ID   A0A2S0MR78_9RHOB        Unreviewed;       723 AA.
AC   A0A2S0MR78;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=C6Y53_12340 {ECO:0000313|EMBL:AVO38399.1};
OS   Pukyongiella litopenaei.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pukyongiella.
OX   NCBI_TaxID=2605946 {ECO:0000313|EMBL:AVO38399.1, ECO:0000313|Proteomes:UP000237655};
RN   [1] {ECO:0000313|Proteomes:UP000237655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-1 {ECO:0000313|Proteomes:UP000237655};
RA   Kim Y.-S., Kim S.-E., Kim K.-H.;
RT   "Genomic analysis of the strain SH-1 isolated from shrimp intestine.";
RL   Submitted (MAR-2018) 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; CP027665; AVO38399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0MR78; -.
DR   KEGG; thas:C6Y53_12340; -.
DR   Proteomes; UP000237655; Chromosome.
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; 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:AVO38399.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237655}.
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          386..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   723 AA;  81593 MW;  950F3F0CACE3AAC1 CRC64;
     MISADDLIAL VRNYNPKTNE DRIRAAYYYG REMHDGQFRH SGEPYFSHPV AVAAILTEQH
     LDDDTIITAL LHDTIEDTQA SYGEVASRFG EEVAALVNGV TKLTNLQINS NETKQAENFR
     KLFMAMSKDL RVILVKLADR LHNMRTIKSM RPEKQVQKAR ETMDIYAPLA GRMGMQWMRD
     ELEDLCFRVL NPEGRASIMR RFITLQRESG DVIQRITGDM RFELAEAEIE AEVFGRAKKP
     YSIWRKMQEK DQGFSRLSDI YGFRIITGSE EDCYRALGAI HQRWRAVPGR FKDYISQPKS
     NGYRSIHTTV SGRDGKRVEV QIRTQQMHEV AETGVAAHWS YKDGERAENP FAVDPAKWLS
     TVSEQFDAEE DHQDFLENLR LELYADQVFC FTPKGDVVKL PRGATPIDFA YAIHTRIGHA
     CVGAKVDTIR VPLWTRLKNG QSVEVITAEG QTPQASWLEI AVTGKARAAI RRALREMDRE
     RFVKLGRELA RSAFEHVDRK ATDKVLDTAA KHLRLSDSKE LLARLGSAEL TAHDVVQAVY
     PDLARDEGDQ IPARRAVVGL EPGQSFERGT CCQPLPGERI VGITYRGKGV VVHAIDCDRL
     SEYENQPDRW VDLHWHAGTH PAVYGTTLDV TIGNDAGVLG RICTLIGEKK ANISNLEFVD
     RKPDYFRLMI NVELRDAEQL HSLMLALEAE SDVASIDRYR ETGGRDLAGL ATADEGQAPV
     AQP
//