ID H0UMM4_9BACT Unreviewed; 762 AA.
AC H0UMM4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=(P)ppGpp synthetase, RelA/SpoT family {ECO:0000313|EMBL:EHM13727.1};
GN ORFNames=JonanDRAFT_1363 {ECO:0000313|EMBL:EHM13727.1};
OS Jonquetella anthropi DSM 22815.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Jonquetella.
OX NCBI_TaxID=885272 {ECO:0000313|EMBL:EHM13727.1, ECO:0000313|Proteomes:UP000003806};
RN [1] {ECO:0000313|EMBL:EHM13727.1, ECO:0000313|Proteomes:UP000003806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22815 {ECO:0000313|EMBL:EHM13727.1,
RC ECO:0000313|Proteomes:UP000003806};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The Noncontiguous Finished genome of Jonquetella anthropi DSM 22815.";
RL Submitted (NOV-2011) 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; CM001376; EHM13727.1; -; Genomic_DNA.
DR RefSeq; WP_008523296.1; NZ_CM001376.1.
DR AlphaFoldDB; H0UMM4; -.
DR STRING; 885272.JonanDRAFT_1363; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_0; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000003806; 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:UP000003806}.
FT DOMAIN 89..188
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 426..489
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 688..762
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 595..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 85733 MW; 117D0A0C0FA34E64 CRC64;
MTVTQETTGT PVPQEMTAAG KRELNSLRDS YIGRLPATQS SATVTYAWRE LWSKISRYLN
RDELKGVGEA FVFAAGAHGE QMRMGGEPYI IHPVFAASIL ADMKLDVATL QAALLHDVLE
DTECTAEQMR ERFGEVVTTL VDGVTKLGKL PFKTFEDYQA ENLRKMFLVM AKDIRVVLIK
LADRTHNMRS LGAMRRDKQI RTAKETLEIY APLAHRLGIY QMKRTLEDLA FKYYDPEMYY
EIKSKVKKRL PEREAVVEQA LEILQARLDE MGIKNSIKGR AKHFYSIYEK MNRKKLSIDQ
LYDLLALRVI VEDVAQCYSV LGVVHTIWKP IPGQFDDYIA NPKNNMYQSL HTTVLGPSGE
PLEVQIRTWA MHWRAEYGVA AHWRYKEGDS HVDDLDSKLE WIRRALEGSD ETNSEEFMER
LKDDVLTSDV FVFTPEGDVK NLPRGSTVVD FAFSVHTQVG EQYVGAMVNN RIVPADYELH
NGDIVKIMTS SSAKPSRDWL RFVKSSKAKS KIRAYFKRLD SLAREDDVSR GKELLERELR
ARLGDAFTSL EALSTSMNRV ARDLGLSNYD DLYFALGSGK LNTSQTAGRI AEAANHSEAE
EQPSATEGPH KLRNKSDSDI VVGGTGGIQI SLAQCCCPVP GDDIVGFVTK IRGIMVHRSD
CERIADVVDE RRVRVAWGDT SRKQYQAQIV IDAVDRSGLF ADVARVCANS EANINSVRAT
QIGVAAGHAR MKMEVMVRDV EHLYSLIAKL GGVRNVIDVK RG
//
