ID   A0A2T0SWC8_9BACT        Unreviewed;       758 AA.
AC   A0A2T0SWC8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:PRY37715.1};
GN   ORFNames=CLV58_110185 {ECO:0000313|EMBL:PRY37715.1};
OS   Spirosoma oryzae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1469603 {ECO:0000313|EMBL:PRY37715.1, ECO:0000313|Proteomes:UP000238375};
RN   [1] {ECO:0000313|EMBL:PRY37715.1, ECO:0000313|Proteomes:UP000238375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28354 {ECO:0000313|EMBL:PRY37715.1,
RC   ECO:0000313|Proteomes:UP000238375};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
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}.
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:PRY37715.1}.
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DR   EMBL; PVTE01000010; PRY37715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0SWC8; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000238375; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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   Kinase {ECO:0000313|EMBL:PRY37715.1};
KW   Transferase {ECO:0000313|EMBL:PRY37715.1}.
FT   DOMAIN          419..480
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   758 AA;  86759 MW;  D34CB9AE3C778E99 CRC64;
     MMDTTERRPA PTAEPVIDLE LERQEILKRY RRLLRAAKPM LKGDDAKLIK KAFNTSAEAH
     KNMRRRSGEP YIYHPIAVAQ IAVEEIGLGP TSIVAALLHD VVEDTETTIA DIDRVFGPKV
     ARIIDGLTKI SGYFEYGTSQ QAENFRKMLL TLSDDVRVIL IKLADRLHNM RTLDSMPRDK
     QLKIASETIY IYAPLAHRLG LYAIKSELED LYLKHVEPEA YKDIAKKLRE TKLARDRFIS
     RFIEPIDRDL TETGIKYVIK GRPKSIYSIW NKLDKSKKPF EEIYDLFAVR VILDVPADQE
     KAACWRAYSI VTDHYKPNPD RLKDWISTPR TNGYESLHTT VMSKSGQWVE VQIRTERMNE
     IAEKGYAAHW KYKGNDTQTG AGIETWISQV RDMIESAGSG DKKAAIEFVD DFRSNLYSEE
     VFVFTPKGDL KVLQRGATAL DFAFDIHTQV GAHCMAAKVN NTLVPLSYVL QNGDQVEVIT
     SNRQKPSEDW LRFVVTSKAK TKIKDLIKEE NKRYVTDGRD LVQKKLKVLR LEMTNEVINQ
     MRAYFGSKTT DDFFYRVGKG HIDPQEIRKF KADKEARENR ANKINTDAIQ DGKSFTKELK
     RIHGERADAD MLLIGEDMDR IDYTLSKCCN PISGDDVFGF VTINDGIKIH RVTCPNAVEL
     MSNHGNRIIK AKWTSQKELA FLAGLRITGT DRVGLINDVT RVISNELHIN MRSVAIDSKD
     GIFEGNIRLY VHDTEHLETL MRKLERVQGV YEVIRFDS
//