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Database: UniProt
Entry: A0A2A4I548_9SPHN
LinkDB: A0A2A4I548_9SPHN
Original site: A0A2A4I548_9SPHN 
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
//
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