR RVGQIDE
//
