ID A0A1H8IYQ1_9RHOB Unreviewed; 705 AA.
AC A0A1H8IYQ1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN ORFNames=SAMN05216227_102253 {ECO:0000313|EMBL:SEN73714.1};
OS Pseudorhodobacter antarcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudorhodobacter.
OX NCBI_TaxID=1077947 {ECO:0000313|EMBL:SEN73714.1, ECO:0000313|Proteomes:UP000183002};
RN [1] {ECO:0000313|EMBL:SEN73714.1, ECO:0000313|Proteomes:UP000183002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10836 {ECO:0000313|EMBL:SEN73714.1,
RC ECO:0000313|Proteomes:UP000183002};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOCO01000022; SEN73714.1; -; Genomic_DNA.
DR RefSeq; WP_050519802.1; NZ_LGHU01000067.1.
DR AlphaFoldDB; A0A1H8IYQ1; -.
DR STRING; 1077947.SAMN05216227_102253; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000183002; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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:SEN73714.1};
KW Kinase {ECO:0000313|EMBL:SEN73714.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183002};
KW Transferase {ECO:0000313|EMBL:SEN73714.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 381..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 626..700
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 705 AA; 79722 MW; A574D39A226D899B CRC64;
MIDVEDLVAL VHNYNPRSNA DLIRAAYAYG LRVHDGQMRH SGEPYFTHPV AVAAILTEQR
LDDATIITAL LHDTIEDTKA TYTDVAAQFG DEVAELVDGV TKLTNLQLSS TQSKQAENFR
KLFMAMSKDL RVILVKLADR LHNMRTIKSM RPEKQAQKAR ETMEIFAPLA GRMGMQWMRE
ELEDLAFRVI NPDARNSIIR RFITLQREAG DVVYKITADI RTELDRADID ADVYGRAKKP
YSVWRKMQEK DLSFSRLSDI YGFRIITRSE ADCYRVLGVI HQRWRAVPGR FKDYISQPKN
NGYRSIHTTV SGRDGKRVEV QIRTRQMHEV AEAGVAAHWS YREGVRANNP FAVDPAKWVA
KLTENMEEDD HDTFLENVKL EMYTDQVFCF TPKGDVVQLP RGATPLDYAY SIHTRIGNST
VSAKIDGIRV PLWTRLKNGQ SVEIITAEGQ RPQSSWIEIV TTGRAKAAIR RSLREEDKGR
FVKLGRELAR AAFDNVGRKA TDKALRTAAR MLALTDETDL LARIGSAELT ARRVLETLYP
ELVQASGDTV DARRPVIGLG DDQIFQRAGC CQPVPGERIV GISYRGQGVV VHAIDCPALA
EMEDQPERWV DLNWQSGRHA AVNTVSLDLT ISNDAGVLGR ICTLIGQQKA NISDLQFVDR
KPDFYRLLID VDLRDVEHLH MIMTALEAET DVAEVGRHRD TRRKP
//
