ID K1JP27_9BURK Unreviewed; 703 AA.
AC K1JP27;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EKB31986.1};
GN ORFNames=HMPREF9465_00380 {ECO:0000313|EMBL:EKB31986.1};
OS Sutterella wadsworthensis 2_1_59BFAA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=742823 {ECO:0000313|EMBL:EKB31986.1, ECO:0000313|Proteomes:UP000005835};
RN [1] {ECO:0000313|EMBL:EKB31986.1, ECO:0000313|Proteomes:UP000005835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_59BFAA {ECO:0000313|EMBL:EKB31986.1,
RC ECO:0000313|Proteomes:UP000005835};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Sutterella wadsworthensis 2_1_59BFAA.";
RL Submitted (MAY-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}.
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:EKB31986.1}.
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DR EMBL; ADMG01000013; EKB31986.1; -; Genomic_DNA.
DR RefSeq; WP_005433584.1; NZ_JH815513.1.
DR AlphaFoldDB; K1JP27; -.
DR STRING; 742823.HMPREF9465_00380; -.
DR PATRIC; fig|742823.3.peg.374; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_4; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000005835; Unassembled WGS sequence.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 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; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
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; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005835}.
FT DOMAIN 380..441
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 632..703
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 703 AA; 78863 MW; D64F1C8A88B383FD CRC64;
MSETPALVVD VSLARSMVEP LYRDLTLPTG ENVMQHADGI ASILREVRDD PELISAAYLF
CVPSVIQNSG EWIEKSFGPA VNGLVQELGQ VNELSRRARS ENEEANTRHQ VEAMRRMFLS
MCKDLRVVLL KLASRLQTLR WFAASKREGA EKFGTETLDL YAPLANRLGI WQLKWELEDL
SLRFTRPSEY REIAQQLDES REQRIEFMQS AVLRIRGLLE ENGIKAEVSG RPKHIYSIWK
KMQRKHLRFD QLFDVRAVRI IVDTVERCYQ VLSIVHENFP VISKEYDDYI AKPKPNGYQS
LHTVVTDKAG RPLEIQIRTR AMHEFAELGV AAHWRYKEAG NSNGATSAEE QRVAWLRQLL
AWGSDMQNQG QPEGEAVLDD HIYALTPQGR VVELPRGGTP VDFAYAVHTQ LGHRTKGAKV
DGVLVPLNTK LETGQTVEII AAKVGQPSRD WLSAEKGFAA SPRTRNKVRQ WFNAQQTAEL
TAQGREKIDK ELARLGKTAV KLEDLAKRLG YEGVDELCLA YGKEEITQTA LATAVQPPKP
AAPEPDEVLI RQSRNTGKSD VLVVGVDSLL TQLARCCHPV PPDEIVGYVT RGRGVTIHRA
DCPNIRNMSE QDHGRLIEVS WGRGGDGVFP AEVFVVATDR PGLIRDISEI FMKAKQNLVG
MNSQKVKTDV HMRFTVEIPS ASSLTSTLTT IRELKGVLSA RRC
//
