ID A0A2S6NJ00_RHOGL Unreviewed; 729 AA.
AC A0A2S6NJ00;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CCS01_10430 {ECO:0000313|EMBL:PPQ34539.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ34539.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ34539.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ34539.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
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:PPQ34539.1}.
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DR EMBL; NHRY01000105; PPQ34539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NJ00; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000239724; 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; 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; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 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:PPQ34539.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239724}.
FT DOMAIN 44..143
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 389..450
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 654..728
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 729 AA; 81030 MW; 1140FFD84839286D CRC64;
MPQCELTSKI LDYDPKAETG LIDSAYELAQ QAHSTQRRDN GEPYFTHPVA VANILAGYRL
DVSSIATALL HDVVEDTPVK LTEIETRFGK EIAGLVDGVT KLTRLELQSD RTKQAENFRK
LVLAMSRDIR VLLVKLADRL HNMRTLHFVR EPDRRKRIAR ETMEIYAPLA ERIGMDAVKT
ELQTLSFTQL EPEAYATIQA RLNFLRGQGA DVIDDVRREL IEVCREGGVE VISVTGREKS
PYSIWEKMHR RNVAFEQLSD IMAFRIVVAT KADCYAALGA VHSAYPVIAG RFKDYISTPK
SNGYQSLHTG VTLRQPRNQK IEVQIRTEEM NDVAENGVAS HWIYKAPEKK VDGSDVQRFR
WVQDLLEILD DSAAPDEFLE NTKLELYADQ VFCFTPKGQL IQLPRGATPV DFGYAVHSQV
GDTCVGAKVN GRLMPLRHHL ENGDQVEIMT ARGGTPSPQW DRFVVTGKAR ARIRRFIHQE
QRQRSRDAGR VELTRAFRQA GVDGSEKSLE PALKALKVAT VDDLYIAVGN SNIGPKDVVH
AAYPELRQTP RAPRMVPQML PRTGKPPTRH DHDMPVTGLV PGMAYSFAGC CHPVPGDEIV
GIVTTGKGIT IHSRDCQTLA AFAATPERFM DVDWNYESVG KTSANGKGSG HTARISVIAA
NEQSALADLA NAIAKQEGAV NNLKIVNRQQ DFMEILVDVD VRDLQHLSKV IVGLRGLKLV
KGVERATGG
//
