ID A0A1C0UTE7_9CYAN Unreviewed; 754 AA.
AC A0A1C0UTE7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:OCQ88806.1};
GN ORFNames=BCR12_15665 {ECO:0000313|EMBL:OCQ88806.1};
OS Limnothrix sp. P13C2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Limnothrix.
OX NCBI_TaxID=1880902 {ECO:0000313|EMBL:OCQ88806.1, ECO:0000313|Proteomes:UP000093334};
RN [1] {ECO:0000313|EMBL:OCQ88806.1, ECO:0000313|Proteomes:UP000093334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P13C2 {ECO:0000313|EMBL:OCQ88806.1};
RA Tan B., Te S.H., Gin K., Thompson J.;
RT "Draft genome of Limnothrix sp. P13C2.";
RL Submitted (JUL-2016) 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:OCQ88806.1}.
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DR EMBL; MBRF01000033; OCQ88806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C0UTE7; -.
DR STRING; 1880902.BCR12_15665; -.
DR Proteomes; UP000093334; Unassembled WGS sequence.
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:UP000093334}.
FT DOMAIN 69..168
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 413..474
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 677..751
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 754 AA; 85647 MW; 38A43BFF9FD50F73 CRC64;
MVVAVSHHYS PIDEYPSLSL PTWLSQCLME DFHHPQGTER PLGNSLICRA FQFAYDLHQD
QYRASGEPYI AHPVAVAGLL RELGGSPEMI AAGFLHDIVE DTATTPEDLE AKFGAEVRFL
VEGVTKLSKF NFSSKKEQQA ENFRRMFLAM AKDIRVIVVK LADRLHNMRT LEHLAPEKQR
RISQETMDIF APLANRLGIG RFKWELEDLS FKYLQPDAYR EIQELVAEKR TDREARLDRV
LQILRDRLNQ LGIQSAETSG RPKHLYGIYQ KMQRQNKSFW EIYDIAAVRV IVQSVDECYR
ALAVVHDEFR PIPGRFKDYI GLPKPNRYQS LHTSVIGLTG RPLEVQIRTE EMHRVAEYGI
AAHWKYKETG GSHLAASTDD EKFIWLRQLL EWQSDLKDAH EYLENVKKNL FEDEIYVFTP
KGDVIALSNH ATPVDFAYRI HTEVGNHCAG ALVNRRMVTL DTGLQNGDII EIITQKNAHP
SLDWLNFVVT ATARNRIRLW YKRSRREENI SRGRELLEKE LGKQGFESFL KSAPMQAVAE
RCNYHSVDDT LAALGYGEIT LNMLLGRIRE VVKTAQPVAE AVIMPSSSPR PHGDSGSNRH
RLSPILGVEG LLHHMAGCCH AVPGEPIVGV VTRSSRGLAI HRQDCSNLAN VPGDRLVPVS
WNPEVTNVGR QPTYPVEIRV ETIDRVGVLK DILTRLADSN VNVNRAAVKT KPGETAMITL
GIDICDRTQL DRVFTHIRKM SDVIDLRRVF QNAE
//
