ID D1AEV7_THECD Unreviewed; 807 AA.
AC D1AEV7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACY97682.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ACY97682.1};
GN OrderedLocusNames=Tcur_2116 {ECO:0000313|EMBL:ACY97682.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY97682.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY97682.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; CP001738; ACY97682.1; -; Genomic_DNA.
DR AlphaFoldDB; D1AEV7; -.
DR STRING; 471852.Tcur_2116; -.
DR KEGG; tcu:Tcur_2116; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000001918; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW Transferase {ECO:0000313|EMBL:ACY97682.1}.
FT DOMAIN 127..224
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 462..525
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 729..803
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 89821 MW; AAFB6B9C20C0130B CRC64;
MPGEVVSTDA VAKAPHGGGP AEPTAKSDPA RPQEAPDRSG RPPAAPSSAA APQQVAPSAA
PPSAARVRRR LARLGAQRGT TMNPVLEPLI RTVRNTHPKA DIRLIERAYE VAAYYHRDQK
RKSGDPYITH PLAVTTILAE LGMNTETLCA ALLHDTIEDT EYTLEELREE FGEEIASLVD
GVTKLDKVKY GDAAEAETVR KMVVAMARDI RVLVIKLADR LHNMRTLRYM PRHKQEKKAR
ETLEVFAPLA HRLGMNTLKW ELEDLAFATL YPKRFDEIAR LVSERAPRRD VYLTEVIDKV
SADLREAKIK ATVTGRPKHY YSIYQKMIAR NVGFDEIYDL VGIRVLVDTV RDCYATLGTI
HARWNPVPGR FKDYIAMPKF NMYQSLHTTV IGPEGKPVEL QIRTWGMHRR AEYGVAAHWK
YKEETVGGRK AADMQWLKQL LDWQKETADP AEFLEGLRFD LSVSEVFVFT PKGDVIALPQ
GATPVDFAYA IHTEVGHRCI GARVNGRLVP LESTLDNGDL VEVFTSKSPD AGPSRDWLNF
VKSARARNKI KHWFTKERRD TAIEAGKESI ARAMRKQNMP LQRMMSGEAL LALARDMRYP
DVSALYAAVG EGHVSAQAVV QRLVEALGGV ESAEEDMAEV AVPTRRRRRS RPAGDPGVVV
AGGDPDVWVR LSRCCTPVPG DEIVGFVTRG HGVSVHRTDC GNVANLRNQP DRLIDVKWSP
SEDSVFLVSI QMEALDRPRL LSDVTRVLSD QHVNILSASV TTTRDRVAVS RFTFEMGDPK
HLGHVLKAVR SVDGVYDVYR VTSGGGR
//
