ID A0A1I0Y2Q0_9RHOB Unreviewed; 723 AA.
AC A0A1I0Y2Q0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05421688_2770 {ECO:0000313|EMBL:SFB07639.1};
OS Poseidonocella pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871651 {ECO:0000313|EMBL:SFB07639.1, ECO:0000313|Proteomes:UP000198796};
RN [1] {ECO:0000313|EMBL:SFB07639.1, ECO:0000313|Proteomes:UP000198796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29316 {ECO:0000313|EMBL:SFB07639.1,
RC ECO:0000313|Proteomes:UP000198796};
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; FOJU01000004; SFB07639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0Y2Q0; -.
DR STRING; 871651.SAMN05421688_2770; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000198796; 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; 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:SFB07639.1};
KW Kinase {ECO:0000313|EMBL:SFB07639.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198796};
KW Transferase {ECO:0000313|EMBL:SFB07639.1}.
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"
FT REGION 693..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 81649 MW; 104E10B1A5F3E818 CRC64;
MISDDDLIAL VHNYNPRADE QLIRRAYEFG ERMHDGQFRQ SGEPYFSHPV AVAAILTEQQ
LDDATIVTAL LHDTIEDTKA SYSEVSRQFG REVADLVDGV TKLTNLQLSS SETKQAENFR
KLFMAMSKDL RVILVKLGDR LHNMRTIKSM RHEKQVQKAR ETMDIYAPLA GRMGMQWMRE
ELEDLAFRVL NADARSSIIR RFITLQRETG DVIQRITGDM RKELEAAGIE AQVFGRAKKP
YSIWRKMREK DVGFSRLSDI YGFRVITETD AECYAALGVI HQRWRAVPGR FKDYISQPKS
NGYRSIHTSV SGRDGKRVEV QIRTAQMHDV AETGVAAHWS YRDGVRSENP FAVDPAKWLA
SLTERFSEDE DHEDFLEAVK LEMYSDQRFC FTPKGDVIKL PRGATPIDFA YAIHTRIGNA
CVGAKVDGMR VPLWTRLKNG QSVEIITAEG QTPQATWLDI VATGRAKSAI RRALRAEDRE
RFMKLGRELA RVAFEHIGKK ATDKALSTAA KLLRVEDRYD LLARLGSAEI TGREVVRALY
PDLSPQPEHE VDFRRAVIGL SPGQNFDRAP CCQPVPGERI VGITTRGRGV VVHAIDCEAL
TSLEDQPDRW LDLHWDSGQH APVHNVSLDI TIANDAGVLG HICTMIGEQK ANISDLHFVD
RKPDYYRLLI DVDLCDAEHL HRVLTALEAE SEVASLERHR DPSRGQHSAP VAGRDMSETT
QEG
//
