ID A0A1F8MQJ9_9CHLR Unreviewed; 737 AA.
AC A0A1F8MQJ9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:OGO00885.1};
GN ORFNames=A2Y58_01460 {ECO:0000313|EMBL:OGO00885.1};
OS Chloroflexi bacterium RBG_13_51_52.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797626 {ECO:0000313|EMBL:OGO00885.1, ECO:0000313|Proteomes:UP000180306};
RN [1] {ECO:0000313|EMBL:OGO00885.1, ECO:0000313|Proteomes:UP000180306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO00885.1}.
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DR EMBL; MGMT01000004; OGO00885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MQJ9; -.
DR STRING; 1797626.A2Y58_01460; -.
DR Proteomes; UP000180306; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; 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: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; PS50889; S4; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 44..147
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 391..452
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 638..712
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 711..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 83089 MW; DE9D3CEA0460B03F CRC64;
MEFNRLLEKA REYHSPEKLA VLEEAYKFAS EKHQGQVRLS GEPFMEHPLQ TAFILAELQL
DTSSLAAALL HDIPEDTGLP IKDIEAKFGP EIAKLVDGTT KLGKVSLTAS GSVPSVTQAE
NLRKMLVAMA EDLRVVFIKL ADRLHNMRTL DALPRDRQLK NAQETLEIYA PLAHRLGIWE
LKWQLEDLSF RYLKPQEYQR IARLVDTRRE QREKFLNRAI RVLKKELDSA GISADIFGRS
KHIYSIYQKM EKYTALGKHF DEIYDLLALR VVVKTMPECY SAVGIIHSIW RPMPDAFDDY
IANPKPNGYQ ALHTAVMCLG TTPLEVQIRT TEMHHIAEYG VAAHWRYKEG GKKDLEFEDR
VGWLRQLVEW HRELAGAEEF LESVKTDIFI DQVFVYTPRG EIKDLPKGST PLDFAYRVHT
DLGHRCIGAK INGKLVSLSY QLKNGDIIEI VSSKAPRGPS LDWLNPNLGF VHTTHARNKI
RQWFNKREKT ESIERGKQIL DKELRRLGIK TDRQAIAELF SYNNLDDFIA AVGNGSITAH
QIVLKLAAQE KESQQVAEPV APAQMAPSAV QVLGVGDLMT SIAQCCHPVP GDKIIGYITR
SRGVTIHRED CHNVINEDEK ERLIPVDWGR SDLLYPVKIQ VDAWDRVGLM RDISTLVAEE
KVNITSMNLT NGNGQRINIF LSLQTKGLAH LSQILKKIDG VKGVLSVSRI GEDASKQSTP
DSPSVPKKAG DVGSSKN
//
