ID A0A0C1GHM5_9RHOB Unreviewed; 710 AA.
AC A0A0C1GHM5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=RA28_20245 {ECO:0000313|EMBL:KIC41726.1};
OS Ruegeria sp. ANG-S4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC41726.1, ECO:0000313|Proteomes:UP000031326};
RN [1] {ECO:0000313|Proteomes:UP000031326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC41726.1}.
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DR EMBL; JWLK01000007; KIC41726.1; -; Genomic_DNA.
DR RefSeq; WP_039532766.1; NZ_JWLK01000007.1.
DR AlphaFoldDB; A0A0C1GHM5; -.
DR STRING; 1577904.RA28_20245; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000031326; Unassembled WGS sequence.
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 Kinase {ECO:0000313|EMBL:KIC41726.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031326};
KW Transferase {ECO:0000313|EMBL:KIC41726.1}.
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..701
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 710 AA; 80622 MW; 01C3A62F5EFF82A8 CRC64;
MISAEDLIAL VRNYNPKTNA ERIERAYEFG QQMHEGQFRH SGEPYFSHPV AVAAILTEQR
LDDATIITAL LHDTIEDTKA NYGRVSELFG DEVAKLVDGV TKLTNLQLSS RETKQAENFR
KLFMAMSKDL RVILVKLADR LHNMRTIKAM RPEKQVQKAR ETMDIYAPLA GRMGMQWMRE
ELEDLAFRVL NPEGRQSIIR RFITLQRETG DVIHRITGDM RHELEKAGIE AEVFGRAKKP
YSIWRKMQEK DQGFSRLSDI YGFRIITQTE EDCYRTLGAI HQRWRAVPGR FKDYISQPKS
NGYRSIHTTV SGRDGKRVEV QIRTRQMHDV AETGVAAHWS YRDGVRSENP FAVDPAKWIS
NLTEQFDSED DHEDFLEAVK LEMYSDQVFC FTPKGDVVKL PRGATPIDFA YAIHTRIGHA
CVGAKVDGIR VPLWTRLKNG QSVDVITADG QTPQVTWLEI AVTGKARTAI RRALREVDRE
RFIKLGKELA RAGFENIGRK ATDKALDTAA KHLRLKDRHE LLARLGSAEL TAHDVVEAVY
PELAKDEGDA IPMRRAVIGL EPGQKFDRAP CCQPLPGERI VGITYRGKGV VVHAIDCDRL
SEFENEPERW VDLHWHSGTH PAVYGATLDL TIGNDAGVLG RICTLIGEKK ANISNLVFID
RKPDFYRLQI SVELRDLEQL HSLMLMLEAE SDVAAVERYR DRAKTTVAAS
//
