ID   A0A399D3H0_9BACT        Unreviewed;       743 AA.
AC   A0A399D3H0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:RIH66107.1};
GN   ORFNames=D1164_07555 {ECO:0000313|EMBL:RIH66107.1};
OS   Mariniphaga sediminis.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Mariniphaga.
OX   NCBI_TaxID=1628158 {ECO:0000313|EMBL:RIH66107.1, ECO:0000313|Proteomes:UP000266441};
RN   [1] {ECO:0000313|EMBL:RIH66107.1, ECO:0000313|Proteomes:UP000266441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY21 {ECO:0000313|EMBL:RIH66107.1,
RC   ECO:0000313|Proteomes:UP000266441};
RX   PubMed=26012581; DOI=10.1099/ijs.0.000354;
RA   Wang F.Q., Shen Q.Y., Chen G.J., Du Z.J.;
RT   "Mariniphaga sediminis sp. nov., isolated from coastal sediment.";
RL   Int. J. Syst. Evol. Microbiol. 65:2908-2912(2015).
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:RIH66107.1}.
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DR   EMBL; QWET01000004; RIH66107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399D3H0; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000266441; 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; 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; 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; 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; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:RIH66107.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266441}.
FT   DOMAIN          398..459
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   743 AA;  85720 MW;  764D62448CD205F4 CRC64;
     MQHFNKAEIR QIEDRYQDFL KVIIEKFDKE RLSRIEKAFR FANAAHDGIK RKSGEPYIIH
     PIAVARIVAK DLGLGATSIC ASILHDVVED TEYSINDIEN MFGGKVAKIV DGLTKLSGDF
     DSRQALTLKK MLMTLSDDVR VILIKIADRL HNMQTLDSMP PNKKIKIAGE TLYLYVPLAH
     RLGLYAIKSE LEELSFKHKH AEEYNKILLM LHNQEEKRNY LVNEFIRPIK EKLTDEKIDS
     TVTHRLKSSY SIWQKMQKKG VTFNEIYDIL AIRIVIKAKS GISEKRQCFD VLSLVTDIYK
     PRPDRIRDWI TMPKANGYES LHVTVMGPQG KWVEVQIRTE RMDEVAEYGF AAHYRYKDIS
     TFENELETWI ARIREQLRNP DSDAFEFLDD FKLNLYAAEI NLFTPKGDMI SMPQGSTVID
     FAYEIHTDLG NKCIGAKINF KLVPISHELE NGDQVEILTS EKQVPKLEWL KFATTAKARS
     KIKDAFKLEK KKHLEKGKTL VEEALKAVKA PITSNNLKKI IAHFNLNNKE QLYSEAGMGF
     LELINLDEIL GKKSPNKLVK YWNITFSRKK KEGTESQKIE EQAKLPKIDK RKPFLLKEAQ
     DNINYSLAKC CNPIPGDKVI GYLTTDDHVI IHKTGCKEVE KFLSSHGNRI ITAEWTRFKK
     QSYLTRLRLE GFDRIGIVNE VTNVVSKQLS INMRAVKFDT HEGIFEGDLF LYIHNAEDLH
     QLIERLEKIK GIDRVSRDEN LSD
//