ID A0A2A4I548_9SPHN Unreviewed; 715 AA.
AC A0A2A4I548;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN ORFNames=COA07_14095 {ECO:0000313|EMBL:PCG13629.1};
OS Sphingomonas adhaesiva.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=28212 {ECO:0000313|EMBL:PCG13629.1, ECO:0000313|Proteomes:UP000218323};
RN [1] {ECO:0000313|EMBL:PCG13629.1, ECO:0000313|Proteomes:UP000218323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7418 {ECO:0000313|EMBL:PCG13629.1,
RC ECO:0000313|Proteomes:UP000218323};
RA Feng G., Zhu H.;
RT "Sphingomonas adhaesiva DSM 7418, whole genome shotgun sequence.";
RL Submitted (SEP-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:PCG13629.1}.
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DR EMBL; NWVC01000007; PCG13629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4I548; -.
DR Proteomes; UP000218323; 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; 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:SF36; 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:PCG13629.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218323}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 398..459
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 643..715
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 715 AA; 79354 MW; 0FC16169EAEFE160 CRC64;
MLRQYELVDR VLDYDPDADE AMLNRAYVFS VNAHGTQKRA SGDPYFSHPI EVAGILTELH
LDDETIATAI LHDTVEDTVA TPEEIERIFG ANVARLVDGV TKLSKIEAQT ENERAAENLR
KFLLAMSGDI RVLLVKLADR LHNMRTLHYI PKPEKRRRIA RETMDIYAPL AERIGMYEFM
KEMQTLAFQQ LEPEAYESIT RRLEQLKDGS DGDRIAKIGS GLKLLLARAG VDAEVSGREK
HPYSIWRKMQ ERHISFEQLS DIMAFRAIVP TVEDCYRALG VIHRRWPMVP GRFKDYISTP
KRNGYRSLHT SVIHAENRRI EIQLRTPEMH AEAEFGLAAH WAYKQSVPAT GGATRRTAQA
AAQPGAQAGW IADLVEILDT AATPEELLEH TRIAMYQDRI FAFTPKGELI QLPKGATPID
FAYAVHTDLG NQAVGAKING RVVPLSTVIE NGDQVQVLRS KAQVPQPAWL NLAITAKALA
AIRRHLRNEE RDQSVALGRK LYDDIVQRLP ATLAANALDE ALKRLKLPDE AALMQAIARR
TLGDAQVMEA LMPGSAGADL ADAPPQSSAI SIQGLAPGVA YELAECCHPV PGDRIVGLRR
PDASIEVHAI DCPVLAALAE RSEEETDWID VQWGNKTEGA VARISVEVRN EPGALGMLAT
VIGQHKANII NLRLDNRDTQ FHTNTIDVEV HDAHQLMRLL AALRAAEAVN AAERI
//