ID A0A2N4YL27_9RHOB Unreviewed; 705 AA.
AC A0A2N4YL27;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=C0V75_01855 {ECO:0000313|EMBL:PLL14214.1};
OS Tabrizicola sp. TH137.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tabrizicola.
OX NCBI_TaxID=2067452 {ECO:0000313|EMBL:PLL14214.1, ECO:0000313|Proteomes:UP000234539};
RN [1] {ECO:0000313|EMBL:PLL14214.1, ECO:0000313|Proteomes:UP000234539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH137 {ECO:0000313|EMBL:PLL14214.1,
RC ECO:0000313|Proteomes:UP000234539};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) 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:PLL14214.1}.
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DR EMBL; PKRQ01000001; PLL14214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4YL27; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000234539; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase 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; 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:PLL14214.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000234539}.
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; 79948 MW; B015DBC8AA4CF0A7 CRC64;
MIDVEDLIAL VRNYNPRTNA DLIRKAYAYG KQMHDGQFRK SGEPYFTHPV AVAAILTEQR
LDDATIITAL LHDTIEDTRS TYSDITQMFG TEVAELVDGV TKLTNLQLSS AQSQQAENFR
KLFMAMSKDL RVILVKLADR LHNMRTIKSM KPEKQAQKAR ETMEIFAPLA GRMGMQWMRE
ELEDLAFRVL NPEARNSIIR RFITLQREAG DVVHKITADI RNELEKVQIE ADVYGRAKKP
YSIWRKMQEK DLAFSRLSDI YGFRVICGSV ADCYRILGVI HQRWRAVPGR FKDYISQPKS
NGYRSIHTTV SGRDGKRVEV QIRTREMHEV AEAGVAAHWS YREGVRAQNP FAVDPAKWIA
SLTERFDAED HDEFLEHVKM EMYSDQVFCF TPKGDVVQLP RGATPLDYAY AIHTRIGNSC
VSAKVDGIRV PLWTRLKNGQ SVEIITAEGQ RPQASWIDIV TTGRAKAAIR KSLREEDRGR
FVKLGQELAR AAFDHVGKKA TDKALRTAAK MLGLSDETDL LARLGSAEIT ARRVIETLYP
ELARAQDDEV DASRPVVGLS DDQSFRRAPC CQPVPGERIV GITYRGQGVV VHAIDCPALE
EFEEQPGRWV DLHWHSGRHA AVHTVSLEIT ISNDAGVLGR ICTLIGEQKA NISDLRFTDR
KPDYYRLIVD VDLRDVEHLH MVMTALEAET DVAQISRHRD MTRKP
//
