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
//