ID C1DC36_LARHH Unreviewed; 724 AA.
AC C1DC36;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=SpoT {ECO:0000313|EMBL:ACO73453.1};
DE EC=3.1.7.2 {ECO:0000313|EMBL:ACO73453.1};
GN Name=spoT {ECO:0000313|EMBL:ACO73453.1};
GN OrderedLocusNames=LHK_00458 {ECO:0000313|EMBL:ACO73453.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO73453.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO73453.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO73453.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO73453.1; -; Genomic_DNA.
DR RefSeq; WP_012695945.1; NC_012559.1.
DR AlphaFoldDB; C1DC36; -.
DR STRING; 557598.LHK_00458; -.
DR KEGG; lhk:LHK_00458; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_4; -.
DR Proteomes; UP000002010; Chromosome.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
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; 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 Hydrolase {ECO:0000313|EMBL:ACO73453.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002010}.
FT DOMAIN 61..160
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 645..720
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 724 AA; 80281 MW; D50020CE77343170 CRC64;
MDHASVPPAV DYDAMVEGQA EELLRTVATY LKPDDLPFVR AAFEFARDAH AGQTRKSGEP
YITHPLSVAQ ILTEWKLDAH GLAAALLHDT MEDTGVAKST LAEKFGKQVA ELVDGLSKLE
RLEYQSKEAR QAENFRKMVL AMARDIRVII IKLADRLHNM RTLDSMREEK RRRIALETLD
VYTPLANRIG LNKVYRELED LCFKYLYPNR YSVLAKAVRA ARGNRRELVG KILTAIARKL
VEANIEAGIR GREKNLYSIY RKMQEKQLSF SEVLDIYAFR VIVNDIPSCY LALGALHSLY
KPIPGKFKDY IAIPKSNGYQ SLHTTLFGPY GTPIEVQIRT RDMHRVAESG VASHWMYKSG
DASLDMARQR THQWLQDILD IQAETGDAVE FFEHIKIDLF PDEVYVFTPK GKIMVLPQGA
TPVDFAYVVH TDIGHRCIAA KVNHALAPLR TQLKNGDTVE IITAAHARPN PSWLNFVVSG
RARSAIRSSL KTLHHEEARS LGDRLLKQSI HSLTTQPFVV SDGVWMAYLK ETGDRHGSAG
EVLASIGAGK QQAMAVAARL LELSGTVLGE PARTGPLVIR GNEGSSIQYA SCCTPLPGDP
VVAVLTKGQG IVLHRKDCAN AKRAEADRQL EAEWDIKSPR SFSVPVAVMT RDERGALAGI
ALGISEAGAN IESVMQDATN GEGFVQIRFR LQVESVAHLE RVLARIEAEP CVERATRGWQ
VAGG
//
