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Database: UniProt
Entry: M9R2S9_9RHOB
LinkDB: M9R2S9_9RHOB
Original site: M9R2S9_9RHOB 
ID   M9R2S9_9RHOB            Unreviewed;       712 AA.
AC   M9R2S9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE            EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE   AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN   Name=spoT {ECO:0000313|EMBL:AGI66053.1};
GN   ORFNames=OAN307_c02940 {ECO:0000313|EMBL:AGI66053.1};
OS   Octadecabacter antarcticus 307.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI66053.1, ECO:0000313|Proteomes:UP000005307};
RN   [1] {ECO:0000313|EMBL:AGI66053.1, ECO:0000313|Proteomes:UP000005307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=307 {ECO:0000313|EMBL:AGI66053.1,
RC   ECO:0000313|Proteomes:UP000005307};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
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; CP003740; AGI66053.1; -; Genomic_DNA.
DR   RefSeq; WP_015498111.1; NC_020911.1.
DR   AlphaFoldDB; M9R2S9; -.
DR   STRING; 391626.OAN307_c02940; -.
DR   KEGG; oat:OAN307_c02940; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_5; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000005307; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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:SF36; 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; 2.
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:AGI66053.1}.
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          382..447
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          627..704
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   712 AA;  80434 MW;  3E019196357E3595 CRC64;
     MITSDDLIAL VCTYNPKTNA KLIADAFVFS AEMHEGQFRH SGEPYFTHPF AVAGILAEQQ
     MDDATLITAL LHDTIEDTKA TYGEVEKRFG REIAELVDGV TKLTNLQLSS HETKQAENFR
     KLFMATSRDL RVTLVKLADR LHNMRTIKSM RDDKQAQKAR ETMDIYAPLA GRMGMQWMRE
     ELEDLAFRVL NPEGRNSIIR RFITLQRETG DVIEKIQVDM EHEMDKAGLA VDIYGRAKKP
     YSIWRKMQEK EQGFSRLSDI YGFRVITQTE ADCYAALGAI HQRWAAVPGR FKDYISQAKT
     NGYRSLHTTV SGRDGKRVEV QIRTVEMHEV AEAGVAAHWS YRDGIRTENR FAVDPARWIA
     QLTERLDDDH DHDEFLDMVK LEMYQDQVFC FTPKGDVIKL PRGATPIDFA YAIHTRIGHA
     CVGAKIDGMR VPLWTRVKNG QSVDVITAEG QTPQATWIDI AVTGRAKTAI RKALRGEDRE
     RFIRLGRELV RVAFENIDKK ATDKAVRTAA KSLGLGNLDD LLERVGSAEI TSREVVSAIH
     PELAKSVGNE IEARRAVVGL EADQSHRRAQ CCQPIPGERI VGITYRGQGV VVHTIDCRVL
     VDYEDQPDRW IDLNWQEGTH SATNTITLEM TITNDAGVLG RICTLIGEKG ANISDLVFID
     RKPDYFRLLI EVDLRDVEHM HIIMTALEAD SNVNAIARHR DPGRAGQIER QG
//
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