ID K9PIE7_9CYAN Unreviewed; 756 AA.
AC K9PIE7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:AFY32716.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:AFY32716.1};
GN ORFNames=Cal7507_2281 {ECO:0000313|EMBL:AFY32716.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY32716.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY32716.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY32716.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) 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; CP003943; AFY32716.1; -; Genomic_DNA.
DR RefSeq; WP_015128530.1; NC_019682.1.
DR AlphaFoldDB; K9PIE7; -.
DR STRING; 99598.Cal7507_2281; -.
DR KEGG; calo:Cal7507_2281; -.
DR PATRIC; fig|99598.3.peg.2552; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_3; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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:UP000010390};
KW Transferase {ECO:0000313|EMBL:AFY32716.1}.
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 679..753
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 756 AA; 85559 MW; A26283B8007572C7 CRC64;
MSSTVINSSI DVPLPEWLQK CLSESSRGGS QAEDDRRHSD AVLIGEAFKF AYRLHQGQYR
KSGEPYICHP VAVAGLLRDL GGSAAMIAAG FLHDVVEDTD VTIEQIGELF GPEVRQLVEG
VTKLSKINFK SKTESQAENF RRMFLSMAQD IRVIVVKLAD RLHNMRTLQV MPDDKRRRIA
QETRDIFAPL ANRLGIWHFK WELEDLSFKY LEPESFREIQ QHVAEKRTSR EEKLARATTI
LQERLKQAGI ECLDVSGRPK HLYSIYQKMQ RQQKEFHEIY DLAALRIIVR TNEECYRALA
VVHDAFRPIP GRFKDYIGLP KPNRYQSLHT GVIGLTGRPL EVQIRTQEMH HIAEYGIAAH
WKYKETGGSN VSNLTTSDEK FTWLRQLLEW QSDLKDAQEY LDSVKDNLFE DDVYVFTPKG
DVVPLSPGAT TIDFAYRIHT EVGNHCAGAR VNGRMVPLST RLQNGDIVVI MTQKNSHPSL
DWLNFVRTSA AKYRIKQWYK RSRREENVAR GRELLEKELG KTGFDSLLKS DAMHSVSEKC
NYHSTEDLLA GLGYGEITLN LVLNRWREVV KAHQPIVNAP LVPTKESAAA TKALRDGPAT
SRTTDSPILG VEGLVYHLAG CCTPIPGEPI IGVVTRGRGI SIHRQGCNNL DSVEYERLVP
VRWNSGAETS SIPQTYPVNL QIEALDRVGV LKDILSRLSD QGINVRHAQV KTAIGQPALI
DLGIDIRDRP QLEHVFVQIK KMSDILNIRR VGQIDE
//
